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class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/4609493/Mitochondrial_potassium_transport_the_role_of_the_mitochondrial_ATP_sensitive_K_channel_in_cardiac_function_and_cardioprotection">Mitochondrial potassium transport: the role of the mitochondrial ATP-sensitive K + channel in cardiac function and cardioprotection</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Coronary artery disease and its sequelae-ischemia, myocardial infarction, and heart failure-are leading causes of morbidity and mortality in man. Considerable effort has been devoted toward improving functional recovery and reducing the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_4609493" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Coronary artery disease and its sequelae-ischemia, myocardial infarction, and heart failure-are leading causes of morbidity and mortality in man. Considerable effort has been devoted toward improving functional recovery and reducing the extent of infarction after ischemic episodes. As a step in this direction, it was found that the heart was significantly protected against ischemia -reperfusion injury if it was first preconditioned by brief ischemia or by administering a potassium channel opener. Both of these preconditioning strategies were found to require opening of a K ATP channel, and in 1997 we showed that this pivotal role was mediated by the mitochondrial ATP-sensitive K + channel (mitoK ATP ). This paper will review the evidence showing that opening mitoK ATP is cardioprotective against ischemiareperfusion injury and, moreover, that mitoK ATP plays this role during all three phases of the natural history of ischemia -reperfusion injury preconditioning, ischemia, and reperfusion. We discuss two distinct mechanisms by which mitoK ATP opening protects the heart-increased mitochondrial production of reactive oxygen species (ROS) during the preconditioning phase and regulation of intermembrane space (IMS) volume during the ischemic and reperfusion phases. It is likely that cardioprotection by ischemic preconditioning (IPC) and K ATP channel openers (KCOs) arises from utilization of normal physiological processes. Accordingly, we summarize the results of new studies that focus on the role of mitoK ATP in normal cardiomyocyte physiology. Here, we observe the same two mechanisms at work. In low-energy states, mitoK ATP opening triggers increased mitochondrial ROS production, thereby amplifying a cell signaling pathway leading to gene transcription and cell growth. In high-energy states, mitoK ATP opening prevents the matrix contraction that would otherwise occur during high rates of electron transport. MitoK ATP -mediated volume regulation, in turn, prevents disruption of the structure -function of the IMS and facilitates efficient energy transfers between mitochondria and myofibrillar ATPases. 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We discuss two distinct mechanisms by which mitoK ATP opening protects the heart-increased mitochondrial production of reactive oxygen species (ROS) during the preconditioning phase and regulation of intermembrane space (IMS) volume during the ischemic and reperfusion phases. It is likely that cardioprotection by ischemic preconditioning (IPC) and K ATP channel openers (KCOs) arises from utilization of normal physiological processes. Accordingly, we summarize the results of new studies that focus on the role of mitoK ATP in normal cardiomyocyte physiology. Here, we observe the same two mechanisms at work. In low-energy states, mitoK ATP opening triggers increased mitochondrial ROS production, thereby amplifying a cell signaling pathway leading to gene transcription and cell growth. In high-energy states, mitoK ATP opening prevents the matrix contraction that would otherwise occur during high rates of electron transport. 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(2) The roles of the classical and gated bilirubin (UCB) chemistry and physical chemistry; newer molecular... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_57724175" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">three strains of mutant rats with congenital conjugated The workshop covered three major areas: Unconjuhyperbilirubinemia. (2) The roles of the classical and gated bilirubin (UCB) chemistry and physical chemistry; newer molecular biological approaches to identification UCB transport and intracellular trafficking; and evaluaof these transporters were contrasted, and their limitation and therapy of neonatal and congenital hyperbilitions were discussed. (3) The relative roles of the multirubinemias. Findings of studies in the chemistry and ple carriers in UCB transport under different conditions physical chemistry area were as follows. (1) Nuclear and substrate concentrations were discussed. (4) Cytomagnetic resonance (NMR) studies of highly enriched solic UCB-binding proteins (e.g., ligandin) were shown 13 COOH mesobilirubin in water-dimethyl sulfoxide systo promote transcellular movement of UCB by solubiliztems indicated that the pK a values of the carboxyl ing and transporting the pigment in the aqueous phase groups are 4.2 and 4.9, respectively. This finding differs while limiting binding of UCB to the relatively immobile from some reports that suggest that the two pK a values membranes of cell organelles. (5) Mechanisms were prein aqueous systems are near or above pH 7.0. (2) Consented for translocation of UDP-glucuronic acid (UDtrasting views of the hydrophobic interactions of UCB PGA) into the lumenal location of UDPGA transferase with bile salts were presented: one suggested that multiin the endoplasmic reticulum, as well as the enhanceple bile salt monomers bind to one UCB molecule; the ment of this process by N-acetyl-glucosamine. Studies other suggested that UCB binds to the nonpolar surface in the neonatal and congenital jaundice area were as of helical bile salt micelles. (3) Structures were proposed follows. (1) Criteria were reviewed for initiating treatfor the varied calcium and copper bilirubinate salts ment of neonatal jaundice, emphasizing the primacy of formed at various pH values and cation/UCB ratios. (4) serum bilirubin levels, gestational age, and hemolysis Studies of binding of UCB to human serum albumin as risk factors for kernicterus. (2) New methods were (HSA) showed marked diminution of UCB-binding affinpresented for frequent, automated monitoring of serum ity as albumin and chloride concentrations increased. bilirubin levels and breath CO levels as an index of rates (5) A unique UCB derivative, bilirubin-C10-sulfonic acid, of formation of UCB from heme. (3) The current status was identified as the major bile pigment in bullfrog bile. and limitations of new approaches to treatment of se-(6) New methods were presented for removal of impurivere unconjugated hyperbilirubinemia were discussed: ties from preparations of bile salts and UCB. Findings hepatocyte transplantation and gene therapy, still in the of studies in the transport area were as follows. (1) Four stage of development in animal models, have provided putative basolateral and two putative canalicular hepaonly partial and temporary relief of hyperbilirubinemia; tocytic transporters of UCB and related organic anions extracorporeal liver assist devices have had some sucwere described. Special emphasis was given to the adencess in initial human studies; and inhibition of heme osine triphosphate (ATP)-dependent canalicular multioxygenase (HO) with metalloporphyrins, especially tin specific organic anion transporter that is defective in mesoporphyrin, which markedly decreases bilirubin production for prolonged periods, is a new alternative Abbreviations: UCB, unconjugated bilirubin; NMR, nuclear magnetic resonance; NOE, to phototherapy. (4) The ontogeny of the two HO isonuclear Overhauser enhancement; DMSO, dimethyl sulfoxide; TC, taurocholate; CMC, criti-zymes was contrasted in the liver, spleen, kidney, and cal micellar concentration; CD, circular dichroism; Bf, concentration of unbound UCB; Kf,</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/57724175" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="4de5aba385c2ea1a32f8ff8a2aaf105e" rel="nofollow" data-download="{"attachment_id":72485155,"asset_id":57724175,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/72485155/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="68591426" href="https://trieste.academia.edu/ClaudioTiribelli">Claudio Tiribelli</a><script data-card-contents-for-user="68591426" type="text/json">{"id":68591426,"first_name":"Claudio","last_name":"Tiribelli","domain_name":"trieste","page_name":"ClaudioTiribelli","display_name":"Claudio Tiribelli","profile_url":"https://trieste.academia.edu/ClaudioTiribelli?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_57724175 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="57724175"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 57724175, container: ".js-paper-rank-work_57724175", }); 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(2) The roles of the classical and gated bilirubin (UCB) chemistry and physical chemistry; newer molecular biological approaches to identification UCB transport and intracellular trafficking; and evaluaof these transporters were contrasted, and their limitation and therapy of neonatal and congenital hyperbilitions were discussed. (3) The relative roles of the multirubinemias. Findings of studies in the chemistry and ple carriers in UCB transport under different conditions physical chemistry area were as follows. (1) Nuclear and substrate concentrations were discussed. (4) Cytomagnetic resonance (NMR) studies of highly enriched solic UCB-binding proteins (e.g., ligandin) were shown 13 COOH mesobilirubin in water-dimethyl sulfoxide systo promote transcellular movement of UCB by solubiliztems indicated that the pK a values of the carboxyl ing and transporting the pigment in the aqueous phase groups are 4.2 and 4.9, respectively. 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(4) serum bilirubin levels, gestational age, and hemolysis Studies of binding of UCB to human serum albumin as risk factors for kernicterus. (2) New methods were (HSA) showed marked diminution of UCB-binding affinpresented for frequent, automated monitoring of serum ity as albumin and chloride concentrations increased. bilirubin levels and breath CO levels as an index of rates (5) A unique UCB derivative, bilirubin-C10-sulfonic acid, of formation of UCB from heme. (3) The current status was identified as the major bile pigment in bullfrog bile. and limitations of new approaches to treatment of se-(6) New methods were presented for removal of impurivere unconjugated hyperbilirubinemia were discussed: ties from preparations of bile salts and UCB. Findings hepatocyte transplantation and gene therapy, still in the of studies in the transport area were as follows. (1) Four stage of development in animal models, have provided putative basolateral and two putative canalicular hepaonly partial and temporary relief of hyperbilirubinemia; tocytic transporters of UCB and related organic anions extracorporeal liver assist devices have had some sucwere described. Special emphasis was given to the adencess in initial human studies; and inhibition of heme osine triphosphate (ATP)-dependent canalicular multioxygenase (HO) with metalloporphyrins, especially tin specific organic anion transporter that is defective in mesoporphyrin, which markedly decreases bilirubin production for prolonged periods, is a new alternative Abbreviations: UCB, unconjugated bilirubin; NMR, nuclear magnetic resonance; NOE, to phototherapy. (4) The ontogeny of the two HO isonuclear Overhauser enhancement; DMSO, dimethyl sulfoxide; TC, taurocholate; CMC, criti-zymes was contrasted in the liver, spleen, kidney, and cal micellar concentration; CD, circular dichroism; Bf, concentration of unbound UCB; Kf,","downloadable_attachments":[{"id":72485155,"asset_id":57724175,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":68591426,"first_name":"Claudio","last_name":"Tiribelli","domain_name":"trieste","page_name":"ClaudioTiribelli","display_name":"Claudio Tiribelli","profile_url":"https://trieste.academia.edu/ClaudioTiribelli?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":7333,"name":"Nuclear Magnetic Resonance","url":"https://www.academia.edu/Documents/in/Nuclear_Magnetic_Resonance?f_ri=1816594","nofollow":true},{"id":7864,"name":"Gene Therapy","url":"https://www.academia.edu/Documents/in/Gene_Therapy?f_ri=1816594","nofollow":true},{"id":37773,"name":"Hepatology","url":"https://www.academia.edu/Documents/in/Hepatology?f_ri=1816594","nofollow":true},{"id":71437,"name":"Liver","url":"https://www.academia.edu/Documents/in/Liver?f_ri=1816594","nofollow":true},{"id":80692,"name":"Copper","url":"https://www.academia.edu/Documents/in/Copper?f_ri=1816594"},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=1816594"},{"id":151951,"name":"Animal Model","url":"https://www.academia.edu/Documents/in/Animal_Model?f_ri=1816594"},{"id":169489,"name":"Heme Oxygenase","url":"https://www.academia.edu/Documents/in/Heme_Oxygenase?f_ri=1816594"},{"id":178062,"name":"Bilirubin","url":"https://www.academia.edu/Documents/in/Bilirubin?f_ri=1816594"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594"},{"id":797418,"name":"Gestational Age","url":"https://www.academia.edu/Documents/in/Gestational_Age?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2225815,"name":"Binding affinity","url":"https://www.academia.edu/Documents/in/Binding_affinity?f_ri=1816594"},{"id":2450535,"name":"Assistive Device","url":"https://www.academia.edu/Documents/in/Assistive_Device?f_ri=1816594"},{"id":3061075,"name":"Genetic Therapy","url":"https://www.academia.edu/Documents/in/Genetic_Therapy?f_ri=1816594"},{"id":3686577,"name":"Human serum albumin","url":"https://www.academia.edu/Documents/in/Human_serum_albumin?f_ri=1816594"},{"id":3754981,"name":"glucuronosyltransferase","url":"https://www.academia.edu/Documents/in/glucuronosyltransferase?f_ri=1816594"},{"id":3789880,"name":"Medical biochemistry and metabolomics","url":"https://www.academia.edu/Documents/in/Medical_biochemistry_and_metabolomics?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_35325353" data-work_id="35325353" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/35325353/Enhancement_of_ATP_Levels_and_Glucose_Metabolism_during_an_Infection_by_Chlamydia_NMR_STUDIES_OF_LIVING_CELLS">Enhancement of ATP Levels and Glucose Metabolism during an Infection by Chlamydia. NMR STUDIES OF LIVING CELLS</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The Chlamydia species are obligate intracellular bacteria that proliferate only within the infected cell. Since the extracellular bacteria are metabolically inert and there are no cell-free systems for characterizing Chlamydia metabolism,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_35325353" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The Chlamydia species are obligate intracellular bacteria that proliferate only within the infected cell. Since the extracellular bacteria are metabolically inert and there are no cell-free systems for characterizing Chlamydia metabolism, we studied metabolic changes related to ATP synthesis and glycolysis in HeLa cells infected with Chlamydia psittaci during the course of the 2-day infection cycle using noninvasive 31 P and 13 C NMR methods. We find that the infection stimulates ATP synthesis in the infected cell, with a peak of ATP levels occurring midway through the infection cycle, when most of the metabolically active bacteria are proliferating. The infection also stimulates synthesis of glutamate with a similar time course as for ATP. The stimulation is apparently due to an enhancement in glucose consumption by the infected cell, which also results in an increased rate of lactate production and glutamate synthesis as well as higher glycogen accumulation during the infection. Concurrently, infection leads to an increase in the expression of the glucose transporter, GLUT-1, on HeLa cells, which may account for the enhanced glucose consumption. The chlamydiae are thus able to stimulate glucose transport in the host cell sufficiently to compensate for the extra energy load on the cell represented by the infection.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/35325353" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="150f91d5802d09d18f73d50fef41b921" rel="nofollow" data-download="{"attachment_id":55186706,"asset_id":35325353,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/55186706/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="68137832" href="https://independent.academia.edu/DOjcius">David Ojcius</a><script data-card-contents-for-user="68137832" type="text/json">{"id":68137832,"first_name":"David","last_name":"Ojcius","domain_name":"independent","page_name":"DOjcius","display_name":"David Ojcius","profile_url":"https://independent.academia.edu/DOjcius?f_ri=1816594","photo":"https://0.academia-photos.com/68137832/18502865/18465638/s65_david.ojcius.jpg"}</script></span></span></li><li class="js-paper-rank-work_35325353 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="35325353"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 35325353, container: ".js-paper-rank-work_35325353", }); 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NMR STUDIES OF LIVING CELLS","created_at":"2017-12-03T11:42:57.474-08:00","url":"https://www.academia.edu/35325353/Enhancement_of_ATP_Levels_and_Glucose_Metabolism_during_an_Infection_by_Chlamydia_NMR_STUDIES_OF_LIVING_CELLS?f_ri=1816594","dom_id":"work_35325353","summary":"The Chlamydia species are obligate intracellular bacteria that proliferate only within the infected cell. Since the extracellular bacteria are metabolically inert and there are no cell-free systems for characterizing Chlamydia metabolism, we studied metabolic changes related to ATP synthesis and glycolysis in HeLa cells infected with Chlamydia psittaci during the course of the 2-day infection cycle using noninvasive 31 P and 13 C NMR methods. We find that the infection stimulates ATP synthesis in the infected cell, with a peak of ATP levels occurring midway through the infection cycle, when most of the metabolically active bacteria are proliferating. The infection also stimulates synthesis of glutamate with a similar time course as for ATP. The stimulation is apparently due to an enhancement in glucose consumption by the infected cell, which also results in an increased rate of lactate production and glutamate synthesis as well as higher glycogen accumulation during the infection. Concurrently, infection leads to an increase in the expression of the glucose transporter, GLUT-1, on HeLa cells, which may account for the enhanced glucose consumption. The chlamydiae are thus able to stimulate glucose transport in the host cell sufficiently to compensate for the extra energy load on the cell represented by the infection.","downloadable_attachments":[{"id":55186706,"asset_id":35325353,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":68137832,"first_name":"David","last_name":"Ojcius","domain_name":"independent","page_name":"DOjcius","display_name":"David Ojcius","profile_url":"https://independent.academia.edu/DOjcius?f_ri=1816594","photo":"https://0.academia-photos.com/68137832/18502865/18465638/s65_david.ojcius.jpg"}],"research_interests":[{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=1816594","nofollow":true},{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=1816594","nofollow":true},{"id":18520,"name":"Biological Chemistry","url":"https://www.academia.edu/Documents/in/Biological_Chemistry?f_ri=1816594","nofollow":true},{"id":21732,"name":"Magnetic Resonance Spectroscopy","url":"https://www.academia.edu/Documents/in/Magnetic_Resonance_Spectroscopy?f_ri=1816594","nofollow":true},{"id":38650,"name":"Cell Division","url":"https://www.academia.edu/Documents/in/Cell_Division?f_ri=1816594"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594"},{"id":71289,"name":"Glucose","url":"https://www.academia.edu/Documents/in/Glucose?f_ri=1816594"},{"id":117643,"name":"Biological","url":"https://www.academia.edu/Documents/in/Biological?f_ri=1816594"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=1816594"},{"id":422325,"name":"HeLa cells","url":"https://www.academia.edu/Documents/in/HeLa_cells?f_ri=1816594"},{"id":541785,"name":"Phosphates","url":"https://www.academia.edu/Documents/in/Phosphates?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_26066584 coauthored" data-work_id="26066584" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/26066584/Modulation_of_locus_coeruleus_neurons_by_extra_and_intracellular_adenosine_5_triphosphate">Modulation of locus coeruleus neurons by extra- and intracellular adenosine 5'-triphosphate</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The cell membrane of rat locus coeruleus (LC) neurons is sensitive to both extra-and intracellular ATP. Extracellular ATP or its enzymatically stable analogues activate membrane receptors of the P2 type. These receptors inhibit a... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_26066584" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The cell membrane of rat locus coeruleus (LC) neurons is sensitive to both extra-and intracellular ATP. Extracellular ATP or its enzymatically stable analogues activate membrane receptors of the P2 type. These receptors inhibit a persistent potassium current and simultaneously activate a nonselective cationic conductance. The resulting depolarization increases the spontaneous firing rate. A decrease in the concentration of intracellular ATP during hypoxia or hypoglycemia opens ATP-sensitive K+ (KATP) channels of LC neurons. The resulting hyperpolarization depresses the discharge of action potentials and conserves energy. The hypoxia-induced hyperpolarization is additionally due to the release of adenosine from neighboring neurons or glial cells. A certain class of compounds, termed potassium channel openers, also decrease the firing, while sulphonylurea antidiabetics known to block KATp channels increase it. Sulphonylurea antidiabetics antagonize the excitability decrease induced both by potassium channel openers and metabolic damage.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/26066584" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="e400f0a22ec3c61694a4823b4bd719c0" rel="nofollow" data-download="{"attachment_id":46413151,"asset_id":26066584,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46413151/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="49946980" href="https://independent.academia.edu/KarenNieber">Karen Nieber</a><script data-card-contents-for-user="49946980" type="text/json">{"id":49946980,"first_name":"Karen","last_name":"Nieber","domain_name":"independent","page_name":"KarenNieber","display_name":"Karen Nieber","profile_url":"https://independent.academia.edu/KarenNieber?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-26066584">+1</span><div class="hidden js-additional-users-26066584"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/IIlles">Illes Illes</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-26066584'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-26066584').html(); 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Extracellular ATP or its enzymatically stable analogues activate membrane receptors of the P2 type. These receptors inhibit a persistent potassium current and simultaneously activate a nonselective cationic conductance. The resulting depolarization increases the spontaneous firing rate. A decrease in the concentration of intracellular ATP during hypoxia or hypoglycemia opens ATP-sensitive K+ (KATP) channels of LC neurons. The resulting hyperpolarization depresses the discharge of action potentials and conserves energy. The hypoxia-induced hyperpolarization is additionally due to the release of adenosine from neighboring neurons or glial cells. A certain class of compounds, termed potassium channel openers, also decrease the firing, while sulphonylurea antidiabetics known to block KATp channels increase it. Sulphonylurea antidiabetics antagonize the excitability decrease induced both by potassium channel openers and metabolic damage.","downloadable_attachments":[{"id":46413151,"asset_id":26066584,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":49946980,"first_name":"Karen","last_name":"Nieber","domain_name":"independent","page_name":"KarenNieber","display_name":"Karen Nieber","profile_url":"https://independent.academia.edu/KarenNieber?f_ri=1816594","photo":"/images/s65_no_pic.png"},{"id":50191779,"first_name":"Illes","last_name":"Illes","domain_name":"independent","page_name":"IIlles","display_name":"Illes Illes","profile_url":"https://independent.academia.edu/IIlles?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":237,"name":"Cognitive Science","url":"https://www.academia.edu/Documents/in/Cognitive_Science?f_ri=1816594","nofollow":true},{"id":10990,"name":"Hypoxia","url":"https://www.academia.edu/Documents/in/Hypoxia?f_ri=1816594","nofollow":true},{"id":61474,"name":"Brain","url":"https://www.academia.edu/Documents/in/Brain?f_ri=1816594","nofollow":true},{"id":193974,"name":"Neurons","url":"https://www.academia.edu/Documents/in/Neurons?f_ri=1816594","nofollow":true},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594"},{"id":548890,"name":"Locus coeruleus","url":"https://www.academia.edu/Documents/in/Locus_coeruleus?f_ri=1816594"},{"id":1239755,"name":"Neurosciences","url":"https://www.academia.edu/Documents/in/Neurosciences?f_ri=1816594"},{"id":1281442,"name":"Extracellular Space","url":"https://www.academia.edu/Documents/in/Extracellular_Space?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_15149763 coauthored" data-work_id="15149763" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/15149763/Gain_and_loss_of_function_of_P2X7_receptors_mechanisms_pharmacology_and_relevance_to_diabetic_neuropathic_pain">Gain and loss of function of P2X7 receptors: mechanisms, pharmacology and relevance to diabetic neuropathic pain</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Background: Genetic causes of exaggerated or reduced pain sensitivity in humans are well known. Recently, single nucleotide polymorphisms (SNPs) in the gene P2RX7, coding for the ATP-gated ion channel P2X 7, have been described that cause... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_15149763" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Background: Genetic causes of exaggerated or reduced pain sensitivity in humans are well known. Recently, single nucleotide polymorphisms (SNPs) in the gene P2RX7, coding for the ATP-gated ion channel P2X 7, have been described that cause gain-of-function (GOF) and loss-of-function (LOF), respectively of this channel. Importantly, P2RX7 SNPs have been associated with more or less severe pain scores in patient suffering of post-mastectomy pain and osteoarthritis. Results: The functional consequences of some P2RX7 SNPs (rs208294 (His155Tyr), rs1718119 (Ala348Thr) and rs3751143 (Glu496Ala)) were studied in recombinant cells in vitro. Our findings suggest a correlation between GOF and LOF of P2X 7 and actual channel protein expression. Both channel and pore function for these mutant P2X 7 receptors changed in parallel to protein levels. On the other hand, the mutant receptors did not differ in their sensitivity to known P2X 7 agonists and antagonists. We further demonstrated that in patients with diabetic peripheral neuropathic pain (DPNP), the presence of the GOF SNPs rs208294 (His155Tyr) and rs1718119 (Ala348Thr) is associated, in females, with higher pain intensity scores.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/15149763" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3e152bd12d911bd5dc8ea05ae570bee9" rel="nofollow" data-download="{"attachment_id":43528982,"asset_id":15149763,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/43528982/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="34188960" href="https://independent.academia.edu/WeiZou2">Wei Zou</a><script data-card-contents-for-user="34188960" type="text/json">{"id":34188960,"first_name":"Wei","last_name":"Zou","domain_name":"independent","page_name":"WeiZou2","display_name":"Wei Zou","profile_url":"https://independent.academia.edu/WeiZou2?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-15149763">+1</span><div class="hidden js-additional-users-15149763"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/YueweiQian">Yue-wei Qian</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-15149763'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-15149763').html(); } } new HoverPopover(popoverSettings); })();</script></li><li class="js-paper-rank-work_15149763 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="15149763"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 15149763, container: ".js-paper-rank-work_15149763", }); });</script></li><li class="js-percentile-work_15149763 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 15149763; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_15149763"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_15149763 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="15149763"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 15149763; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=15149763]").text(description); $(".js-view-count-work_15149763").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_15149763").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="15149763"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">9</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="372410" rel="nofollow" href="https://www.academia.edu/Documents/in/Genotype">Genotype</a>, <script data-card-contents-for-ri="372410" type="text/json">{"id":372410,"name":"Genotype","url":"https://www.academia.edu/Documents/in/Genotype?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="413194" rel="nofollow" href="https://www.academia.edu/Documents/in/Analysis_of_Variance">Analysis of Variance</a>, <script data-card-contents-for-ri="413194" type="text/json">{"id":413194,"name":"Analysis of Variance","url":"https://www.academia.edu/Documents/in/Analysis_of_Variance?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="620070" rel="nofollow" href="https://www.academia.edu/Documents/in/Transfection">Transfection</a><script data-card-contents-for-ri="620070" type="text/json">{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=15149763]'), work: {"id":15149763,"title":"Gain and loss of function of P2X7 receptors: mechanisms, pharmacology and relevance to diabetic neuropathic pain","created_at":"2015-08-24T09:48:36.484-07:00","url":"https://www.academia.edu/15149763/Gain_and_loss_of_function_of_P2X7_receptors_mechanisms_pharmacology_and_relevance_to_diabetic_neuropathic_pain?f_ri=1816594","dom_id":"work_15149763","summary":"Background: Genetic causes of exaggerated or reduced pain sensitivity in humans are well known. Recently, single nucleotide polymorphisms (SNPs) in the gene P2RX7, coding for the ATP-gated ion channel P2X 7, have been described that cause gain-of-function (GOF) and loss-of-function (LOF), respectively of this channel. Importantly, P2RX7 SNPs have been associated with more or less severe pain scores in patient suffering of post-mastectomy pain and osteoarthritis. Results: The functional consequences of some P2RX7 SNPs (rs208294 (His155Tyr), rs1718119 (Ala348Thr) and rs3751143 (Glu496Ala)) were studied in recombinant cells in vitro. Our findings suggest a correlation between GOF and LOF of P2X 7 and actual channel protein expression. Both channel and pore function for these mutant P2X 7 receptors changed in parallel to protein levels. On the other hand, the mutant receptors did not differ in their sensitivity to known P2X 7 agonists and antagonists. We further demonstrated that in patients with diabetic peripheral neuropathic pain (DPNP), the presence of the GOF SNPs rs208294 (His155Tyr) and rs1718119 (Ala348Thr) is associated, in females, with higher pain intensity scores.","downloadable_attachments":[{"id":43528982,"asset_id":15149763,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":34188960,"first_name":"Wei","last_name":"Zou","domain_name":"independent","page_name":"WeiZou2","display_name":"Wei Zou","profile_url":"https://independent.academia.edu/WeiZou2?f_ri=1816594","photo":"/images/s65_no_pic.png"},{"id":34349698,"first_name":"Yue-wei","last_name":"Qian","domain_name":"independent","page_name":"YueweiQian","display_name":"Yue-wei Qian","profile_url":"https://independent.academia.edu/YueweiQian?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":372410,"name":"Genotype","url":"https://www.academia.edu/Documents/in/Genotype?f_ri=1816594","nofollow":true},{"id":413194,"name":"Analysis of Variance","url":"https://www.academia.edu/Documents/in/Analysis_of_Variance?f_ri=1816594","nofollow":true},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection?f_ri=1816594","nofollow":true},{"id":824508,"name":"Benzoxazoles","url":"https://www.academia.edu/Documents/in/Benzoxazoles?f_ri=1816594"},{"id":1239755,"name":"Neurosciences","url":"https://www.academia.edu/Documents/in/Neurosciences?f_ri=1816594"},{"id":1262481,"name":"Pain Measurement","url":"https://www.academia.edu/Documents/in/Pain_Measurement?f_ri=1816594"},{"id":1763968,"name":"Gene Expression Regulation","url":"https://www.academia.edu/Documents/in/Gene_Expression_Regulation?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_15668749" data-work_id="15668749" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/15668749/_Immuknow_to_Measurement_of_Cell_Mediated_Immunity_in_Renal_Transplant_Recipients_Undergoing_Short_Term_Evaluation">“Immuknow” to Measurement of Cell-Mediated Immunity in Renal Transplant Recipients Undergoing Short-Term Evaluation</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The aim of this preliminary, observational study was to evaluate the value of ImmuKnow (IK), a new tool to measure the net state of immunefunction among renal transplant recipients, in correlation with clinical and laboratory data among... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_15668749" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The aim of this preliminary, observational study was to evaluate the value of ImmuKnow (IK), a new tool to measure the net state of immunefunction among renal transplant recipients, in correlation with clinical and laboratory data among unselected renal transplant recipients. Forty-nine recipients of mean age of 51 years were enrolled and followed for 1 year after transplantation. All subjects received the same immunosuppressive strategy with basiliximab induction and tacrolimus, mycophenolate mofetil and steroid maintenance therapy. Samples for IK were collected before transplantation as well as at 7, 14, 21 and 42 days and after 3, 6, and 12 months. There were 54 samples with IK Ͻ225 ng/mL, 201 samples with normal IK values, and 135 samples with Ͼ525 ng/mL. We divided recipients into 3 groups with respect to their basal IK values: Group 1 (Gr1; IK Ͻ225 ng/mL); Group 2 (Gr2; normal values of IK between 226 and 524 ng/mL); and Group 3 (Gr3; IK Ͼ525 ng/mL). At 1 year, we observed a significant difference among IK values at the start and the end of the study: Gr1 vs Gr2, P Ͻ .0001; Gr2 vs Gr3, P Ͻ .06 and Gr 1 vs Gr 3, P Ͻ .01). We observed reduced IK values to predict an increased risk of infection, particularly with cytomegalovirus (CMV) replication while higher IK value did not correlate with an increased risk of acute rejection episodes. Reduction of serum creatine levels occurred within 1 year in all groups (P Ͻ .005), but there was a significant difference between Gr 2 versus Grs 1 and 3 (P Ͻ .0001 and P Ͻ .0005, respectively). There findings suggested that more stable IK values were associated with clinical quiescence and laboratory stability. In conclusion, our preliminary analysis showed a beneficial capacity of this assay to represent the global depression of the immune system. We noted that reduced IK values, as a sign of excessive immunosuppressive therapy, were associated with an increased risk of infection. We did not confirm the predictive value of higher IK values for an increased risk of an acute rejection episode.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/15668749" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="f088d57d3efcafd4f225aabeb30ec4dc" rel="nofollow" data-download="{"attachment_id":42987039,"asset_id":15668749,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/42987039/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="34855933" href="https://independent.academia.edu/ChiaraAgrati">Chiara Agrati</a><script data-card-contents-for-user="34855933" type="text/json">{"id":34855933,"first_name":"Chiara","last_name":"Agrati","domain_name":"independent","page_name":"ChiaraAgrati","display_name":"Chiara Agrati","profile_url":"https://independent.academia.edu/ChiaraAgrati?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_15668749 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="15668749"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 15668749, container: ".js-paper-rank-work_15668749", }); 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Forty-nine recipients of mean age of 51 years were enrolled and followed for 1 year after transplantation. All subjects received the same immunosuppressive strategy with basiliximab induction and tacrolimus, mycophenolate mofetil and steroid maintenance therapy. Samples for IK were collected before transplantation as well as at 7, 14, 21 and 42 days and after 3, 6, and 12 months. There were 54 samples with IK Ͻ225 ng/mL, 201 samples with normal IK values, and 135 samples with Ͼ525 ng/mL. We divided recipients into 3 groups with respect to their basal IK values: Group 1 (Gr1; IK Ͻ225 ng/mL); Group 2 (Gr2; normal values of IK between 226 and 524 ng/mL); and Group 3 (Gr3; IK Ͼ525 ng/mL). At 1 year, we observed a significant difference among IK values at the start and the end of the study: Gr1 vs Gr2, P Ͻ .0001; Gr2 vs Gr3, P Ͻ .06 and Gr 1 vs Gr 3, P Ͻ .01). We observed reduced IK values to predict an increased risk of infection, particularly with cytomegalovirus (CMV) replication while higher IK value did not correlate with an increased risk of acute rejection episodes. Reduction of serum creatine levels occurred within 1 year in all groups (P Ͻ .005), but there was a significant difference between Gr 2 versus Grs 1 and 3 (P Ͻ .0001 and P Ͻ .0005, respectively). There findings suggested that more stable IK values were associated with clinical quiescence and laboratory stability. In conclusion, our preliminary analysis showed a beneficial capacity of this assay to represent the global depression of the immune system. We noted that reduced IK values, as a sign of excessive immunosuppressive therapy, were associated with an increased risk of infection. We did not confirm the predictive value of higher IK values for an increased risk of an acute rejection episode.","downloadable_attachments":[{"id":42987039,"asset_id":15668749,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":34855933,"first_name":"Chiara","last_name":"Agrati","domain_name":"independent","page_name":"ChiaraAgrati","display_name":"Chiara Agrati","profile_url":"https://independent.academia.edu/ChiaraAgrati?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9003,"name":"Kidney transplantation","url":"https://www.academia.edu/Documents/in/Kidney_transplantation?f_ri=1816594","nofollow":true},{"id":12426,"name":"Treatment Outcome","url":"https://www.academia.edu/Documents/in/Treatment_Outcome?f_ri=1816594","nofollow":true},{"id":16664,"name":"Risk 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factors","url":"https://www.academia.edu/Documents/in/Risk_factors?f_ri=1816594"},{"id":289271,"name":"Aged","url":"https://www.academia.edu/Documents/in/Aged?f_ri=1816594"},{"id":324154,"name":"Immune system","url":"https://www.academia.edu/Documents/in/Immune_system?f_ri=1816594"},{"id":413195,"name":"Time Factors","url":"https://www.academia.edu/Documents/in/Time_Factors?f_ri=1816594"},{"id":487159,"name":"Group","url":"https://www.academia.edu/Documents/in/Group?f_ri=1816594"},{"id":568482,"name":"Biological markers","url":"https://www.academia.edu/Documents/in/Biological_markers?f_ri=1816594"},{"id":572282,"name":"Combination drug therapy","url":"https://www.academia.edu/Documents/in/Combination_drug_therapy?f_ri=1816594"},{"id":620049,"name":"Risk Factors","url":"https://www.academia.edu/Documents/in/Risk_Factors-1?f_ri=1816594"},{"id":622589,"name":"Risk Assessment","url":"https://www.academia.edu/Documents/in/Risk_Assessment-2?f_ri=1816594"},{"id":893785,"name":"Graft Rejection","url":"https://www.academia.edu/Documents/in/Graft_Rejection?f_ri=1816594"},{"id":910024,"name":"Observational Study","url":"https://www.academia.edu/Documents/in/Observational_Study?f_ri=1816594"},{"id":945595,"name":"Pilot Projects","url":"https://www.academia.edu/Documents/in/Pilot_Projects?f_ri=1816594"},{"id":1007684,"name":"Virus diseases","url":"https://www.academia.edu/Documents/in/Virus_diseases?f_ri=1816594"},{"id":1318932,"name":"Predictive value of tests","url":"https://www.academia.edu/Documents/in/Predictive_value_of_tests?f_ri=1816594"},{"id":1740530,"name":"Mycophenolate mofetil","url":"https://www.academia.edu/Documents/in/Mycophenolate_mofetil?f_ri=1816594"},{"id":1740532,"name":"Acute rejection","url":"https://www.academia.edu/Documents/in/Acute_rejection?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div 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Vink","profile_url":"https://unisa-au.academia.edu/RobertVink?f_ri=1816594","photo":"https://0.academia-photos.com/33940403/11811950/13165455/s65_robert.vink.jpg"}],"research_interests":[{"id":237,"name":"Cognitive Science","url":"https://www.academia.edu/Documents/in/Cognitive_Science?f_ri=1816594","nofollow":true},{"id":6200,"name":"Magnetic Resonance Imaging","url":"https://www.academia.edu/Documents/in/Magnetic_Resonance_Imaging?f_ri=1816594","nofollow":true},{"id":70902,"name":"Magnesium","url":"https://www.academia.edu/Documents/in/Magnesium?f_ri=1816594","nofollow":true},{"id":172083,"name":"Phosphorylation","url":"https://www.academia.edu/Documents/in/Phosphorylation?f_ri=1816594","nofollow":true},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594"},{"id":1137254,"name":"Hydrogen-Ion Concentration","url":"https://www.academia.edu/Documents/in/Hydrogen-Ion_Concentration?f_ri=1816594"},{"id":1239755,"name":"Neurosciences","url":"https://www.academia.edu/Documents/in/Neurosciences?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_79327166" data-work_id="79327166" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/79327166/ATP_and_ADP_actin_states">ATP and ADP actin states</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a 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contradictory effects due to the simultaneous elevation of both ketone bodies and free fatty acids. While the elevation of ketone bodies increase the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_29792771" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Ketosis induced by starvation or feeding a ketogenic diet have widespread and often contradictory effects due to the simultaneous elevation of both ketone bodies and free fatty acids. While the elevation of ketone bodies increase the energy of ATP hydrolysis by reducing mitochondrial NAD couple and oxidizing the co-Q couple, thus increasing the redox span between site I and site II. In contrast, metabolism of fatty acids leads to a reduction of both mitochondrial NAD but also of mitochondrial Q causing decrease in the G of ATP hydrolysis. In contrast, feeding ketone body esters leads to pure ketosis, unaccompanied by elevation of free fatty acids, producing a physiological state not previously seen in nature. The effects of pure ketosis on transcription and upon certain neurodegenerative diseases make approach not only interesting, but one of potential therapeutic value. by guest, on November 11, 2016 <a href="http://www.jlr.org" rel="nofollow">www.jlr.org</a> Downloaded from 12. Li, L., and J. L. Messina. 2009. Acute insulin resistance following injury. Trends Endocrinol.Metab 20: 429-435. 13. Kashiwaya, Y., M. T. King, and R. L. Veech. 1997. Substrate signaling by insulin: a ketone bodies ratio mimics insulin action in heart. Am.J.Cardiol. 80: 50A-64A.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/29792771" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="a195ac603353bfd79a2b66b1579f39d5" rel="nofollow" data-download="{"attachment_id":50249316,"asset_id":29792771,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/50249316/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="55839260" href="https://independent.academia.edu/RichardLVeech">Richard L Veech</a><script data-card-contents-for-user="55839260" type="text/json">{"id":55839260,"first_name":"Richard L","last_name":"Veech","domain_name":"independent","page_name":"RichardLVeech","display_name":"Richard L Veech","profile_url":"https://independent.academia.edu/RichardLVeech?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_29792771 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="29792771"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 29792771, container: ".js-paper-rank-work_29792771", }); 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$(".js-view-count[data-work-id=29792771]").text(description); $(".js-view-count-work_29792771").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_29792771").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="29792771"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">9</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="42915" rel="nofollow" href="https://www.academia.edu/Documents/in/Starvation">Starvation</a>, <script data-card-contents-for-ri="42915" type="text/json">{"id":42915,"name":"Starvation","url":"https://www.academia.edu/Documents/in/Starvation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="64848" rel="nofollow" href="https://www.academia.edu/Documents/in/Ketosis">Ketosis</a>, <script data-card-contents-for-ri="64848" type="text/json">{"id":64848,"name":"Ketosis","url":"https://www.academia.edu/Documents/in/Ketosis?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="72314" rel="nofollow" href="https://www.academia.edu/Documents/in/Fatty_acids">Fatty acids</a>, <script data-card-contents-for-ri="72314" type="text/json">{"id":72314,"name":"Fatty acids","url":"https://www.academia.edu/Documents/in/Fatty_acids?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="717115" rel="nofollow" href="https://www.academia.edu/Documents/in/Lipid">Lipid</a><script data-card-contents-for-ri="717115" type="text/json">{"id":717115,"name":"Lipid","url":"https://www.academia.edu/Documents/in/Lipid?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29792771]'), work: {"id":29792771,"title":"Ketone Ester Effects on Metabolism and Transcription","created_at":"2016-11-11T03:49:17.910-08:00","url":"https://www.academia.edu/29792771/Ketone_Ester_Effects_on_Metabolism_and_Transcription?f_ri=1816594","dom_id":"work_29792771","summary":"Ketosis induced by starvation or feeding a ketogenic diet have widespread and often contradictory effects due to the simultaneous elevation of both ketone bodies and free fatty acids. While the elevation of ketone bodies increase the energy of ATP hydrolysis by reducing mitochondrial NAD couple and oxidizing the co-Q couple, thus increasing the redox span between site I and site II. In contrast, metabolism of fatty acids leads to a reduction of both mitochondrial NAD but also of mitochondrial Q causing decrease in the G of ATP hydrolysis. In contrast, feeding ketone body esters leads to pure ketosis, unaccompanied by elevation of free fatty acids, producing a physiological state not previously seen in nature. The effects of pure ketosis on transcription and upon certain neurodegenerative diseases make approach not only interesting, but one of potential therapeutic value. by guest, on November 11, 2016 www.jlr.org Downloaded from 12. Li, L., and J. L. Messina. 2009. Acute insulin resistance following injury. Trends Endocrinol.Metab 20: 429-435. 13. Kashiwaya, Y., M. T. King, and R. L. Veech. 1997. Substrate signaling by insulin: a ketone bodies ratio mimics insulin action in heart. Am.J.Cardiol. 80: 50A-64A.","downloadable_attachments":[{"id":50249316,"asset_id":29792771,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":55839260,"first_name":"Richard L","last_name":"Veech","domain_name":"independent","page_name":"RichardLVeech","display_name":"Richard L Veech","profile_url":"https://independent.academia.edu/RichardLVeech?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":42915,"name":"Starvation","url":"https://www.academia.edu/Documents/in/Starvation?f_ri=1816594","nofollow":true},{"id":64848,"name":"Ketosis","url":"https://www.academia.edu/Documents/in/Ketosis?f_ri=1816594","nofollow":true},{"id":72314,"name":"Fatty acids","url":"https://www.academia.edu/Documents/in/Fatty_acids?f_ri=1816594","nofollow":true},{"id":717115,"name":"Lipid","url":"https://www.academia.edu/Documents/in/Lipid?f_ri=1816594","nofollow":true},{"id":828507,"name":"NAD","url":"https://www.academia.edu/Documents/in/NAD?f_ri=1816594"},{"id":1121353,"name":"Esters","url":"https://www.academia.edu/Documents/in/Esters?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1893820,"name":"Ketogenic diet","url":"https://www.academia.edu/Documents/in/Ketogenic_diet?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_29661594" data-work_id="29661594" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/29661594/Cell_free_biosynthesis_of_surfactin_a_cyclic_lipopeptide_produced_by_Bacillus_subtilis">Cell-free biosynthesis of surfactin, a cyclic lipopeptide produced by Bacillus subtilis</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The lipopeptide antibiotic surfactin is a potent extracellular biosurfactant produced by various Bacillus subtilis strains. Biosynthesis of surfactin was studied in a cell-free system prepared from B. subtilis ATCC 21332 and OKB 105,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_29661594" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The lipopeptide antibiotic surfactin is a potent extracellular biosurfactant produced by various Bacillus subtilis strains. Biosynthesis of surfactin was studied in a cell-free system prepared from B. subtilis ATCC 21332 and OKB 105, which is a transformant producing surfactin in high yield [Nakano, M. M., Marahiel, M.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/29661594" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="66f17906116fafa12f1faa8cd44605f6" rel="nofollow" data-download="{"attachment_id":50097753,"asset_id":29661594,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/50097753/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="56021668" href="https://tu-berlin.academia.edu/JoachimVater">Joachim Vater</a><script data-card-contents-for-user="56021668" type="text/json">{"id":56021668,"first_name":"Joachim","last_name":"Vater","domain_name":"tu-berlin","page_name":"JoachimVater","display_name":"Joachim Vater","profile_url":"https://tu-berlin.academia.edu/JoachimVater?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_29661594 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="29661594"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 29661594, container: ".js-paper-rank-work_29661594", }); 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$(".js-view-count[data-work-id=29661594]").text(description); $(".js-view-count-work_29661594").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_29661594").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="29661594"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="145" rel="nofollow" href="https://www.academia.edu/Documents/in/Biochemistry">Biochemistry</a>, <script data-card-contents-for-ri="145" type="text/json">{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="5769" rel="nofollow" href="https://www.academia.edu/Documents/in/Mass_Spectrometry">Mass Spectrometry</a>, <script data-card-contents-for-ri="5769" type="text/json">{"id":5769,"name":"Mass Spectrometry","url":"https://www.academia.edu/Documents/in/Mass_Spectrometry?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="113903" rel="nofollow" href="https://www.academia.edu/Documents/in/Bacteria">Bacteria</a>, <script data-card-contents-for-ri="113903" type="text/json">{"id":113903,"name":"Bacteria","url":"https://www.academia.edu/Documents/in/Bacteria?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="158399" rel="nofollow" href="https://www.academia.edu/Documents/in/Cyclic_peptides">Cyclic peptides</a><script data-card-contents-for-ri="158399" type="text/json">{"id":158399,"name":"Cyclic peptides","url":"https://www.academia.edu/Documents/in/Cyclic_peptides?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29661594]'), work: {"id":29661594,"title":"Cell-free biosynthesis of surfactin, a cyclic lipopeptide produced by Bacillus subtilis","created_at":"2016-11-04T03:09:57.998-07:00","url":"https://www.academia.edu/29661594/Cell_free_biosynthesis_of_surfactin_a_cyclic_lipopeptide_produced_by_Bacillus_subtilis?f_ri=1816594","dom_id":"work_29661594","summary":"The lipopeptide antibiotic surfactin is a potent extracellular biosurfactant produced by various Bacillus subtilis strains. Biosynthesis of surfactin was studied in a cell-free system prepared from B. subtilis ATCC 21332 and OKB 105, which is a transformant producing surfactin in high yield [Nakano, M. M., Marahiel, M.","downloadable_attachments":[{"id":50097753,"asset_id":29661594,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":56021668,"first_name":"Joachim","last_name":"Vater","domain_name":"tu-berlin","page_name":"JoachimVater","display_name":"Joachim Vater","profile_url":"https://tu-berlin.academia.edu/JoachimVater?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=1816594","nofollow":true},{"id":5769,"name":"Mass Spectrometry","url":"https://www.academia.edu/Documents/in/Mass_Spectrometry?f_ri=1816594","nofollow":true},{"id":113903,"name":"Bacteria","url":"https://www.academia.edu/Documents/in/Bacteria?f_ri=1816594","nofollow":true},{"id":158399,"name":"Cyclic peptides","url":"https://www.academia.edu/Documents/in/Cyclic_peptides?f_ri=1816594","nofollow":true},{"id":295928,"name":"Amino Acids","url":"https://www.academia.edu/Documents/in/Amino_Acids?f_ri=1816594"},{"id":386872,"name":"Bacillus subtilis","url":"https://www.academia.edu/Documents/in/Bacillus_subtilis?f_ri=1816594"},{"id":509439,"name":"Autoradiography","url":"https://www.academia.edu/Documents/in/Autoradiography?f_ri=1816594"},{"id":541785,"name":"Phosphates","url":"https://www.academia.edu/Documents/in/Phosphates?f_ri=1816594"},{"id":784076,"name":"Species Specificity","url":"https://www.academia.edu/Documents/in/Species_Specificity?f_ri=1816594"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=1816594"},{"id":965028,"name":"Cell free System","url":"https://www.academia.edu/Documents/in/Cell_free_System?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1744302,"name":"Lipopeptides","url":"https://www.academia.edu/Documents/in/Lipopeptides?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_29141543" data-work_id="29141543" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/29141543/Effects_of_Unloaded_Reperfusion_on_Mitochondrial_Function_in_the_Postischemic_Myocardium">Effects of Unloaded Reperfusion on Mitochondrial Function in the Postischemic Myocardium</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The effect of mechanical unloading on recovery of postischemic myocardial performance, high energy phosphate content, and mitochondrial function was tested in an isolated working rabbit heart model. After 30 min of global ischemia,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_29141543" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The effect of mechanical unloading on recovery of postischemic myocardial performance, high energy phosphate content, and mitochondrial function was tested in an isolated working rabbit heart model. After 30 min of global ischemia, prolonged unloaded reperfusion could prevent complete loss of contractility, deterioration of mitochondrial function, and depletion of the ATP pool as was found when only short-term unloading was performed. Aortic flow recovered to 21% of preischemic control, and left ventricular dP/dt max to 46% (p < 0.05 vs. short-term unloading). OPR and ADP/O stabilized at 42 and 72%, respectively (p < 0.05 vs. short-term un. loading), and ATP at 33% of control (p < 0.05 vs. shortterm unloading). These results show the beneficial effect of prolonged unloading in postischemic hearts.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/29141543" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="be9ec3dbdc5a79bd578c373ceb1c4c30" rel="nofollow" data-download="{"attachment_id":49588436,"asset_id":29141543,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/49588436/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="12108245" href="https://independent.academia.edu/FerdinandWaldenberger">Ferdinand Waldenberger</a><script data-card-contents-for-user="12108245" type="text/json">{"id":12108245,"first_name":"Ferdinand","last_name":"Waldenberger","domain_name":"independent","page_name":"FerdinandWaldenberger","display_name":"Ferdinand Waldenberger","profile_url":"https://independent.academia.edu/FerdinandWaldenberger?f_ri=1816594","photo":"https://0.academia-photos.com/12108245/8425730/9419211/s65_ferdinand.waldenberger.jpg"}</script></span></span></li><li class="js-paper-rank-work_29141543 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="29141543"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 29141543, container: ".js-paper-rank-work_29141543", }); });</script></li><li class="js-percentile-work_29141543 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 29141543; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_29141543"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_29141543 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="29141543"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29141543; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29141543]").text(description); $(".js-view-count-work_29141543").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_29141543").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="29141543"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">9</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="1131" rel="nofollow" href="https://www.academia.edu/Documents/in/Biomedical_Engineering">Biomedical Engineering</a>, <script data-card-contents-for-ri="1131" type="text/json">{"id":1131,"name":"Biomedical Engineering","url":"https://www.academia.edu/Documents/in/Biomedical_Engineering?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="11101" rel="nofollow" href="https://www.academia.edu/Documents/in/Artificial_Organs">Artificial Organs</a>, <script data-card-contents-for-ri="11101" type="text/json">{"id":11101,"name":"Artificial Organs","url":"https://www.academia.edu/Documents/in/Artificial_Organs?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="131495" rel="nofollow" href="https://www.academia.edu/Documents/in/Heart">Heart</a>, <script data-card-contents-for-ri="131495" type="text/json">{"id":131495,"name":"Heart","url":"https://www.academia.edu/Documents/in/Heart?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="244814" rel="nofollow" href="https://www.academia.edu/Documents/in/Clinical_Sciences">Clinical Sciences</a><script data-card-contents-for-ri="244814" type="text/json">{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29141543]'), work: {"id":29141543,"title":"Effects of Unloaded Reperfusion on Mitochondrial Function in the Postischemic Myocardium","created_at":"2016-10-13T23:28:50.654-07:00","url":"https://www.academia.edu/29141543/Effects_of_Unloaded_Reperfusion_on_Mitochondrial_Function_in_the_Postischemic_Myocardium?f_ri=1816594","dom_id":"work_29141543","summary":"The effect of mechanical unloading on recovery of postischemic myocardial performance, high energy phosphate content, and mitochondrial function was tested in an isolated working rabbit heart model. After 30 min of global ischemia, prolonged unloaded reperfusion could prevent complete loss of contractility, deterioration of mitochondrial function, and depletion of the ATP pool as was found when only short-term unloading was performed. Aortic flow recovered to 21% of preischemic control, and left ventricular dP/dt max to 46% (p \u003c 0.05 vs. short-term unloading). OPR and ADP/O stabilized at 42 and 72%, respectively (p \u003c 0.05 vs. short-term un. loading), and ATP at 33% of control (p \u003c 0.05 vs. shortterm unloading). These results show the beneficial effect of prolonged unloading in postischemic hearts.","downloadable_attachments":[{"id":49588436,"asset_id":29141543,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":12108245,"first_name":"Ferdinand","last_name":"Waldenberger","domain_name":"independent","page_name":"FerdinandWaldenberger","display_name":"Ferdinand Waldenberger","profile_url":"https://independent.academia.edu/FerdinandWaldenberger?f_ri=1816594","photo":"https://0.academia-photos.com/12108245/8425730/9419211/s65_ferdinand.waldenberger.jpg"}],"research_interests":[{"id":1131,"name":"Biomedical Engineering","url":"https://www.academia.edu/Documents/in/Biomedical_Engineering?f_ri=1816594","nofollow":true},{"id":11101,"name":"Artificial Organs","url":"https://www.academia.edu/Documents/in/Artificial_Organs?f_ri=1816594","nofollow":true},{"id":131495,"name":"Heart","url":"https://www.academia.edu/Documents/in/Heart?f_ri=1816594","nofollow":true},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594","nofollow":true},{"id":434453,"name":"Oxidative phosphorylation","url":"https://www.academia.edu/Documents/in/Oxidative_phosphorylation?f_ri=1816594"},{"id":788677,"name":"Rabbits","url":"https://www.academia.edu/Documents/in/Rabbits?f_ri=1816594"},{"id":1193624,"name":"Oxygen Consumption","url":"https://www.academia.edu/Documents/in/Oxygen_Consumption?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2503388,"name":"Myocardial Ischemia","url":"https://www.academia.edu/Documents/in/Myocardial_Ischemia?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_29014825" data-work_id="29014825" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/29014825/Thrombotic_thrombocytopenic_purpura_in_2_siblings_Defective_platelet_function_and_plasma_factor_deficiency_occurring_simultaneously">Thrombotic thrombocytopenic purpura in 2 siblings: Defective platelet function and plasma factor deficiency occurring simultaneously</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">In 2 siblings with recurring attacks of thrombotic thrombocytopenic purpura, platelet aggregation was found to be decreased during attacks. In contrast with reported observations in other patients, aggregation was found decreased also in... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_29014825" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">In 2 siblings with recurring attacks of thrombotic thrombocytopenic purpura, platelet aggregation was found to be decreased during attacks. In contrast with reported observations in other patients, aggregation was found decreased also in symptom-free periods. ATP/ADP ratio in platelet rich plasma was normal. The cause of decreased aggregation was not uraemia, alcohol or drugs. In a healthy sister, platelet aggregation induced by A D P was subnormal. The attacks in 1 of the patients responded to infusion of fresh frozen plasma.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/29014825" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="3ecc22667912daa2dbc2963073c511fc" rel="nofollow" data-download="{"attachment_id":49464360,"asset_id":29014825,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/49464360/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32696017" href="https://ntnu-no.academia.edu/AndersWaage">Anders Waage</a><script data-card-contents-for-user="32696017" type="text/json">{"id":32696017,"first_name":"Anders","last_name":"Waage","domain_name":"ntnu-no","page_name":"AndersWaage","display_name":"Anders Waage","profile_url":"https://ntnu-no.academia.edu/AndersWaage?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_29014825 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="29014825"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 29014825, container: ".js-paper-rank-work_29014825", }); });</script></li><li class="js-percentile-work_29014825 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 29014825; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_29014825"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_29014825 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="29014825"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29014825; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29014825]").text(description); $(".js-view-count-work_29014825").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_29014825").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="29014825"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">8</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="61099" rel="nofollow" href="https://www.academia.edu/Documents/in/Thrombin">Thrombin</a>, <script data-card-contents-for-ri="61099" type="text/json">{"id":61099,"name":"Thrombin","url":"https://www.academia.edu/Documents/in/Thrombin?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="65641" rel="nofollow" href="https://www.academia.edu/Documents/in/Platelet_aggregation">Platelet aggregation</a>, <script data-card-contents-for-ri="65641" type="text/json">{"id":65641,"name":"Platelet aggregation","url":"https://www.academia.edu/Documents/in/Platelet_aggregation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="117555" rel="nofollow" href="https://www.academia.edu/Documents/in/Plasma">Plasma</a>, <script data-card-contents-for-ri="117555" type="text/json">{"id":117555,"name":"Plasma","url":"https://www.academia.edu/Documents/in/Plasma?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="225159" rel="nofollow" href="https://www.academia.edu/Documents/in/Platelet_function">Platelet function</a><script data-card-contents-for-ri="225159" type="text/json">{"id":225159,"name":"Platelet function","url":"https://www.academia.edu/Documents/in/Platelet_function?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29014825]'), work: {"id":29014825,"title":"Thrombotic thrombocytopenic purpura in 2 siblings: Defective platelet function and plasma factor deficiency occurring simultaneously","created_at":"2016-10-08T18:55:45.096-07:00","url":"https://www.academia.edu/29014825/Thrombotic_thrombocytopenic_purpura_in_2_siblings_Defective_platelet_function_and_plasma_factor_deficiency_occurring_simultaneously?f_ri=1816594","dom_id":"work_29014825","summary":"In 2 siblings with recurring attacks of thrombotic thrombocytopenic purpura, platelet aggregation was found to be decreased during attacks. In contrast with reported observations in other patients, aggregation was found decreased also in symptom-free periods. ATP/ADP ratio in platelet rich plasma was normal. The cause of decreased aggregation was not uraemia, alcohol or drugs. In a healthy sister, platelet aggregation induced by A D P was subnormal. The attacks in 1 of the patients responded to infusion of fresh frozen plasma.","downloadable_attachments":[{"id":49464360,"asset_id":29014825,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32696017,"first_name":"Anders","last_name":"Waage","domain_name":"ntnu-no","page_name":"AndersWaage","display_name":"Anders Waage","profile_url":"https://ntnu-no.academia.edu/AndersWaage?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":61099,"name":"Thrombin","url":"https://www.academia.edu/Documents/in/Thrombin?f_ri=1816594","nofollow":true},{"id":65641,"name":"Platelet aggregation","url":"https://www.academia.edu/Documents/in/Platelet_aggregation?f_ri=1816594","nofollow":true},{"id":117555,"name":"Plasma","url":"https://www.academia.edu/Documents/in/Plasma?f_ri=1816594","nofollow":true},{"id":225159,"name":"Platelet function","url":"https://www.academia.edu/Documents/in/Platelet_function?f_ri=1816594","nofollow":true},{"id":627890,"name":"Blood Transfusion","url":"https://www.academia.edu/Documents/in/Blood_Transfusion?f_ri=1816594"},{"id":1028649,"name":"Thrombotic Thrombocytopenic Purpura","url":"https://www.academia.edu/Documents/in/Thrombotic_Thrombocytopenic_Purpura?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1831948,"name":"Adenosine Diphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Diphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_11753066 coauthored" data-work_id="11753066" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/11753066/Role_of_the_Transmembrane_Potential_in_the_Membrane_Proton_Leak">Role of the Transmembrane Potential in the Membrane Proton Leak</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The molecular mechanism responsible for the regulation of the mitochondrial membrane proton conductance (G) is not clearly understood. This study investigates the role of the transmembrane potential (DJ m ) using planar membranes,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_11753066" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The molecular mechanism responsible for the regulation of the mitochondrial membrane proton conductance (G) is not clearly understood. This study investigates the role of the transmembrane potential (DJ m ) using planar membranes, reconstituted with purified uncoupling proteins (UCP1 and UCP2) and/or unsaturated FA. We show that high DJ m (similar to DJ m in mitochondrial State IV) significantly activates the protonophoric function of UCPs in the presence of FA. The proton conductance increases nonlinearly with DJ m . The application of DJ m up to 220 mV leads to the overriding of the protein inhibition at a constant ATP concentration. Both, the exposure of FA-containing bilayers to high DJ m and the increase of FA membrane concentration bring about the significant exponential G m increase, implying the contribution of FA in proton leak. Quantitative analysis of the energy barrier for the transport of FA anions in the presence and absence of protein suggests that FA À remain exposed to membrane lipids while crossing the UCP-containing membrane. We believe this study shows that UCPs and FA decrease DJ m more effectively if it is sufficiently high. Thus, the tight regulation of proton conductance and/or FA concentration by DJ m may be key in mitochondrial respiration and metabolism.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/11753066" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="8bd14dba08efd675d60cce6df54fed9f" rel="nofollow" data-download="{"attachment_id":46544054,"asset_id":11753066,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46544054/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="28861763" href="https://independent.academia.edu/ValeriBeck">Valeri Beck</a><script data-card-contents-for-user="28861763" type="text/json">{"id":28861763,"first_name":"Valeri","last_name":"Beck","domain_name":"independent","page_name":"ValeriBeck","display_name":"Valeri Beck","profile_url":"https://independent.academia.edu/ValeriBeck?f_ri=1816594","photo":"https://0.academia-photos.com/28861763/20815221/20362331/s65_valeri.beck.jpg"}</script></span></span><span class="u-displayInlineBlock InlineList-item-text"> and <span class="u-textDecorationUnderline u-clickable InlineList-item-text js-work-more-authors-11753066">+2</span><div class="hidden js-additional-users-11753066"><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://independent.academia.edu/OlafNinnemann">Olaf Ninnemann</a></span></div><div><span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a href="https://vetmeduni.academia.edu/ElenaPohl">Elena Pohl</a></span></div></div></span><script>(function(){ var popoverSettings = { el: $('.js-work-more-authors-11753066'), placement: 'bottom', hide_delay: 200, html: true, content: function(){ return $('.js-additional-users-11753066').html(); 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This study investigates the role of the transmembrane potential (DJ m ) using planar membranes, reconstituted with purified uncoupling proteins (UCP1 and UCP2) and/or unsaturated FA. We show that high DJ m (similar to DJ m in mitochondrial State IV) significantly activates the protonophoric function of UCPs in the presence of FA. The proton conductance increases nonlinearly with DJ m . The application of DJ m up to 220 mV leads to the overriding of the protein inhibition at a constant ATP concentration. Both, the exposure of FA-containing bilayers to high DJ m and the increase of FA membrane concentration bring about the significant exponential G m increase, implying the contribution of FA in proton leak. Quantitative analysis of the energy barrier for the transport of FA anions in the presence and absence of protein suggests that FA À remain exposed to membrane lipids while crossing the UCP-containing membrane. We believe this study shows that UCPs and FA decrease DJ m more effectively if it is sufficiently high. Thus, the tight regulation of proton conductance and/or FA concentration by DJ m may be key in mitochondrial respiration and metabolism.","downloadable_attachments":[{"id":46544054,"asset_id":11753066,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":28861763,"first_name":"Valeri","last_name":"Beck","domain_name":"independent","page_name":"ValeriBeck","display_name":"Valeri Beck","profile_url":"https://independent.academia.edu/ValeriBeck?f_ri=1816594","photo":"https://0.academia-photos.com/28861763/20815221/20362331/s65_valeri.beck.jpg"},{"id":38176455,"first_name":"Olaf","last_name":"Ninnemann","domain_name":"independent","page_name":"OlafNinnemann","display_name":"Olaf Ninnemann","profile_url":"https://independent.academia.edu/OlafNinnemann?f_ri=1816594","photo":"/images/s65_no_pic.png"},{"id":14135489,"first_name":"Elena","last_name":"Pohl","domain_name":"vetmeduni","page_name":"ElenaPohl","display_name":"Elena Pohl","profile_url":"https://vetmeduni.academia.edu/ElenaPohl?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":5493,"name":"Nonlinear dynamics","url":"https://www.academia.edu/Documents/in/Nonlinear_dynamics?f_ri=1816594","nofollow":true},{"id":19156,"name":"Biophysical Chemistry","url":"https://www.academia.edu/Documents/in/Biophysical_Chemistry?f_ri=1816594","nofollow":true},{"id":31084,"name":"Ion Channels","url":"https://www.academia.edu/Documents/in/Ion_Channels?f_ri=1816594","nofollow":true},{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=1816594","nofollow":true},{"id":37434,"name":"Quantitative analysis","url":"https://www.academia.edu/Documents/in/Quantitative_analysis?f_ri=1816594"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594"},{"id":72314,"name":"Fatty acids","url":"https://www.academia.edu/Documents/in/Fatty_acids?f_ri=1816594"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice?f_ri=1816594"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=1816594"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=1816594"},{"id":486713,"name":"Fatty Acid","url":"https://www.academia.edu/Documents/in/Fatty_Acid?f_ri=1816594"},{"id":641216,"name":"Quantitative Analysis","url":"https://www.academia.edu/Documents/in/Quantitative_Analysis-1?f_ri=1816594"},{"id":669339,"name":"Mes","url":"https://www.academia.edu/Documents/in/Mes?f_ri=1816594"},{"id":1027866,"name":"SLS","url":"https://www.academia.edu/Documents/in/SLS?f_ri=1816594"},{"id":1137254,"name":"Hydrogen-Ion Concentration","url":"https://www.academia.edu/Documents/in/Hydrogen-Ion_Concentration?f_ri=1816594"},{"id":1161031,"name":"Uncoupling Protein","url":"https://www.academia.edu/Documents/in/Uncoupling_Protein?f_ri=1816594"},{"id":1202042,"name":"Electric Conductivity","url":"https://www.academia.edu/Documents/in/Electric_Conductivity?f_ri=1816594"},{"id":1208793,"name":"Protons","url":"https://www.academia.edu/Documents/in/Protons?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2445801,"name":"Mitochondrial Proteins","url":"https://www.academia.edu/Documents/in/Mitochondrial_Proteins?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_71445883" data-work_id="71445883" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/71445883/Role_of_ferredoxin_in_the_reductive_assimilation_of_CO2_and_acetate_by_extracts_of_the_photosynthetic_bacterium_Chromatium">Role of ferredoxin in the reductive assimilation of CO2 and acetate by extracts of the photosynthetic bacterium, Chromatium</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/71445883" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="7b07b022bcfd3f7b2884b856df429961" rel="nofollow" data-download="{"attachment_id":80785083,"asset_id":71445883,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/80785083/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="184843113" href="https://independent.academia.edu/RBachofen">Reinhard Bachofen</a><script data-card-contents-for-user="184843113" 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type="text/json">{"id":4594,"name":"Carbon Dioxide","url":"https://www.academia.edu/Documents/in/Carbon_Dioxide?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="5345" rel="nofollow" href="https://www.academia.edu/Documents/in/Photosynthesis">Photosynthesis</a>, <script data-card-contents-for-ri="5345" type="text/json">{"id":5345,"name":"Photosynthesis","url":"https://www.academia.edu/Documents/in/Photosynthesis?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="7710" rel="nofollow" href="https://www.academia.edu/Documents/in/Biology">Biology</a><script data-card-contents-for-ri="7710" type="text/json">{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=71445883]'), work: {"id":71445883,"title":"Role of ferredoxin in the reductive assimilation of CO2 and acetate by extracts of the photosynthetic bacterium, Chromatium","created_at":"2022-02-14T00:06:40.289-08:00","url":"https://www.academia.edu/71445883/Role_of_ferredoxin_in_the_reductive_assimilation_of_CO2_and_acetate_by_extracts_of_the_photosynthetic_bacterium_Chromatium?f_ri=1816594","dom_id":"work_71445883","summary":null,"downloadable_attachments":[{"id":80785083,"asset_id":71445883,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":184843113,"first_name":"Reinhard","last_name":"Bachofen","domain_name":"independent","page_name":"RBachofen","display_name":"Reinhard Bachofen","profile_url":"https://independent.academia.edu/RBachofen?f_ri=1816594","photo":"https://0.academia-photos.com/184843113/110578037/99826298/s65_reinhard.bachofen.jpeg"}],"research_interests":[{"id":3770,"name":"Metabolism","url":"https://www.academia.edu/Documents/in/Metabolism?f_ri=1816594","nofollow":true},{"id":4594,"name":"Carbon Dioxide","url":"https://www.academia.edu/Documents/in/Carbon_Dioxide?f_ri=1816594","nofollow":true},{"id":5345,"name":"Photosynthesis","url":"https://www.academia.edu/Documents/in/Photosynthesis?f_ri=1816594","nofollow":true},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology?f_ri=1816594","nofollow":true},{"id":19870,"name":"Research","url":"https://www.academia.edu/Documents/in/Research?f_ri=1816594"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=1816594"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary?f_ri=1816594"},{"id":158597,"name":"Iron","url":"https://www.academia.edu/Documents/in/Iron?f_ri=1816594"},{"id":1292672,"name":"Clostridium","url":"https://www.academia.edu/Documents/in/Clostridium?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":3450788,"name":"Chromatium","url":"https://www.academia.edu/Documents/in/Chromatium?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_34341616" data-work_id="34341616" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/34341616/Inhibition_of_energy_metabolism_alters_the_processing_of_amyloid_precursor_protein_and_induces_a_potentially_amyloidogenic_derivative">Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The cellular mechanisms which lead to the generation and pathological deposition of p amyloid in Alzheimer's disease are unknown. In this report we describe the proteolytic processing of the amyloid precursor protein (APP) to an 11.5-kDa... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_34341616" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The cellular mechanisms which lead to the generation and pathological deposition of p amyloid in Alzheimer's disease are unknown. In this report we describe the proteolytic processing of the amyloid precursor protein (APP) to an 11.5-kDa COOH-terminal derivative which contains the full-length fi amyloid sequence. This processing step normally occurs at low levels in parallel with APP maturation in the secretory pathway. Inhibition of oxidative energy metabolism by sodium azide or the mitochondrial uncoupler carbonyl cyanide m-chlorophenylhydrazone increased the proteolysis of APP to the 11.5-kDa derivative by about 80-fold with accumulation of this APP derivative in the Golgi complex. Agents which inhibit protein transport in the secretory pathway, including monensin and brefeldin A, also increased the production of the 11.5-kDa derivative. Inhibition of APP maturation demonstrated that the 11.5-kDa derivative could be produced by proteolysis of immature APP. These results demonstrate that APP processing to potentially amyloidogenic COOH-terminal derivatives occurs in either the endoplasmic reticulum or Golgi complex and can be modulated by the state of cellular energy metabolism. Deficits in oxidative energy metabolism have recently been found in the cerebral cortex of patients with Alzheimer's disease. These findings raise the possibility that energy-related metabolic stress may lead to altered metabolism of APP and contribute to amyloidosis in Alzheimer's disease.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/34341616" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="5c3d2a7942e55d01e0ae2ff1f442ee36" rel="nofollow" data-download="{"attachment_id":54235588,"asset_id":34341616,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/54235588/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="67566740" href="https://independent.academia.edu/JorgeBusciglio">Jorge Busciglio</a><script data-card-contents-for-user="67566740" type="text/json">{"id":67566740,"first_name":"Jorge","last_name":"Busciglio","domain_name":"independent","page_name":"JorgeBusciglio","display_name":"Jorge Busciglio","profile_url":"https://independent.academia.edu/JorgeBusciglio?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_34341616 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="34341616"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 34341616, container: ".js-paper-rank-work_34341616", }); 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$(".js-view-count[data-work-id=34341616]").text(description); $(".js-view-count-work_34341616").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_34341616").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="34341616"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">11</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="11035" rel="nofollow" href="https://www.academia.edu/Documents/in/Regulation">Regulation</a>, <script data-card-contents-for-ri="11035" type="text/json">{"id":11035,"name":"Regulation","url":"https://www.academia.edu/Documents/in/Regulation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="15719" rel="nofollow" href="https://www.academia.edu/Documents/in/Mitochondria">Mitochondria</a>, <script data-card-contents-for-ri="15719" type="text/json">{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="36213" rel="nofollow" href="https://www.academia.edu/Documents/in/Energy_Metabolism">Energy Metabolism</a>, <script data-card-contents-for-ri="36213" type="text/json">{"id":36213,"name":"Energy Metabolism","url":"https://www.academia.edu/Documents/in/Energy_Metabolism?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="40539" rel="nofollow" href="https://www.academia.edu/Documents/in/Amyloid">Amyloid</a><script data-card-contents-for-ri="40539" type="text/json">{"id":40539,"name":"Amyloid","url":"https://www.academia.edu/Documents/in/Amyloid?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=34341616]'), work: {"id":34341616,"title":"Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative","created_at":"2017-08-24T09:53:42.637-07:00","url":"https://www.academia.edu/34341616/Inhibition_of_energy_metabolism_alters_the_processing_of_amyloid_precursor_protein_and_induces_a_potentially_amyloidogenic_derivative?f_ri=1816594","dom_id":"work_34341616","summary":"The cellular mechanisms which lead to the generation and pathological deposition of p amyloid in Alzheimer's disease are unknown. In this report we describe the proteolytic processing of the amyloid precursor protein (APP) to an 11.5-kDa COOH-terminal derivative which contains the full-length fi amyloid sequence. This processing step normally occurs at low levels in parallel with APP maturation in the secretory pathway. Inhibition of oxidative energy metabolism by sodium azide or the mitochondrial uncoupler carbonyl cyanide m-chlorophenylhydrazone increased the proteolysis of APP to the 11.5-kDa derivative by about 80-fold with accumulation of this APP derivative in the Golgi complex. Agents which inhibit protein transport in the secretory pathway, including monensin and brefeldin A, also increased the production of the 11.5-kDa derivative. Inhibition of APP maturation demonstrated that the 11.5-kDa derivative could be produced by proteolysis of immature APP. These results demonstrate that APP processing to potentially amyloidogenic COOH-terminal derivatives occurs in either the endoplasmic reticulum or Golgi complex and can be modulated by the state of cellular energy metabolism. Deficits in oxidative energy metabolism have recently been found in the cerebral cortex of patients with Alzheimer's disease. These findings raise the possibility that energy-related metabolic stress may lead to altered metabolism of APP and contribute to amyloidosis in Alzheimer's disease.","downloadable_attachments":[{"id":54235588,"asset_id":34341616,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":67566740,"first_name":"Jorge","last_name":"Busciglio","domain_name":"independent","page_name":"JorgeBusciglio","display_name":"Jorge Busciglio","profile_url":"https://independent.academia.edu/JorgeBusciglio?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":11035,"name":"Regulation","url":"https://www.academia.edu/Documents/in/Regulation?f_ri=1816594","nofollow":true},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true},{"id":36213,"name":"Energy Metabolism","url":"https://www.academia.edu/Documents/in/Energy_Metabolism?f_ri=1816594","nofollow":true},{"id":40539,"name":"Amyloid","url":"https://www.academia.edu/Documents/in/Amyloid?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594"},{"id":117643,"name":"Biological","url":"https://www.academia.edu/Documents/in/Biological?f_ri=1816594"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=1816594"},{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis?f_ri=1816594"},{"id":1490737,"name":"Secretion","url":"https://www.academia.edu/Documents/in/Secretion?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2028686,"name":"Amyloid Beta Precursor Protein","url":"https://www.academia.edu/Documents/in/Amyloid_Beta_Precursor_Protein?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_29649984" data-work_id="29649984" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/29649984/The_molecular_mechanism_of_inhibition_of_alpha_type_DNA_polymerases_by_N_2_butylphenyl_dGTP_and_2_butylanilino_dATP_variation_in_susceptibility_to_polymerization">The molecular mechanism of inhibition of alpha-type DNA polymerases by N 2 -(butylphenyl)dGTP and 2-(butylanilino)dATP: variation in susceptibility to polymerization</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Inhibrtorprimer-template complex. Primer extension experiments using the guanine form as the model analog Indicated that pol a cannot utilize these nucleotides to extend primer termini. In contrast, pol T4 polymerized BuPdGTP, indicating... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_29649984" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Inhibrtorprimer-template complex. Primer extension experiments using the guanine form as the model analog Indicated that pol a cannot utilize these nucleotides to extend primer termini. In contrast, pol T4 polymerized BuPdGTP, indicating that resistance to polymerization is not a common feature of the inhibitor mechanism among the broad membership of the alpha polymerase family.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/29649984" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="fb886ed0cbfe9a780883c4c2bd3909cb" rel="nofollow" data-download="{"attachment_id":50085779,"asset_id":29649984,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/50085779/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="56081673" href="https://independent.academia.edu/NaseemaKhan4">Naseema Khan</a><script data-card-contents-for-user="56081673" type="text/json">{"id":56081673,"first_name":"Naseema","last_name":"Khan","domain_name":"independent","page_name":"NaseemaKhan4","display_name":"Naseema Khan","profile_url":"https://independent.academia.edu/NaseemaKhan4?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_29649984 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="29649984"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 29649984, container: ".js-paper-rank-work_29649984", }); 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$(".js-view-count[data-work-id=29649984]").text(description); $(".js-view-count-work_29649984").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_29649984").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="29649984"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="4987" rel="nofollow" href="https://www.academia.edu/Documents/in/Kinetics">Kinetics</a>, <script data-card-contents-for-ri="4987" type="text/json">{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="21466" rel="nofollow" href="https://www.academia.edu/Documents/in/Polymers">Polymers</a>, <script data-card-contents-for-ri="21466" type="text/json">{"id":21466,"name":"Polymers","url":"https://www.academia.edu/Documents/in/Polymers?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="32909" rel="nofollow" href="https://www.academia.edu/Documents/in/Polymerization">Polymerization</a>, <script data-card-contents-for-ri="32909" type="text/json">{"id":32909,"name":"Polymerization","url":"https://www.academia.edu/Documents/in/Polymerization?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="35637" rel="nofollow" href="https://www.academia.edu/Documents/in/Molecular_Mechanics">Molecular Mechanics</a><script data-card-contents-for-ri="35637" type="text/json">{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=29649984]'), work: {"id":29649984,"title":"The molecular mechanism of inhibition of alpha-type DNA polymerases by N 2 -(butylphenyl)dGTP and 2-(butylanilino)dATP: variation in susceptibility to polymerization","created_at":"2016-11-03T12:56:10.152-07:00","url":"https://www.academia.edu/29649984/The_molecular_mechanism_of_inhibition_of_alpha_type_DNA_polymerases_by_N_2_butylphenyl_dGTP_and_2_butylanilino_dATP_variation_in_susceptibility_to_polymerization?f_ri=1816594","dom_id":"work_29649984","summary":"Inhibrtorprimer-template complex. Primer extension experiments using the guanine form as the model analog Indicated that pol a cannot utilize these nucleotides to extend primer termini. In contrast, pol T4 polymerized BuPdGTP, indicating that resistance to polymerization is not a common feature of the inhibitor mechanism among the broad membership of the alpha polymerase family.","downloadable_attachments":[{"id":50085779,"asset_id":29649984,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":56081673,"first_name":"Naseema","last_name":"Khan","domain_name":"independent","page_name":"NaseemaKhan4","display_name":"Naseema Khan","profile_url":"https://independent.academia.edu/NaseemaKhan4?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=1816594","nofollow":true},{"id":21466,"name":"Polymers","url":"https://www.academia.edu/Documents/in/Polymers?f_ri=1816594","nofollow":true},{"id":32909,"name":"Polymerization","url":"https://www.academia.edu/Documents/in/Polymerization?f_ri=1816594","nofollow":true},{"id":35637,"name":"Molecular Mechanics","url":"https://www.academia.edu/Documents/in/Molecular_Mechanics?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594"},{"id":58054,"name":"Environmental Sciences","url":"https://www.academia.edu/Documents/in/Environmental_Sciences?f_ri=1816594"},{"id":172024,"name":"Analog","url":"https://www.academia.edu/Documents/in/Analog?f_ri=1816594"},{"id":178906,"name":"Nucleic Acids","url":"https://www.academia.edu/Documents/in/Nucleic_Acids?f_ri=1816594"},{"id":206988,"name":"NAR","url":"https://www.academia.edu/Documents/in/NAR?f_ri=1816594"},{"id":260829,"name":"Cattle","url":"https://www.academia.edu/Documents/in/Cattle?f_ri=1816594"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence?f_ri=1816594"},{"id":1581100,"name":"DNA Polymerase","url":"https://www.academia.edu/Documents/in/DNA_Polymerase?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2235833,"name":"Dna Synthesis","url":"https://www.academia.edu/Documents/in/Dna_Synthesis?f_ri=1816594"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_6073628" data-work_id="6073628" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/6073628/Bioluminometric_assay_of_ATP_in_mouse_brain_Determinant_factors_for_enhanced_test_sensitivity">Bioluminometric assay of ATP in mouse brain: Determinant factors for enhanced test sensitivity</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Firefly luciferase bioluminescence (FLB) is a highly sensitive and specific method for the analysis of adenosine-5-triphosphate (ATP) in biological samples. Earlier attempts to modify the FLB test for enhanced sensitivity have been... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_6073628" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Firefly luciferase bioluminescence (FLB) is a highly sensitive and specific method for the analysis of adenosine-5-triphosphate (ATP) in biological samples. Earlier attempts to modify the FLB test for enhanced sensitivity have been typically based onin vitro cell systems. This study reports an optimized FLB procedure for the analysis of ATP in small tissue samples. The results showed that the sensitivity of the FLB test can be enhanced several fold by using ultraturax homogenizer, perchloric acid extraction, neutralization of acid extract and its optimal dilution, before performing the assay reaction.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/6073628" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="b5de098ce9eda9c07dcf2b1519763395" rel="nofollow" data-download="{"attachment_id":49028958,"asset_id":6073628,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/49028958/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="313871" href="https://king-saud.academia.edu/DrHaseebAhmadKhan">Prof. Haseeb Ahmad Khan</a><script data-card-contents-for-user="313871" type="text/json">{"id":313871,"first_name":"Prof. Haseeb","last_name":"Ahmad Khan","domain_name":"king-saud","page_name":"DrHaseebAhmadKhan","display_name":"Prof. Haseeb Ahmad Khan","profile_url":"https://king-saud.academia.edu/DrHaseebAhmadKhan?f_ri=1816594","photo":"https://0.academia-photos.com/313871/15131376/15833093/s65_haseeb.ahmad_khan.jpg"}</script></span></span></li><li class="js-paper-rank-work_6073628 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="6073628"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 6073628, container: ".js-paper-rank-work_6073628", }); 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Earlier attempts to modify the FLB test for enhanced sensitivity have been typically based onin vitro cell systems. This study reports an optimized FLB procedure for the analysis of ATP in small tissue samples. The results showed that the sensitivity of the FLB test can be enhanced several fold by using ultraturax homogenizer, perchloric acid extraction, neutralization of acid extract and its optimal dilution, before performing the assay reaction.","downloadable_attachments":[{"id":49028958,"asset_id":6073628,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":313871,"first_name":"Prof. Haseeb","last_name":"Ahmad Khan","domain_name":"king-saud","page_name":"DrHaseebAhmadKhan","display_name":"Prof. Haseeb Ahmad Khan","profile_url":"https://king-saud.academia.edu/DrHaseebAhmadKhan?f_ri=1816594","photo":"https://0.academia-photos.com/313871/15131376/15833093/s65_haseeb.ahmad_khan.jpg"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological 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Ruiz","profile_url":"https://uca-es.academia.edu/FelixARuiz?f_ri=1816594","photo":"https://gravatar.com/avatar/4a6dd05e3d3dd130ef038e3d9d332bc0?s=65"}],"research_interests":[{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=1816594","nofollow":true},{"id":7700,"name":"Fluorescence Microscopy","url":"https://www.academia.edu/Documents/in/Fluorescence_Microscopy?f_ri=1816594","nofollow":true},{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":13346,"name":"Toxoplasma","url":"https://www.academia.edu/Documents/in/Toxoplasma?f_ri=1816594","nofollow":true},{"id":18520,"name":"Biological Chemistry","url":"https://www.academia.edu/Documents/in/Biological_Chemistry?f_ri=1816594"},{"id":37801,"name":"Toxoplasma gondii","url":"https://www.academia.edu/Documents/in/Toxoplasma_gondii?f_ri=1816594"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594"},{"id":48972,"name":"Organelles","url":"https://www.academia.edu/Documents/in/Organelles?f_ri=1816594"},{"id":117643,"name":"Biological","url":"https://www.academia.edu/Documents/in/Biological?f_ri=1816594"},{"id":122188,"name":"Cell Fractionation","url":"https://www.academia.edu/Documents/in/Cell_Fractionation?f_ri=1816594"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES?f_ri=1816594"},{"id":263252,"name":"Anions","url":"https://www.academia.edu/Documents/in/Anions?f_ri=1816594"},{"id":335984,"name":"Anti-Bacterial Agents","url":"https://www.academia.edu/Documents/in/Anti-Bacterial_Agents?f_ri=1816594"},{"id":376084,"name":"Trypanosoma Cruzi","url":"https://www.academia.edu/Documents/in/Trypanosoma_Cruzi?f_ri=1816594"},{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis?f_ri=1816594"},{"id":1109994,"name":"Diphosphates","url":"https://www.academia.edu/Documents/in/Diphosphates?f_ri=1816594"},{"id":1256875,"name":"Acids","url":"https://www.academia.edu/Documents/in/Acids?f_ri=1816594"},{"id":1335153,"name":"Acridine Orange","url":"https://www.academia.edu/Documents/in/Acridine_Orange?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2027577,"name":"Macrolides","url":"https://www.academia.edu/Documents/in/Macrolides?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_12321879" data-work_id="12321879" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/12321879/In_vitro_Characterization_of_Parasympathetic_and_Sympathetic_Responses_in_Cyclophosphamide_Induced_Cystitis_in_the_Rat">In vitro Characterization of Parasympathetic and Sympathetic Responses in Cyclophosphamide-Induced Cystitis in the Rat</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">In cyclophosphamide-induced cystitis in the rat, detrusor function is impaired and the expression and effects of muscarinic receptors altered. Whether or not the neuronal transmission may be affected by cystitis was presently... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_12321879" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">In cyclophosphamide-induced cystitis in the rat, detrusor function is impaired and the expression and effects of muscarinic receptors altered. Whether or not the neuronal transmission may be affected by cystitis was presently investigated. Responses of urinary strip preparations from control and cyclophosphamide-pretreated rats to electrical field stimulation and to agonists were assessed in the absence and presence of muscarinic, adrenergic and purinergic receptor antagonists. Generally, atropine reduced contractions, but in contrast to controls, it also reduced responses to low electrical field stimulation intensity (1-5 Hz) in inflamed preparations. In both types, purinoceptor desensitization with α , β -methylene adenosine-5'-triphosphate ( α , β -meATP) caused further reductions at low frequencies ( < 10 Hz). The muscarinic receptor antagonists atropine, 4-diphenylacetoxy-N -methylpiperidine (4-DAMP) ('M 1 /M 3 /M 5 -selective'), methoctramine ('M 2 -selective') and pirenzepine ('M 1 -selective') antagonized the tonic component of the electrical field stimulation-evoked contractile response more potently than the phasic component. 4-DAMP inhibited the tonic contractions in controls more potently than methoctramine and pirenzepine. In inflamed preparations, the muscarinic receptor antagonism on the phasic component of the electrical field stimulation-evoked contraction was decreased and the pirenzepine and 4-DAMP antagonism on the tonic component was much less efficient than in controls. In contrast to controls, methoctramine increased -instead of decreased -the tonic responses at high frequencies. While contractions to carbachol and ATP were the same in inflamed and in control strips when related to a reference potassium response, isoprenaline-induced relaxations were smaller in inflamed strips. Thus, in cystitis substantial changes of the efferent functional responses occur. While postjunctional β -adrenoceptor-mediated relaxations are reduced, effects by prejunctional inhibitory muscarinic receptors may be increased.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/12321879" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="9167f8358ab264d96504b4db5cd74a2e" rel="nofollow" data-download="{"attachment_id":46244018,"asset_id":12321879,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46244018/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="30967814" href="https://gu-se.academia.edu/GunnarTobin">Gunnar Tobin</a><script data-card-contents-for-user="30967814" type="text/json">{"id":30967814,"first_name":"Gunnar","last_name":"Tobin","domain_name":"gu-se","page_name":"GunnarTobin","display_name":"Gunnar Tobin","profile_url":"https://gu-se.academia.edu/GunnarTobin?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_12321879 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="12321879"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 12321879, container: ".js-paper-rank-work_12321879", }); 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$(".js-view-count[data-work-id=12321879]").text(description); $(".js-view-count-work_12321879").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_12321879").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="12321879"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">10</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="59370" rel="nofollow" href="https://www.academia.edu/Documents/in/In_Vitro">In Vitro</a>, <script data-card-contents-for-ri="59370" type="text/json">{"id":59370,"name":"In Vitro","url":"https://www.academia.edu/Documents/in/In_Vitro?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="375054" rel="nofollow" href="https://www.academia.edu/Documents/in/Rats">Rats</a>, <script data-card-contents-for-ri="375054" type="text/json">{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="417494" rel="nofollow" href="https://www.academia.edu/Documents/in/Rat">Rat</a>, <script data-card-contents-for-ri="417494" type="text/json">{"id":417494,"name":"Rat","url":"https://www.academia.edu/Documents/in/Rat?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="469030" rel="nofollow" href="https://www.academia.edu/Documents/in/Parasympatholytics">Parasympatholytics</a><script data-card-contents-for-ri="469030" type="text/json">{"id":469030,"name":"Parasympatholytics","url":"https://www.academia.edu/Documents/in/Parasympatholytics?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=12321879]'), work: {"id":12321879,"title":"In vitro Characterization of Parasympathetic and Sympathetic Responses in Cyclophosphamide-Induced Cystitis in the Rat","created_at":"2015-05-10T12:53:14.077-07:00","url":"https://www.academia.edu/12321879/In_vitro_Characterization_of_Parasympathetic_and_Sympathetic_Responses_in_Cyclophosphamide_Induced_Cystitis_in_the_Rat?f_ri=1816594","dom_id":"work_12321879","summary":"In cyclophosphamide-induced cystitis in the rat, detrusor function is impaired and the expression and effects of muscarinic receptors altered. Whether or not the neuronal transmission may be affected by cystitis was presently investigated. Responses of urinary strip preparations from control and cyclophosphamide-pretreated rats to electrical field stimulation and to agonists were assessed in the absence and presence of muscarinic, adrenergic and purinergic receptor antagonists. Generally, atropine reduced contractions, but in contrast to controls, it also reduced responses to low electrical field stimulation intensity (1-5 Hz) in inflamed preparations. In both types, purinoceptor desensitization with α , β -methylene adenosine-5'-triphosphate ( α , β -meATP) caused further reductions at low frequencies ( \u003c 10 Hz). The muscarinic receptor antagonists atropine, 4-diphenylacetoxy-N -methylpiperidine (4-DAMP) ('M 1 /M 3 /M 5 -selective'), methoctramine ('M 2 -selective') and pirenzepine ('M 1 -selective') antagonized the tonic component of the electrical field stimulation-evoked contractile response more potently than the phasic component. 4-DAMP inhibited the tonic contractions in controls more potently than methoctramine and pirenzepine. In inflamed preparations, the muscarinic receptor antagonism on the phasic component of the electrical field stimulation-evoked contraction was decreased and the pirenzepine and 4-DAMP antagonism on the tonic component was much less efficient than in controls. In contrast to controls, methoctramine increased -instead of decreased -the tonic responses at high frequencies. While contractions to carbachol and ATP were the same in inflamed and in control strips when related to a reference potassium response, isoprenaline-induced relaxations were smaller in inflamed strips. Thus, in cystitis substantial changes of the efferent functional responses occur. While postjunctional β -adrenoceptor-mediated relaxations are reduced, effects by prejunctional inhibitory muscarinic receptors may be increased.","downloadable_attachments":[{"id":46244018,"asset_id":12321879,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":30967814,"first_name":"Gunnar","last_name":"Tobin","domain_name":"gu-se","page_name":"GunnarTobin","display_name":"Gunnar Tobin","profile_url":"https://gu-se.academia.edu/GunnarTobin?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":59370,"name":"In Vitro","url":"https://www.academia.edu/Documents/in/In_Vitro?f_ri=1816594","nofollow":true},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594","nofollow":true},{"id":417494,"name":"Rat","url":"https://www.academia.edu/Documents/in/Rat?f_ri=1816594","nofollow":true},{"id":469030,"name":"Parasympatholytics","url":"https://www.academia.edu/Documents/in/Parasympatholytics?f_ri=1816594","nofollow":true},{"id":556021,"name":"Muscle contraction","url":"https://www.academia.edu/Documents/in/Muscle_contraction?f_ri=1816594"},{"id":719379,"name":"Propranolol","url":"https://www.academia.edu/Documents/in/Propranolol?f_ri=1816594"},{"id":1198588,"name":"Cyclophosphamide","url":"https://www.academia.edu/Documents/in/Cyclophosphamide?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1880638,"name":"Piperidines","url":"https://www.academia.edu/Documents/in/Piperidines?f_ri=1816594"},{"id":1902592,"name":"Urinary Bladder","url":"https://www.academia.edu/Documents/in/Urinary_Bladder?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_12575120" data-work_id="12575120" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/12575120/Encapsulation_metabolism_and_release_of_2_fluoro_ara_AMP_from_human_erythrocytes">Encapsulation, metabolism and release of 2-fluoro-ara-AMP from human erythrocytes</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">2-Fluoro-ara-AMP (fludarabine phosphate) is a purine analogue with anti-neoplastic activity in lymphoproliferative malignancies. Fludarabine phosphate activity and toxicity is schedule-dependent; multiple daily administrations (for five... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_12575120" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">2-Fluoro-ara-AMP (fludarabine phosphate) is a purine analogue with anti-neoplastic activity in lymphoproliferative malignancies. Fludarabine phosphate activity and toxicity is schedule-dependent; multiple daily administrations (for five days) are more effective than single dose. We have encapsulated fludarabine phosphate in human erythrocytes and found that it is slowly released as fludarabine for more than four days. Encapsulated fludarabine phosphate does not affect erythrocyte metabolism and is rapidly converted by erythrocyte enzymes both to fludarabine with a K m of 0.4 mM and a Vma x of 20 nmol/min per g hemoglobin and to fludarabine diphosphate and triphosphate. The apparent K m for fludarabine monophosphate in the phosphorylation reaction was 0.4 mM and the Vma x 40 nmol/min per g hemoglobin. In the phosphorylation of 2-fluoro-ara-AMP to the di-and triphosphate derivatives, ATP was the phosphate donor with apparent K m of 0.12 and 1.0 mM, respectively. During incubations of 2-fluoro-ara-AMP-loaded erythrocytes at 37°C fludarabine was found in equilibrium between the erythrocyte and the culture medium suggesting that permeation of the erythrocyte membrane is not rate-limiting. Thus, fludarabine phosphate-loaded erythrocytes might be used as a slow-delivery system for fludarabine administration in the treatment of lymphoid malignancies.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/12575120" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="48acaca4b448aa8e6690c9b5c774ebae" rel="nofollow" data-download="{"attachment_id":46078002,"asset_id":12575120,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/46078002/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="31502666" href="https://independent.academia.edu/MauroMagnani2">Mauro Magnani</a><script data-card-contents-for-user="31502666" type="text/json">{"id":31502666,"first_name":"Mauro","last_name":"Magnani","domain_name":"independent","page_name":"MauroMagnani2","display_name":"Mauro Magnani","profile_url":"https://independent.academia.edu/MauroMagnani2?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_12575120 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="12575120"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 12575120, container: ".js-paper-rank-work_12575120", }); 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Fludarabine phosphate activity and toxicity is schedule-dependent; multiple daily administrations (for five days) are more effective than single dose. We have encapsulated fludarabine phosphate in human erythrocytes and found that it is slowly released as fludarabine for more than four days. Encapsulated fludarabine phosphate does not affect erythrocyte metabolism and is rapidly converted by erythrocyte enzymes both to fludarabine with a K m of 0.4 mM and a Vma x of 20 nmol/min per g hemoglobin and to fludarabine diphosphate and triphosphate. The apparent K m for fludarabine monophosphate in the phosphorylation reaction was 0.4 mM and the Vma x 40 nmol/min per g hemoglobin. In the phosphorylation of 2-fluoro-ara-AMP to the di-and triphosphate derivatives, ATP was the phosphate donor with apparent K m of 0.12 and 1.0 mM, respectively. During incubations of 2-fluoro-ara-AMP-loaded erythrocytes at 37°C fludarabine was found in equilibrium between the erythrocyte and the culture medium suggesting that permeation of the erythrocyte membrane is not rate-limiting. Thus, fludarabine phosphate-loaded erythrocytes might be used as a slow-delivery system for fludarabine administration in the treatment of lymphoid malignancies.","downloadable_attachments":[{"id":46078002,"asset_id":12575120,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":31502666,"first_name":"Mauro","last_name":"Magnani","domain_name":"independent","page_name":"MauroMagnani2","display_name":"Mauro Magnani","profile_url":"https://independent.academia.edu/MauroMagnani2?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":4987,"name":"Kinetics","url":"https://www.academia.edu/Documents/in/Kinetics?f_ri=1816594","nofollow":true},{"id":20799,"name":"Drug Delivery System","url":"https://www.academia.edu/Documents/in/Drug_Delivery_System?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=1816594","nofollow":true},{"id":159187,"name":"Drug Delivery Systems","url":"https://www.academia.edu/Documents/in/Drug_Delivery_Systems?f_ri=1816594"},{"id":172083,"name":"Phosphorylation","url":"https://www.academia.edu/Documents/in/Phosphorylation?f_ri=1816594"},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme?f_ri=1816594"},{"id":421276,"name":"Delivery System","url":"https://www.academia.edu/Documents/in/Delivery_System?f_ri=1816594"},{"id":982534,"name":"Erythrocytes","url":"https://www.academia.edu/Documents/in/Erythrocytes?f_ri=1816594"},{"id":1031068,"name":"Drug Carriers","url":"https://www.academia.edu/Documents/in/Drug_Carriers?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1831948,"name":"Adenosine Diphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Diphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_12994821" data-work_id="12994821" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/12994821/Metabolic_aspects_of_phosphate_replacement_therapy_for_hypophosphatemia_after_renal_transplantation_Impact_on_muscular_phosphate_content_mineral_metabolism_and_acid_base_homeostasis">Metabolic aspects of phosphate replacement therapy for hypophosphatemia after renal transplantation: Impact on muscular phosphate content, mineral metabolism, and acid/base homeostasis</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Hypophosphatemia caused by renal phosphate loss occurs frequently after kidney transplantation. In assumption of systemic phosphorus depletion, the presumed deficit commonly is replaced by oral phosphate supplements. However, such... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_12994821" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Hypophosphatemia caused by renal phosphate loss occurs frequently after kidney transplantation. In assumption of systemic phosphorus depletion, the presumed deficit commonly is replaced by oral phosphate supplements. However, such treatment is debatable, because intracellular phosphorus stores have not been assessed in this setting and may not be accurately reflected by serum phosphate concentrations. Moreover, disturbances in mineral metabolism from chronic renal failure, such as hypocalcemia and hyperparathyroidism, may be prolonged with oral phosphate supplements. Conversely, a neutral phosphate salt might improve renal acid excretion and systemic acid/base homeostasis for its properties as a urinary buffer and a poorly reabsorbable anion. Twenty-eight patients with mild early posttransplantation hypophosphatemia (0.3-0.75 mmol/L) were randomly assigned to receive either neutral sodium phosphate (Na 2 HPO 4 ) or sodium chloride (NaCl) for 12 weeks and examined with regard to (1) correction of serum phosphate concentration and urinary phosphate handling; (2) muscular phosphate content; (3) serum calcium and parathyroid hormone (PTH); and, (4) renal acid handling and systemic acid/base homeostasis. Mean serum phosphate concentrations were similar and normal in both groups after 12 weeks of treatment; however, more patients in the NaCl group remained hypophosphatemic (93% versus 67%). Total muscular phosphorus content did not correlate with serum phosphate concentrations and was 25% below normophosphatemic controls but was completely restored after 12 weeks with and without phosphate supplementation. However, the percentage of the energy-rich phosphorus compound adenosine triphosphate (ATP) was significantly higher in the Na 2 HPO 4 group, as was the relative content of phosphodiesters. Also, compensated metabolic acidosis (hypobicarbonatemia with respiratory stimulation) was detected in most patients, which was significantly improved by neutral phosphate supplements through increased urinary titratable acidity. These benefits of added phosphate intake were not associated with any adverse effects on serum calcium and PTH concentrations. In conclusion, oral supplementation with a neutral phosphate salt effectively corrects posttransplantation hypophosphatemia, increases muscular ATP and phosphodiester content without affecting mineral metabolism, and improves renal acid excretion and systemic acid/base status. 1999 by the National Kidney Foundation, Inc. INDEX WORDS: Hypophosphatemia; renal transplantation; renal phosphate handling; muscular phosphate content; parathyroid hormone; calcium; acid/base homeostasis.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/12994821" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="94e2a2819f853fc5f39df5746b540d4c" rel="nofollow" data-download="{"attachment_id":45792657,"asset_id":12994821,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45792657/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32199075" href="https://independent.academia.edu/UlrikeDydak">Ulrike Dydak</a><script data-card-contents-for-user="32199075" type="text/json">{"id":32199075,"first_name":"Ulrike","last_name":"Dydak","domain_name":"independent","page_name":"UlrikeDydak","display_name":"Ulrike Dydak","profile_url":"https://independent.academia.edu/UlrikeDydak?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_12994821 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="12994821"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 12994821, container: ".js-paper-rank-work_12994821", }); 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In assumption of systemic phosphorus depletion, the presumed deficit commonly is replaced by oral phosphate supplements. However, such treatment is debatable, because intracellular phosphorus stores have not been assessed in this setting and may not be accurately reflected by serum phosphate concentrations. Moreover, disturbances in mineral metabolism from chronic renal failure, such as hypocalcemia and hyperparathyroidism, may be prolonged with oral phosphate supplements. Conversely, a neutral phosphate salt might improve renal acid excretion and systemic acid/base homeostasis for its properties as a urinary buffer and a poorly reabsorbable anion. Twenty-eight patients with mild early posttransplantation hypophosphatemia (0.3-0.75 mmol/L) were randomly assigned to receive either neutral sodium phosphate (Na 2 HPO 4 ) or sodium chloride (NaCl) for 12 weeks and examined with regard to (1) correction of serum phosphate concentration and urinary phosphate handling; (2) muscular phosphate content; (3) serum calcium and parathyroid hormone (PTH); and, (4) renal acid handling and systemic acid/base homeostasis. Mean serum phosphate concentrations were similar and normal in both groups after 12 weeks of treatment; however, more patients in the NaCl group remained hypophosphatemic (93% versus 67%). Total muscular phosphorus content did not correlate with serum phosphate concentrations and was 25% below normophosphatemic controls but was completely restored after 12 weeks with and without phosphate supplementation. However, the percentage of the energy-rich phosphorus compound adenosine triphosphate (ATP) was significantly higher in the Na 2 HPO 4 group, as was the relative content of phosphodiesters. Also, compensated metabolic acidosis (hypobicarbonatemia with respiratory stimulation) was detected in most patients, which was significantly improved by neutral phosphate supplements through increased urinary titratable acidity. These benefits of added phosphate intake were not associated with any adverse effects on serum calcium and PTH concentrations. In conclusion, oral supplementation with a neutral phosphate salt effectively corrects posttransplantation hypophosphatemia, increases muscular ATP and phosphodiester content without affecting mineral metabolism, and improves renal acid excretion and systemic acid/base status. 1999 by the National Kidney Foundation, Inc. INDEX WORDS: Hypophosphatemia; renal transplantation; renal phosphate handling; muscular phosphate content; parathyroid hormone; calcium; acid/base homeostasis.","downloadable_attachments":[{"id":45792657,"asset_id":12994821,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32199075,"first_name":"Ulrike","last_name":"Dydak","domain_name":"independent","page_name":"UlrikeDydak","display_name":"Ulrike Dydak","profile_url":"https://independent.academia.edu/UlrikeDydak?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":4228,"name":"Skeletal muscle biology","url":"https://www.academia.edu/Documents/in/Skeletal_muscle_biology?f_ri=1816594","nofollow":true},{"id":9003,"name":"Kidney transplantation","url":"https://www.academia.edu/Documents/in/Kidney_transplantation?f_ri=1816594","nofollow":true},{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":12426,"name":"Treatment Outcome","url":"https://www.academia.edu/Documents/in/Treatment_Outcome?f_ri=1816594","nofollow":true},{"id":53108,"name":"Phosphorus","url":"https://www.academia.edu/Documents/in/Phosphorus?f_ri=1816594"},{"id":58379,"name":"Renal transplantation","url":"https://www.academia.edu/Documents/in/Renal_transplantation?f_ri=1816594"},{"id":151448,"name":"American","url":"https://www.academia.edu/Documents/in/American?f_ri=1816594"},{"id":203383,"name":"Parathyroid Hormone","url":"https://www.academia.edu/Documents/in/Parathyroid_Hormone?f_ri=1816594"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594"},{"id":290332,"name":"Chronic Renal Failure","url":"https://www.academia.edu/Documents/in/Chronic_Renal_Failure?f_ri=1816594"},{"id":379033,"name":"Kidney Transplant","url":"https://www.academia.edu/Documents/in/Kidney_Transplant?f_ri=1816594"},{"id":379889,"name":"Homeostasis","url":"https://www.academia.edu/Documents/in/Homeostasis?f_ri=1816594"},{"id":541785,"name":"Phosphates","url":"https://www.academia.edu/Documents/in/Phosphates?f_ri=1816594"},{"id":612864,"name":"Metabolic Acidosis","url":"https://www.academia.edu/Documents/in/Metabolic_Acidosis?f_ri=1816594"},{"id":1223913,"name":"Sodium Chloride","url":"https://www.academia.edu/Documents/in/Sodium_Chloride?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1832259,"name":"Titratable acidity","url":"https://www.academia.edu/Documents/in/Titratable_acidity?f_ri=1816594"},{"id":2045642,"name":"Acid-Base Equilibrium","url":"https://www.academia.edu/Documents/in/Acid-Base_Equilibrium?f_ri=1816594"},{"id":2209628,"name":"Hypophosphatemia","url":"https://www.academia.edu/Documents/in/Hypophosphatemia?f_ri=1816594"},{"id":2463621,"name":"Postoperative Complications","url":"https://www.academia.edu/Documents/in/Postoperative_Complications?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_23518232" data-work_id="23518232" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/23518232/Calcium_and_mitochondria_mechanisms_and_functions_of_a_troubled_relationship">Calcium and mitochondria: mechanisms and functions of a troubled relationship</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Mitochondria promptly respond to Ca 2+ -mediated cell stimulations with a rapid accumulation of the cation into the matrix. In this article, we review (i) the basic principles of mitochondrial Ca 2+ transport, (ii) the... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_23518232" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Mitochondria promptly respond to Ca 2+ -mediated cell stimulations with a rapid accumulation of the cation into the matrix. In this article, we review (i) the basic principles of mitochondrial Ca 2+ transport, (ii) the physiological/pathological role of mitochondrial Ca 2+ uptake, (iii) the regulatory mechanisms that may operate in vivo, and (iv) the new targeted Ca 2+ probes that allowed the brediscoveryQ of these organelles in calcium signalling. D</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/23518232" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="cd526cd404aad85cd0d91bdce501f8ab" rel="nofollow" data-download="{"attachment_id":43953842,"asset_id":23518232,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/43953842/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="45533806" href="https://unifueu.academia.edu/ARimessi">A. Rimessi</a><script data-card-contents-for-user="45533806" type="text/json">{"id":45533806,"first_name":"A.","last_name":"Rimessi","domain_name":"unifueu","page_name":"ARimessi","display_name":"A. 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In this article, we review (i) the basic principles of mitochondrial Ca 2+ transport, (ii) the physiological/pathological role of mitochondrial Ca 2+ uptake, (iii) the regulatory mechanisms that may operate in vivo, and (iv) the new targeted Ca 2+ probes that allowed the brediscoveryQ of these organelles in calcium signalling. D","downloadable_attachments":[{"id":43953842,"asset_id":23518232,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":45533806,"first_name":"A.","last_name":"Rimessi","domain_name":"unifueu","page_name":"ARimessi","display_name":"A. Rimessi","profile_url":"https://unifueu.academia.edu/ARimessi?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":6947,"name":"Medical Microbiology","url":"https://www.academia.edu/Documents/in/Medical_Microbiology?f_ri=1816594","nofollow":true},{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true},{"id":58382,"name":"Calcium Signalling","url":"https://www.academia.edu/Documents/in/Calcium_Signalling?f_ri=1816594"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=1816594"},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=1816594"},{"id":815023,"name":"Ion Transport","url":"https://www.academia.edu/Documents/in/Ion_Transport?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_21124444" data-work_id="21124444" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/21124444/Changes_in_gut_function_during_hibernation_implications_for_bowel_transplantation_and_surgery">Changes in gut function during hibernation: implications for bowel transplantation and surgery</a></div></div><div class="u-pb4x u-mt3x"></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/21124444" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="2bc5d8322d38099cae95972cbe5eca07" rel="nofollow" data-download="{"attachment_id":41725672,"asset_id":21124444,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/41725672/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33164933" href="https://vcu.academia.edu/MartinMangino">Martin Mangino</a><script data-card-contents-for-user="33164933" type="text/json">{"id":33164933,"first_name":"Martin","last_name":"Mangino","domain_name":"vcu","page_name":"MartinMangino","display_name":"Martin Mangino","profile_url":"https://vcu.academia.edu/MartinMangino?f_ri=1816594","photo":"https://0.academia-photos.com/33164933/9835133/35851978/s65_martin.mangino.jpg"}</script></span></span></li><li class="js-paper-rank-work_21124444 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="21124444"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 21124444, container: ".js-paper-rank-work_21124444", }); 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$(".js-view-count[data-work-id=21124444]").text(description); $(".js-view-count-work_21124444").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_21124444").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="21124444"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">9</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="19295" rel="nofollow" href="https://www.academia.edu/Documents/in/Cryopreservation">Cryopreservation</a>, <script data-card-contents-for-ri="19295" type="text/json">{"id":19295,"name":"Cryopreservation","url":"https://www.academia.edu/Documents/in/Cryopreservation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="45304" rel="nofollow" href="https://www.academia.edu/Documents/in/Hibernation">Hibernation</a>, <script data-card-contents-for-ri="45304" type="text/json">{"id":45304,"name":"Hibernation","url":"https://www.academia.edu/Documents/in/Hibernation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="123418" rel="nofollow" href="https://www.academia.edu/Documents/in/NF-kappa_B">NF-kappa B</a>, <script data-card-contents-for-ri="123418" type="text/json">{"id":123418,"name":"NF-kappa B","url":"https://www.academia.edu/Documents/in/NF-kappa_B?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="244814" rel="nofollow" href="https://www.academia.edu/Documents/in/Clinical_Sciences">Clinical Sciences</a><script data-card-contents-for-ri="244814" type="text/json">{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=21124444]'), work: {"id":21124444,"title":"Changes in gut function during hibernation: implications for bowel transplantation and surgery","created_at":"2016-01-29T04:54:45.242-08:00","url":"https://www.academia.edu/21124444/Changes_in_gut_function_during_hibernation_implications_for_bowel_transplantation_and_surgery?f_ri=1816594","dom_id":"work_21124444","summary":null,"downloadable_attachments":[{"id":41725672,"asset_id":21124444,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33164933,"first_name":"Martin","last_name":"Mangino","domain_name":"vcu","page_name":"MartinMangino","display_name":"Martin Mangino","profile_url":"https://vcu.academia.edu/MartinMangino?f_ri=1816594","photo":"https://0.academia-photos.com/33164933/9835133/35851978/s65_martin.mangino.jpg"}],"research_interests":[{"id":19295,"name":"Cryopreservation","url":"https://www.academia.edu/Documents/in/Cryopreservation?f_ri=1816594","nofollow":true},{"id":45304,"name":"Hibernation","url":"https://www.academia.edu/Documents/in/Hibernation?f_ri=1816594","nofollow":true},{"id":123418,"name":"NF-kappa B","url":"https://www.academia.edu/Documents/in/NF-kappa_B?f_ri=1816594","nofollow":true},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594","nofollow":true},{"id":291136,"name":"Intestines","url":"https://www.academia.edu/Documents/in/Intestines?f_ri=1816594"},{"id":376494,"name":"Epithelium","url":"https://www.academia.edu/Documents/in/Epithelium?f_ri=1816594"},{"id":537750,"name":"Gut","url":"https://www.academia.edu/Documents/in/Gut?f_ri=1816594"},{"id":794984,"name":"Reperfusion injury","url":"https://www.academia.edu/Documents/in/Reperfusion_injury?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_20009795" data-work_id="20009795" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/20009795/Biochemical_and_Structural_Studies_of_the_Interaction_of_Cdc37_with_Hsp90">Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The heat shock protein Hsp90 plays a key, but poorly understood role in the folding, assembly and activation of a large number of signal transduction molecules, in particular kinases and steroid hormone receptors. In carrying out these... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_20009795" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The heat shock protein Hsp90 plays a key, but poorly understood role in the folding, assembly and activation of a large number of signal transduction molecules, in particular kinases and steroid hormone receptors. In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP-and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones. Cdc37 is one such co-chaperone protein that also has a role in client protein recognition, in that it is required for Hsp90-dependent folding and activation of a particular group of protein kinases. These include the cyclin-dependent kinases (Cdk) 4/6 and Cdk9, Raf-1, Akt and many others. Here, the biochemical details of the interaction of human Hsp90b and Cdc37 have been characterised. Small angle X-ray scattering (SAXS) was then used to study the solution structure of Hsp90 and its complexes with Cdc37. The results suggest a model for the interaction of Cdc37 with Hsp90, whereby a Cdc37 dimer binds the two N-terminal domain/linker regions in an Hsp90 dimer, fixing them in a single conformation that is presumably suitable for client protein recognition.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/20009795" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c7b4cb1876c8f54bf58afa0d9b6e604b" rel="nofollow" data-download="{"attachment_id":40955303,"asset_id":20009795,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/40955303/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="40915110" href="https://independent.academia.edu/MiriamHirshberg">Miriam Hirshberg</a><script data-card-contents-for-user="40915110" type="text/json">{"id":40915110,"first_name":"Miriam","last_name":"Hirshberg","domain_name":"independent","page_name":"MiriamHirshberg","display_name":"Miriam Hirshberg","profile_url":"https://independent.academia.edu/MiriamHirshberg?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_20009795 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="20009795"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 20009795, container: ".js-paper-rank-work_20009795", }); 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In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP-and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones. Cdc37 is one such co-chaperone protein that also has a role in client protein recognition, in that it is required for Hsp90-dependent folding and activation of a particular group of protein kinases. These include the cyclin-dependent kinases (Cdk) 4/6 and Cdk9, Raf-1, Akt and many others. Here, the biochemical details of the interaction of human Hsp90b and Cdc37 have been characterised. Small angle X-ray scattering (SAXS) was then used to study the solution structure of Hsp90 and its complexes with Cdc37. The results suggest a model for the interaction of Cdc37 with Hsp90, whereby a Cdc37 dimer binds the two N-terminal domain/linker regions in an Hsp90 dimer, fixing them in a single conformation that is presumably suitable for client protein recognition.","downloadable_attachments":[{"id":40955303,"asset_id":20009795,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":40915110,"first_name":"Miriam","last_name":"Hirshberg","domain_name":"independent","page_name":"MiriamHirshberg","display_name":"Miriam Hirshberg","profile_url":"https://independent.academia.edu/MiriamHirshberg?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology?f_ri=1816594","nofollow":true},{"id":10636,"name":"Small Angle X Ray Scattering","url":"https://www.academia.edu/Documents/in/Small_Angle_X_Ray_Scattering?f_ri=1816594","nofollow":true},{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=1816594","nofollow":true},{"id":48981,"name":"Molecular chaperones","url":"https://www.academia.edu/Documents/in/Molecular_chaperones?f_ri=1816594","nofollow":true},{"id":50157,"name":"Molecular","url":"https://www.academia.edu/Documents/in/Molecular?f_ri=1816594"},{"id":50487,"name":"Protein-Protein Interaction","url":"https://www.academia.edu/Documents/in/Protein-Protein_Interaction?f_ri=1816594"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli?f_ri=1816594"},{"id":96893,"name":"Calibration","url":"https://www.academia.edu/Documents/in/Calibration?f_ri=1816594"},{"id":151086,"name":"Peptides","url":"https://www.academia.edu/Documents/in/Peptides?f_ri=1816594"},{"id":162983,"name":"Absorption","url":"https://www.academia.edu/Documents/in/Absorption?f_ri=1816594"},{"id":193464,"name":"Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis","url":"https://www.academia.edu/Documents/in/Sodium_Dodecyl_Sulfate-Polyacrylamide_Gel_Electrophoresis?f_ri=1816594"},{"id":386527,"name":"X ray diffraction","url":"https://www.academia.edu/Documents/in/X_ray_diffraction?f_ri=1816594"},{"id":414692,"name":"Solutions","url":"https://www.academia.edu/Documents/in/Solutions?f_ri=1816594"},{"id":457191,"name":"Analytical Ultracentrifugation","url":"https://www.academia.edu/Documents/in/Analytical_Ultracentrifugation?f_ri=1816594"},{"id":577933,"name":"Genetic variation","url":"https://www.academia.edu/Documents/in/Genetic_variation?f_ri=1816594"},{"id":736136,"name":"Protein Kinase","url":"https://www.academia.edu/Documents/in/Protein_Kinase?f_ri=1816594"},{"id":765872,"name":"Heat Shock Protein","url":"https://www.academia.edu/Documents/in/Heat_Shock_Protein?f_ri=1816594"},{"id":983317,"name":"Cell Cycle Proteins","url":"https://www.academia.edu/Documents/in/Cell_Cycle_Proteins?f_ri=1816594"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=1816594"},{"id":1311550,"name":"Size Exclusion Chromatography","url":"https://www.academia.edu/Documents/in/Size_Exclusion_Chromatography?f_ri=1816594"},{"id":1333505,"name":"Solution Structure","url":"https://www.academia.edu/Documents/in/Solution_Structure?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1809037,"name":"Dimerization","url":"https://www.academia.edu/Documents/in/Dimerization?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2229576,"name":"Chaperonins","url":"https://www.academia.edu/Documents/in/Chaperonins?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_81930247" data-work_id="81930247" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/81930247/A_macrophage_mediated_factor_that_increases_the_high_energy_phosphate_content_of_skeletal_muscle">A macrophage-mediated factor that increases the high energy phosphate content of skeletal muscle</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A marked cellular infiltrate accompanies wounding. The phagocytic and bacteriocidal activities of this infiltrate require increased substrate and Or consumption. This rapid utilization of available oxygen and substrates could jeopardize... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_81930247" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A marked cellular infiltrate accompanies wounding. The phagocytic and bacteriocidal activities of this infiltrate require increased substrate and Or consumption. This rapid utilization of available oxygen and substrates could jeopardize an already compromised resident cellular component of a wound. Recent studies have demonstrated macrophage-mediated cell stimulatoty agents which induce proliferation of nonlymphoid mesenchymal cells. This study was designed to examine macrophageresident tissue interactions and their possible significance in wounded tissue. A reconstituted wound system was designed which combines the major components of a X-carrageenan skeletal muscle wound (muscle + macrophages). The extensor digitorum longi (EDL) of male Fisher rats were incubated in a standardized fashion [ 121. The groups of EDL were muscle incubated alone, muscle with the addition to the incubate of activated peritoneal macrophages or muscle with the addition of a conditioned supematant from the incubation of activated or nonactivated peritonal macrophages. Muscle ATP and CP content were noted to be increased 46 and 22%, respectively, when macrophages and skeletal muscle were coincubated. Macrophage-conditioned media from activated or nonactivated macrophages increased the ATP and CP muscle content 44 and 37%, respectively. Preliminary characterization of this high energy phosphate (HEP) promoting factor demonstrates it to be heat and cold stable and less than 10,000 Da. Therefore, a macrophage-mediated transferable factor is capable of increasing the HEP content of skeletal muscle in an in vitro system. This may have important consequences in maintaining host Cell integrity fOliOWing injury. 0 1985 Academic press, IX.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/81930247" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="d7cec4e0274af9bd8fbf1f8ce2e892b1" rel="nofollow" data-download="{"attachment_id":87801829,"asset_id":81930247,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/87801829/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="13700988" href="https://biola.academia.edu/MichaelCaldwell">Michael D Caldwell</a><script data-card-contents-for-user="13700988" type="text/json">{"id":13700988,"first_name":"Michael","last_name":"Caldwell","domain_name":"biola","page_name":"MichaelCaldwell","display_name":"Michael D Caldwell","profile_url":"https://biola.academia.edu/MichaelCaldwell?f_ri=1816594","photo":"https://0.academia-photos.com/13700988/10253409/11442729/s65_michael.caldwell.jpg_oh_2883624ff38d8b0815ee11cfaae40edc_oe_56abebcb___gda___1452888307_b4566e5d0fb3359e122fb06084e7d3cf"}</script></span></span></li><li class="js-paper-rank-work_81930247 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="81930247"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 81930247, container: ".js-paper-rank-work_81930247", }); 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The phagocytic and bacteriocidal activities of this infiltrate require increased substrate and Or consumption. This rapid utilization of available oxygen and substrates could jeopardize an already compromised resident cellular component of a wound. Recent studies have demonstrated macrophage-mediated cell stimulatoty agents which induce proliferation of nonlymphoid mesenchymal cells. This study was designed to examine macrophageresident tissue interactions and their possible significance in wounded tissue. A reconstituted wound system was designed which combines the major components of a X-carrageenan skeletal muscle wound (muscle + macrophages). The extensor digitorum longi (EDL) of male Fisher rats were incubated in a standardized fashion [ 121. The groups of EDL were muscle incubated alone, muscle with the addition to the incubate of activated peritoneal macrophages or muscle with the addition of a conditioned supematant from the incubation of activated or nonactivated peritonal macrophages. Muscle ATP and CP content were noted to be increased 46 and 22%, respectively, when macrophages and skeletal muscle were coincubated. Macrophage-conditioned media from activated or nonactivated macrophages increased the ATP and CP muscle content 44 and 37%, respectively. Preliminary characterization of this high energy phosphate (HEP) promoting factor demonstrates it to be heat and cold stable and less than 10,000 Da. Therefore, a macrophage-mediated transferable factor is capable of increasing the HEP content of skeletal muscle in an in vitro system. This may have important consequences in maintaining host Cell integrity fOliOWing injury. 0 1985 Academic press, IX.","downloadable_attachments":[{"id":87801829,"asset_id":81930247,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":13700988,"first_name":"Michael","last_name":"Caldwell","domain_name":"biola","page_name":"MichaelCaldwell","display_name":"Michael D Caldwell","profile_url":"https://biola.academia.edu/MichaelCaldwell?f_ri=1816594","photo":"https://0.academia-photos.com/13700988/10253409/11442729/s65_michael.caldwell.jpg_oh_2883624ff38d8b0815ee11cfaae40edc_oe_56abebcb___gda___1452888307_b4566e5d0fb3359e122fb06084e7d3cf"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry?f_ri=1816594","nofollow":true},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology?f_ri=1816594","nofollow":true},{"id":8991,"name":"Wound Healing","url":"https://www.academia.edu/Documents/in/Wound_Healing?f_ri=1816594","nofollow":true},{"id":17491,"name":"Macrophages","url":"https://www.academia.edu/Documents/in/Macrophages?f_ri=1816594","nofollow":true},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=1816594"},{"id":36213,"name":"Energy Metabolism","url":"https://www.academia.edu/Documents/in/Energy_Metabolism?f_ri=1816594"},{"id":134095,"name":"Muscles","url":"https://www.academia.edu/Documents/in/Muscles?f_ri=1816594"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594"},{"id":357849,"name":"Skeletal Muscle","url":"https://www.academia.edu/Documents/in/Skeletal_Muscle?f_ri=1816594"},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594"},{"id":568887,"name":"Carrageenan","url":"https://www.academia.edu/Documents/in/Carrageenan?f_ri=1816594"},{"id":916082,"name":"Surgical","url":"https://www.academia.edu/Documents/in/Surgical?f_ri=1816594"},{"id":957359,"name":"Culture Media","url":"https://www.academia.edu/Documents/in/Culture_Media?f_ri=1816594"},{"id":1193624,"name":"Oxygen Consumption","url":"https://www.academia.edu/Documents/in/Oxygen_Consumption?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2285363,"name":"Phosphocreatine","url":"https://www.academia.edu/Documents/in/Phosphocreatine?f_ri=1816594"},{"id":3464694,"name":"Macrophage activation","url":"https://www.academia.edu/Documents/in/Macrophage_activation?f_ri=1816594"},{"id":3881526,"name":"In Vitro Techniques","url":"https://www.academia.edu/Documents/in/In_Vitro_Techniques?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_78161913" data-work_id="78161913" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/78161913/N_1_Aryl_2_1_imidazolo_ethyl_guanidine_derivatives_as_potent_inhibitors_of_the_bovine_mitochondrial_F1F0_ATP_hydrolase">N-[1-Aryl-2-(1-imidazolo)ethyl]-guanidine derivatives as potent inhibitors of the bovine mitochondrial F1F0 ATP hydrolase</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">A series of substituted guanidine derivatives were prepared and evaluated as potent and selective inhibitors of mitochondrial F 1 F 0 ATP hydrolase. The initial thiourethane derived lead molecules possessed intriguing in vitro... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_78161913" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">A series of substituted guanidine derivatives were prepared and evaluated as potent and selective inhibitors of mitochondrial F 1 F 0 ATP hydrolase. The initial thiourethane derived lead molecules possessed intriguing in vitro pharmacological profiles, though contained moieties considered non-drug-like. Analogue synthesis efforts led to compounds with maintained potency and superior physical properties. Small molecules in this series which potently and selectivity inhibit ATP hydrolase and not ATP synthase may have utility as cardioprotective agents.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/78161913" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="00ca6f9dc761791f845fa463ae769d80" rel="nofollow" data-download="{"attachment_id":85306324,"asset_id":78161913,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/85306324/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="1016864" href="https://staffs.academia.edu/saleemAhmad">saleem Ahmad</a><script data-card-contents-for-user="1016864" type="text/json">{"id":1016864,"first_name":"saleem","last_name":"Ahmad","domain_name":"staffs","page_name":"saleemAhmad","display_name":"saleem Ahmad","profile_url":"https://staffs.academia.edu/saleemAhmad?f_ri=1816594","photo":"https://0.academia-photos.com/1016864/2914807/69049795/s65_saleem.ahmad.jpeg"}</script></span></span></li><li class="js-paper-rank-work_78161913 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="78161913"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 78161913, container: ".js-paper-rank-work_78161913", }); 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$(".js-view-count[data-work-id=78161913]").text(description); $(".js-view-count-work_78161913").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_78161913").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="78161913"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">13</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="523" rel="nofollow" href="https://www.academia.edu/Documents/in/Chemistry">Chemistry</a>, <script data-card-contents-for-ri="523" type="text/json">{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="531" rel="nofollow" href="https://www.academia.edu/Documents/in/Organic_Chemistry">Organic Chemistry</a>, <script data-card-contents-for-ri="531" type="text/json">{"id":531,"name":"Organic Chemistry","url":"https://www.academia.edu/Documents/in/Organic_Chemistry?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="12981" rel="nofollow" href="https://www.academia.edu/Documents/in/Enzyme_Inhibitors">Enzyme Inhibitors</a>, <script data-card-contents-for-ri="12981" type="text/json">{"id":12981,"name":"Enzyme Inhibitors","url":"https://www.academia.edu/Documents/in/Enzyme_Inhibitors?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="15719" rel="nofollow" href="https://www.academia.edu/Documents/in/Mitochondria">Mitochondria</a><script data-card-contents-for-ri="15719" type="text/json">{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=78161913]'), work: {"id":78161913,"title":"N-[1-Aryl-2-(1-imidazolo)ethyl]-guanidine derivatives as potent inhibitors of the bovine mitochondrial F1F0 ATP hydrolase","created_at":"2022-05-01T17:29:28.738-07:00","url":"https://www.academia.edu/78161913/N_1_Aryl_2_1_imidazolo_ethyl_guanidine_derivatives_as_potent_inhibitors_of_the_bovine_mitochondrial_F1F0_ATP_hydrolase?f_ri=1816594","dom_id":"work_78161913","summary":"A series of substituted guanidine derivatives were prepared and evaluated as potent and selective inhibitors of mitochondrial F 1 F 0 ATP hydrolase. The initial thiourethane derived lead molecules possessed intriguing in vitro pharmacological profiles, though contained moieties considered non-drug-like. Analogue synthesis efforts led to compounds with maintained potency and superior physical properties. Small molecules in this series which potently and selectivity inhibit ATP hydrolase and not ATP synthase may have utility as cardioprotective agents.","downloadable_attachments":[{"id":85306324,"asset_id":78161913,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":1016864,"first_name":"saleem","last_name":"Ahmad","domain_name":"staffs","page_name":"saleemAhmad","display_name":"saleem Ahmad","profile_url":"https://staffs.academia.edu/saleemAhmad?f_ri=1816594","photo":"https://0.academia-photos.com/1016864/2914807/69049795/s65_saleem.ahmad.jpeg"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry?f_ri=1816594","nofollow":true},{"id":531,"name":"Organic Chemistry","url":"https://www.academia.edu/Documents/in/Organic_Chemistry?f_ri=1816594","nofollow":true},{"id":12981,"name":"Enzyme Inhibitors","url":"https://www.academia.edu/Documents/in/Enzyme_Inhibitors?f_ri=1816594","nofollow":true},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine?f_ri=1816594"},{"id":146190,"name":"ATP synthase","url":"https://www.academia.edu/Documents/in/ATP_synthase?f_ri=1816594"},{"id":260829,"name":"Cattle","url":"https://www.academia.edu/Documents/in/Cattle?f_ri=1816594"},{"id":728493,"name":"Bioorganic and medicinal Chemistry","url":"https://www.academia.edu/Documents/in/Bioorganic_and_medicinal_Chemistry?f_ri=1816594"},{"id":801416,"name":"Guanidines","url":"https://www.academia.edu/Documents/in/Guanidines?f_ri=1816594"},{"id":967839,"name":"Structure activity Relationship","url":"https://www.academia.edu/Documents/in/Structure_activity_Relationship?f_ri=1816594"},{"id":1228946,"name":"Physical Properties","url":"https://www.academia.edu/Documents/in/Physical_Properties?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":3789884,"name":"Pharmacology and pharmaceutical sciences","url":"https://www.academia.edu/Documents/in/Pharmacology_and_pharmaceutical_sciences?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_54065702" data-work_id="54065702" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/54065702/Biophysical_characterization_of_higher_plant_Rubisco_activase">Biophysical characterization of higher plant Rubisco activase</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Rubisco activase (Rca) is a chaperone-like protein of the AAA+ family, which uses mechano-chemical energy derived from ATP hydrolysis to release tightly bound inhibitors from the active site of the primary carbon fixing enzyme ribulose... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_54065702" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Rubisco activase (Rca) is a chaperone-like protein of the AAA+ family, which uses mechano-chemical energy derived from ATP hydrolysis to release tightly bound inhibitors from the active site of the primary carbon fixing enzyme ribulose 1,5-bisphosphate oxygenase/carboxylase (Rubisco). Mechanistic and structural investigations of Rca have been hampered by its exceptional thermolability, high degree of size polydispersity and propensity towards subunit aggregation. In this work, we have characterized the thermal stability and self-association behavior of recombinant Rca preparations, and have developed ligand screening methods. Thermal denaturation profiles generated by circular dichroism indicate that creosote and tobacco short-form Rcas are the most stable proteins examined, with an estimated mid-point temperature of 45-47°C for protein denaturation. We demonstrate that ADP provides a higher degree of stabilization than ATP, that magnesium ions have a small stabilizing effect on ATP-bound, but a significant destabilizing effect on ADP-bound Rca, and that phosphate provides weak stabilization of the ADP-bound form of the protein. A dimeric species was identified by size-exclusion chromatography, suggesting that the two-subunit module may comprise the basic building block for larger assemblies. Evidence is provided that chromatographic procedures reflect non-equilibrium multimeric states. Dynamic light scattering experiments performed on nucleotide-bearing Rca support the notion that several larger, highly polydisperse assembly states coexist over a broad concentration range. No significant changes in aggregation are observed upon replacement of ADP with ATP. However, in the absence of nucleotides, the major protein population appears to consist of a monodisperse oligomer smaller than a hexamer.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/54065702" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="d710e7da3c425eb11fd4350c91923013" rel="nofollow" data-download="{"attachment_id":70609776,"asset_id":54065702,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/70609776/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="179853204" href="https://independent.academia.edu/NathanHenderson16">Nathan Henderson</a><script data-card-contents-for-user="179853204" type="text/json">{"id":179853204,"first_name":"Nathan","last_name":"Henderson","domain_name":"independent","page_name":"NathanHenderson16","display_name":"Nathan Henderson","profile_url":"https://independent.academia.edu/NathanHenderson16?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_54065702 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="54065702"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 54065702, container: ".js-paper-rank-work_54065702", }); 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$(".js-view-count[data-work-id=54065702]").text(description); $(".js-view-count-work_54065702").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_54065702").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="54065702"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9109" rel="nofollow" href="https://www.academia.edu/Documents/in/Tobacco">Tobacco</a>, <script data-card-contents-for-ri="9109" type="text/json">{"id":9109,"name":"Tobacco","url":"https://www.academia.edu/Documents/in/Tobacco?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="38443" rel="nofollow" href="https://www.academia.edu/Documents/in/Protein_Stability">Protein Stability</a>, <script data-card-contents-for-ri="38443" type="text/json">{"id":38443,"name":"Protein Stability","url":"https://www.academia.edu/Documents/in/Protein_Stability?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="48981" rel="nofollow" href="https://www.academia.edu/Documents/in/Molecular_chaperones">Molecular chaperones</a><script data-card-contents-for-ri="48981" type="text/json">{"id":48981,"name":"Molecular chaperones","url":"https://www.academia.edu/Documents/in/Molecular_chaperones?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=54065702]'), work: {"id":54065702,"title":"Biophysical characterization of higher plant Rubisco activase","created_at":"2021-09-29T16:31:14.343-07:00","url":"https://www.academia.edu/54065702/Biophysical_characterization_of_higher_plant_Rubisco_activase?f_ri=1816594","dom_id":"work_54065702","summary":"Rubisco activase (Rca) is a chaperone-like protein of the AAA+ family, which uses mechano-chemical energy derived from ATP hydrolysis to release tightly bound inhibitors from the active site of the primary carbon fixing enzyme ribulose 1,5-bisphosphate oxygenase/carboxylase (Rubisco). Mechanistic and structural investigations of Rca have been hampered by its exceptional thermolability, high degree of size polydispersity and propensity towards subunit aggregation. In this work, we have characterized the thermal stability and self-association behavior of recombinant Rca preparations, and have developed ligand screening methods. Thermal denaturation profiles generated by circular dichroism indicate that creosote and tobacco short-form Rcas are the most stable proteins examined, with an estimated mid-point temperature of 45-47°C for protein denaturation. We demonstrate that ADP provides a higher degree of stabilization than ATP, that magnesium ions have a small stabilizing effect on ATP-bound, but a significant destabilizing effect on ADP-bound Rca, and that phosphate provides weak stabilization of the ADP-bound form of the protein. A dimeric species was identified by size-exclusion chromatography, suggesting that the two-subunit module may comprise the basic building block for larger assemblies. Evidence is provided that chromatographic procedures reflect non-equilibrium multimeric states. Dynamic light scattering experiments performed on nucleotide-bearing Rca support the notion that several larger, highly polydisperse assembly states coexist over a broad concentration range. No significant changes in aggregation are observed upon replacement of ADP with ATP. However, in the absence of nucleotides, the major protein population appears to consist of a monodisperse oligomer smaller than a hexamer.","downloadable_attachments":[{"id":70609776,"asset_id":54065702,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":179853204,"first_name":"Nathan","last_name":"Henderson","domain_name":"independent","page_name":"NathanHenderson16","display_name":"Nathan Henderson","profile_url":"https://independent.academia.edu/NathanHenderson16?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9109,"name":"Tobacco","url":"https://www.academia.edu/Documents/in/Tobacco?f_ri=1816594","nofollow":true},{"id":38443,"name":"Protein Stability","url":"https://www.academia.edu/Documents/in/Protein_Stability?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true},{"id":48981,"name":"Molecular chaperones","url":"https://www.academia.edu/Documents/in/Molecular_chaperones?f_ri=1816594","nofollow":true},{"id":75847,"name":"HPLC","url":"https://www.academia.edu/Documents/in/HPLC?f_ri=1816594"},{"id":76407,"name":"Circular Dichroism","url":"https://www.academia.edu/Documents/in/Circular_Dichroism?f_ri=1816594"},{"id":83843,"name":"RuBisCO","url":"https://www.academia.edu/Documents/in/RuBisCO?f_ri=1816594"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences?f_ri=1816594"},{"id":143874,"name":"Protein Aggregation","url":"https://www.academia.edu/Documents/in/Protein_Aggregation?f_ri=1816594"},{"id":956752,"name":"Protein Quaternary Structure","url":"https://www.academia.edu/Documents/in/Protein_Quaternary_Structure?f_ri=1816594"},{"id":1030179,"name":"DLS","url":"https://www.academia.edu/Documents/in/DLS?f_ri=1816594"},{"id":1181939,"name":"PLANT PROTEINS","url":"https://www.academia.edu/Documents/in/PLANT_PROTEINS?f_ri=1816594"},{"id":1186541,"name":"Protein Denaturation","url":"https://www.academia.edu/Documents/in/Protein_Denaturation?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2478277,"name":"Polydispersity","url":"https://www.academia.edu/Documents/in/Polydispersity?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_51216119" data-work_id="51216119" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/51216119/A_functional_role_for_the_fibroblast_like_cells_in_gastrointestinal_smooth_muscles">A functional role for the 'fibroblast-like cells' in gastrointestinal smooth muscles</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Non-technical summary Smooth muscles, as in the gastrointestinal tract, are composed of several types of cells. Gastrointestinal muscles contain smooth muscle cells, enteric neurons, glial cells, immune cells, and various classes of... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_51216119" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Non-technical summary Smooth muscles, as in the gastrointestinal tract, are composed of several types of cells. Gastrointestinal muscles contain smooth muscle cells, enteric neurons, glial cells, immune cells, and various classes of interstitial cells. One type of interstitial cell, referred to as 'fibroblast-like cells' by morphologists, are common, but their function is unknown. These cells are found near the terminals of enteric motor neurons, suggesting they could have a role in generating neural responses that help control gastrointestinal movements. We used a novel mouse with bright green fluorescent protein expressed specifically in the fibroblast-like cells to help us identify these cells in the mixture of cells obtained when whole muscles are dispersed with enzymes. We isolated these cells and found they respond to a major class of inhibitory neurotransmitters-purines. We characterized these responses, and our results provide a new hypothesis about the role of fibroblast-like cells in smooth muscle tissues.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/51216119" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="914366260c85d798227c5fdb6bd51d9c" rel="nofollow" data-download="{"attachment_id":69031793,"asset_id":51216119,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/69031793/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="51226987" href="https://independent.academia.edu/SeanWard9">Sean Ward</a><script data-card-contents-for-user="51226987" type="text/json">{"id":51226987,"first_name":"Sean","last_name":"Ward","domain_name":"independent","page_name":"SeanWard9","display_name":"Sean Ward","profile_url":"https://independent.academia.edu/SeanWard9?f_ri=1816594","photo":"https://0.academia-photos.com/51226987/13563552/14732229/s65_sean.ward.jpg"}</script></span></span></li><li class="js-paper-rank-work_51216119 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="51216119"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 51216119, container: ".js-paper-rank-work_51216119", }); 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$(".js-view-count[data-work-id=51216119]").text(description); $(".js-view-count-work_51216119").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_51216119").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="51216119"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="27784" rel="nofollow" href="https://www.academia.edu/Documents/in/Gene_expression">Gene expression</a>, <script data-card-contents-for-ri="27784" type="text/json">{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="37793" rel="nofollow" href="https://www.academia.edu/Documents/in/Patch-clamp_and_imaging_techniques">Patch-clamp and imaging techniques</a>, <script data-card-contents-for-ri="37793" type="text/json">{"id":37793,"name":"Patch-clamp and imaging techniques","url":"https://www.academia.edu/Documents/in/Patch-clamp_and_imaging_techniques?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a><script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=51216119]'), work: {"id":51216119,"title":"A functional role for the 'fibroblast-like cells' in gastrointestinal smooth muscles","created_at":"2021-09-03T17:50:03.856-07:00","url":"https://www.academia.edu/51216119/A_functional_role_for_the_fibroblast_like_cells_in_gastrointestinal_smooth_muscles?f_ri=1816594","dom_id":"work_51216119","summary":"Non-technical summary Smooth muscles, as in the gastrointestinal tract, are composed of several types of cells. Gastrointestinal muscles contain smooth muscle cells, enteric neurons, glial cells, immune cells, and various classes of interstitial cells. One type of interstitial cell, referred to as 'fibroblast-like cells' by morphologists, are common, but their function is unknown. These cells are found near the terminals of enteric motor neurons, suggesting they could have a role in generating neural responses that help control gastrointestinal movements. We used a novel mouse with bright green fluorescent protein expressed specifically in the fibroblast-like cells to help us identify these cells in the mixture of cells obtained when whole muscles are dispersed with enzymes. We isolated these cells and found they respond to a major class of inhibitory neurotransmitters-purines. We characterized these responses, and our results provide a new hypothesis about the role of fibroblast-like cells in smooth muscle tissues.","downloadable_attachments":[{"id":69031793,"asset_id":51216119,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":51226987,"first_name":"Sean","last_name":"Ward","domain_name":"independent","page_name":"SeanWard9","display_name":"Sean Ward","profile_url":"https://independent.academia.edu/SeanWard9?f_ri=1816594","photo":"https://0.academia-photos.com/51226987/13563552/14732229/s65_sean.ward.jpg"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=1816594","nofollow":true},{"id":37793,"name":"Patch-clamp and imaging techniques","url":"https://www.academia.edu/Documents/in/Patch-clamp_and_imaging_techniques?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true},{"id":65171,"name":"Smooth muscle","url":"https://www.academia.edu/Documents/in/Smooth_muscle?f_ri=1816594"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice?f_ri=1816594"},{"id":176503,"name":"Synaptic Transmission","url":"https://www.academia.edu/Documents/in/Synaptic_Transmission?f_ri=1816594"},{"id":537759,"name":"Gastrointestinal Tract","url":"https://www.academia.edu/Documents/in/Gastrointestinal_Tract?f_ri=1816594"},{"id":828507,"name":"NAD","url":"https://www.academia.edu/Documents/in/NAD?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1831948,"name":"Adenosine Diphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Diphosphate?f_ri=1816594"},{"id":2468093,"name":"Cell Membrane","url":"https://www.academia.edu/Documents/in/Cell_Membrane?f_ri=1816594"},{"id":2533047,"name":"fibroblasts","url":"https://www.academia.edu/Documents/in/fibroblasts?f_ri=1816594"},{"id":2552788,"name":"Motor Neurons","url":"https://www.academia.edu/Documents/in/Motor_Neurons?f_ri=1816594"},{"id":3763225,"name":"Medical and Health Sciences","url":"https://www.academia.edu/Documents/in/Medical_and_Health_Sciences?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_51052804" data-work_id="51052804" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/51052804/Effects_of_metabolic_modulation_by_trimetazidine_on_left_ventricular_function_and_phosphocreatine_adenosine_triphosphate_ratio_in_patients_with_heart_failure">Effects of metabolic modulation by trimetazidine on left ventricular function and phosphocreatine/adenosine triphosphate ratio in patients with heart failure</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The addition of trimetazidine to standard treatment has been shown to improve left ventricular (LV) function in patients with heart failure. The aim of this study is to non-invasively assess, by means of in vivo 31 P-magnetic resonance... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_51052804" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The addition of trimetazidine to standard treatment has been shown to improve left ventricular (LV) function in patients with heart failure. The aim of this study is to non-invasively assess, by means of in vivo 31 P-magnetic resonance spectroscopy (31 P-MRS), the effects of trimetazidine on LV cardiac phosphocreatine and adenosine triphosphate (PCr/ATP) ratio in patients with heart failure. Methods and results Twelve heart failure patients were randomized in a double-blind, cross-over study to placebo or trimetazidine (20 mg t.i.d.) for two periods of 90 days. At the end of each period, all patients underwent exercise testing, 2D echocardiography, and MRS. New York Heart Association (NYHA) class, ejection fraction (EF), maximal rate-pressure product, and metabolic equivalent system (METS) were evaluated. Relative concentrations of PCr and ATP were determined by cardiac 31 P-MRS. On trimetazidine, NYHA class decreased from 3.04 + 0.26 to 2.45 + 0.52 (P ¼ 0.005), whereas EF (34 + 10 vs. 39 + 10%, P ¼ 0.03) and METS (from 7.44 + 1.84 to 8.78 + 2.72, P ¼ 0.03) increased. The mean cardiac PCr/ATP ratio was 1.35 + 0.33 with placebo, but was increased by 33% to 1.80 + 0.50 (P ¼ 0.03) with trimetazidine. Conclusion Trimetazidine improves functional class and LV function in patients with heart failure. These effects are associated to the observed trimetazidine-induced increase in the PCr/ATP ratio, indicating preservation of the myocardial high-energy phosphate levels.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/51052804" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="b33380cd74b6900a86b4e66eea09e935" rel="nofollow" data-download="{"attachment_id":68914968,"asset_id":51052804,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/68914968/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="71650379" href="https://independent.academia.edu/GianlucaPerseghin">Gianluca Perseghin</a><script data-card-contents-for-user="71650379" type="text/json">{"id":71650379,"first_name":"Gianluca","last_name":"Perseghin","domain_name":"independent","page_name":"GianlucaPerseghin","display_name":"Gianluca Perseghin","profile_url":"https://independent.academia.edu/GianlucaPerseghin?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_51052804 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="51052804"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 51052804, container: ".js-paper-rank-work_51052804", }); 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$(".js-view-count[data-work-id=51052804]").text(description); $(".js-view-count-work_51052804").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_51052804").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="51052804"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">17</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="606" rel="nofollow" href="https://www.academia.edu/Documents/in/Cardiology">Cardiology</a>, <script data-card-contents-for-ri="606" type="text/json">{"id":606,"name":"Cardiology","url":"https://www.academia.edu/Documents/in/Cardiology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="24925" rel="nofollow" href="https://www.academia.edu/Documents/in/Modulation">Modulation</a>, <script data-card-contents-for-ri="24925" type="text/json">{"id":24925,"name":"Modulation","url":"https://www.academia.edu/Documents/in/Modulation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="46824" rel="nofollow" href="https://www.academia.edu/Documents/in/Echocardiography">Echocardiography</a>, <script data-card-contents-for-ri="46824" type="text/json">{"id":46824,"name":"Echocardiography","url":"https://www.academia.edu/Documents/in/Echocardiography?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="49633" rel="nofollow" href="https://www.academia.edu/Documents/in/Heart_Failure">Heart Failure</a><script data-card-contents-for-ri="49633" type="text/json">{"id":49633,"name":"Heart Failure","url":"https://www.academia.edu/Documents/in/Heart_Failure?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=51052804]'), work: {"id":51052804,"title":"Effects of metabolic modulation by trimetazidine on left ventricular function and phosphocreatine/adenosine triphosphate ratio in patients with heart failure","created_at":"2021-08-28T02:36:38.166-07:00","url":"https://www.academia.edu/51052804/Effects_of_metabolic_modulation_by_trimetazidine_on_left_ventricular_function_and_phosphocreatine_adenosine_triphosphate_ratio_in_patients_with_heart_failure?f_ri=1816594","dom_id":"work_51052804","summary":"The addition of trimetazidine to standard treatment has been shown to improve left ventricular (LV) function in patients with heart failure. The aim of this study is to non-invasively assess, by means of in vivo 31 P-magnetic resonance spectroscopy (31 P-MRS), the effects of trimetazidine on LV cardiac phosphocreatine and adenosine triphosphate (PCr/ATP) ratio in patients with heart failure. Methods and results Twelve heart failure patients were randomized in a double-blind, cross-over study to placebo or trimetazidine (20 mg t.i.d.) for two periods of 90 days. At the end of each period, all patients underwent exercise testing, 2D echocardiography, and MRS. New York Heart Association (NYHA) class, ejection fraction (EF), maximal rate-pressure product, and metabolic equivalent system (METS) were evaluated. Relative concentrations of PCr and ATP were determined by cardiac 31 P-MRS. On trimetazidine, NYHA class decreased from 3.04 + 0.26 to 2.45 + 0.52 (P ¼ 0.005), whereas EF (34 + 10 vs. 39 + 10%, P ¼ 0.03) and METS (from 7.44 + 1.84 to 8.78 + 2.72, P ¼ 0.03) increased. The mean cardiac PCr/ATP ratio was 1.35 + 0.33 with placebo, but was increased by 33% to 1.80 + 0.50 (P ¼ 0.03) with trimetazidine. Conclusion Trimetazidine improves functional class and LV function in patients with heart failure. These effects are associated to the observed trimetazidine-induced increase in the PCr/ATP ratio, indicating preservation of the myocardial high-energy phosphate levels.","downloadable_attachments":[{"id":68914968,"asset_id":51052804,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":71650379,"first_name":"Gianluca","last_name":"Perseghin","domain_name":"independent","page_name":"GianlucaPerseghin","display_name":"Gianluca Perseghin","profile_url":"https://independent.academia.edu/GianlucaPerseghin?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":606,"name":"Cardiology","url":"https://www.academia.edu/Documents/in/Cardiology?f_ri=1816594","nofollow":true},{"id":24925,"name":"Modulation","url":"https://www.academia.edu/Documents/in/Modulation?f_ri=1816594","nofollow":true},{"id":46824,"name":"Echocardiography","url":"https://www.academia.edu/Documents/in/Echocardiography?f_ri=1816594","nofollow":true},{"id":49633,"name":"Heart Failure","url":"https://www.academia.edu/Documents/in/Heart_Failure?f_ri=1816594","nofollow":true},{"id":62112,"name":"Prospective studies","url":"https://www.academia.edu/Documents/in/Prospective_studies?f_ri=1816594"},{"id":74347,"name":"Hemodynamics","url":"https://www.academia.edu/Documents/in/Hemodynamics?f_ri=1816594"},{"id":91755,"name":"Energetics","url":"https://www.academia.edu/Documents/in/Energetics?f_ri=1816594"},{"id":198747,"name":"Left Ventricular Dysfunction","url":"https://www.academia.edu/Documents/in/Left_Ventricular_Dysfunction?f_ri=1816594"},{"id":289271,"name":"Aged","url":"https://www.academia.edu/Documents/in/Aged?f_ri=1816594"},{"id":918981,"name":"Left Ventricular Function","url":"https://www.academia.edu/Documents/in/Left_Ventricular_Function?f_ri=1816594"},{"id":1024379,"name":"Nuclear Magnetic Resonance Imaging","url":"https://www.academia.edu/Documents/in/Nuclear_Magnetic_Resonance_Imaging?f_ri=1816594"},{"id":1222887,"name":"Ratio","url":"https://www.academia.edu/Documents/in/Ratio?f_ri=1816594"},{"id":1702533,"name":"Trimetazidine","url":"https://www.academia.edu/Documents/in/Trimetazidine?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1944553,"name":"Magnetic resonance angiography","url":"https://www.academia.edu/Documents/in/Magnetic_resonance_angiography?f_ri=1816594"},{"id":2285363,"name":"Phosphocreatine","url":"https://www.academia.edu/Documents/in/Phosphocreatine?f_ri=1816594"},{"id":3789879,"name":"Cardiovascular medicine and haematology","url":"https://www.academia.edu/Documents/in/Cardiovascular_medicine_and_haematology?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_36357308" data-work_id="36357308" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/36357308/Mitochondrial_DNA_Mutation_Elicited_Oxidative_Stress_Oxidative_Damage_and_Altered_Gene_Expression_in_Cultured_Cells_of_Patients_with_MERRF_Syndrome">Mitochondrial DNA Mutation-Elicited Oxidative Stress, Oxidative Damage, and Altered Gene Expression in Cultured Cells of Patients with MERRF Syndrome</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Myoclonic epilepsy and ragged-red fibers (MERRF) syndrome is a rare disorder characterized by myoclonus, muscle weakness, cerebellar ataxia, heart conduction block, and dementia. It has been documented that 80-90% of the patients with... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_36357308" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Myoclonic epilepsy and ragged-red fibers (MERRF) syndrome is a rare disorder characterized by myoclonus, muscle weakness, cerebellar ataxia, heart conduction block, and dementia. It has been documented that 80-90% of the patients with MERRF syndrome are caused by the A8344G mutation in the tRNA Lys gene of mitochondrial DNA (mtDNA). We and other investigators have reported that the mtDNA mutation results in not only inefficient generation of adenosine triphosphate but also increased production of reactive oxygen species (ROS) in cultured cells harboring A8344G mutation of mtDNA. In addition, we found an imbalance in the gene expression of antioxidant enzymes in the skin fibroblasts of MERRF patients. The mRNA, protein, and enzyme activity levels of manganese-superoxide dismutase were increased, but those of Cu,Zn-SOD, catalase, and glutathione peroxidase did not show significant changes. Recently, we showed that the excess ROS could damage voltage-dependent anion channel, prohibitin, Lon protease, and aconitase in the MERRF cells. Moreover, there was a dramatic increase in the gene expression and activity of matrix metalloproteinase 1, which may contribute to the cytoskeleton remodeling involved in the weakness and atrophy of muscle commonly seen in MERRF patients. Taken together, we suggest that mtDNA mutation-elicited oxidative stress, oxidative dam-age, and altered gene expression are involved in the pathogenesis and progression of MERRF syndrome.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/36357308" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="4d9489073ee970d803bdbe81099e44dc" rel="nofollow" data-download="{"attachment_id":56266238,"asset_id":36357308,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/56266238/download_file?st=MTczOTc5ODAwOSw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="35613279" href="https://ym.academia.edu/YauhueiWei">Yau-huei Wei</a><script data-card-contents-for-user="35613279" type="text/json">{"id":35613279,"first_name":"Yau-huei","last_name":"Wei","domain_name":"ym","page_name":"YauhueiWei","display_name":"Yau-huei Wei","profile_url":"https://ym.academia.edu/YauhueiWei?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_36357308 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="36357308"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 36357308, container: ".js-paper-rank-work_36357308", }); 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$(".js-view-count[data-work-id=36357308]").text(description); $(".js-view-count-work_36357308").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_36357308").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="36357308"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">23</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="237" rel="nofollow" href="https://www.academia.edu/Documents/in/Cognitive_Science">Cognitive Science</a>, <script data-card-contents-for-ri="237" type="text/json">{"id":237,"name":"Cognitive Science","url":"https://www.academia.edu/Documents/in/Cognitive_Science?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="14292" rel="nofollow" href="https://www.academia.edu/Documents/in/Oxidative_Stress">Oxidative Stress</a>, <script data-card-contents-for-ri="14292" type="text/json">{"id":14292,"name":"Oxidative Stress","url":"https://www.academia.edu/Documents/in/Oxidative_Stress?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="23066" rel="nofollow" href="https://www.academia.edu/Documents/in/DNA_damage">DNA damage</a>, <script data-card-contents-for-ri="23066" type="text/json">{"id":23066,"name":"DNA damage","url":"https://www.academia.edu/Documents/in/DNA_damage?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="27784" rel="nofollow" href="https://www.academia.edu/Documents/in/Gene_expression">Gene expression</a><script data-card-contents-for-ri="27784" type="text/json">{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=36357308]'), work: {"id":36357308,"title":"Mitochondrial DNA Mutation-Elicited Oxidative Stress, Oxidative Damage, and Altered Gene Expression in Cultured Cells of Patients with MERRF Syndrome","created_at":"2018-04-08T02:00:07.885-07:00","url":"https://www.academia.edu/36357308/Mitochondrial_DNA_Mutation_Elicited_Oxidative_Stress_Oxidative_Damage_and_Altered_Gene_Expression_in_Cultured_Cells_of_Patients_with_MERRF_Syndrome?f_ri=1816594","dom_id":"work_36357308","summary":"Myoclonic epilepsy and ragged-red fibers (MERRF) syndrome is a rare disorder characterized by myoclonus, muscle weakness, cerebellar ataxia, heart conduction block, and dementia. It has been documented that 80-90% of the patients with MERRF syndrome are caused by the A8344G mutation in the tRNA Lys gene of mitochondrial DNA (mtDNA). We and other investigators have reported that the mtDNA mutation results in not only inefficient generation of adenosine triphosphate but also increased production of reactive oxygen species (ROS) in cultured cells harboring A8344G mutation of mtDNA. In addition, we found an imbalance in the gene expression of antioxidant enzymes in the skin fibroblasts of MERRF patients. The mRNA, protein, and enzyme activity levels of manganese-superoxide dismutase were increased, but those of Cu,Zn-SOD, catalase, and glutathione peroxidase did not show significant changes. Recently, we showed that the excess ROS could damage voltage-dependent anion channel, prohibitin, Lon protease, and aconitase in the MERRF cells. Moreover, there was a dramatic increase in the gene expression and activity of matrix metalloproteinase 1, which may contribute to the cytoskeleton remodeling involved in the weakness and atrophy of muscle commonly seen in MERRF patients. Taken together, we suggest that mtDNA mutation-elicited oxidative stress, oxidative dam-age, and altered gene expression are involved in the pathogenesis and progression of MERRF syndrome.","downloadable_attachments":[{"id":56266238,"asset_id":36357308,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":35613279,"first_name":"Yau-huei","last_name":"Wei","domain_name":"ym","page_name":"YauhueiWei","display_name":"Yau-huei Wei","profile_url":"https://ym.academia.edu/YauhueiWei?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":237,"name":"Cognitive Science","url":"https://www.academia.edu/Documents/in/Cognitive_Science?f_ri=1816594","nofollow":true},{"id":14292,"name":"Oxidative Stress","url":"https://www.academia.edu/Documents/in/Oxidative_Stress?f_ri=1816594","nofollow":true},{"id":23066,"name":"DNA damage","url":"https://www.academia.edu/Documents/in/DNA_damage?f_ri=1816594","nofollow":true},{"id":27784,"name":"Gene expression","url":"https://www.academia.edu/Documents/in/Gene_expression?f_ri=1816594","nofollow":true},{"id":37508,"name":"Cytoskeleton","url":"https://www.academia.edu/Documents/in/Cytoskeleton?f_ri=1816594"},{"id":41818,"name":"Molecular Neurobiology","url":"https://www.academia.edu/Documents/in/Molecular_Neurobiology?f_ri=1816594"},{"id":51711,"name":"Antioxidants","url":"https://www.academia.edu/Documents/in/Antioxidants?f_ri=1816594"},{"id":63093,"name":"Mitochondrial DNA","url":"https://www.academia.edu/Documents/in/Mitochondrial_DNA?f_ri=1816594"},{"id":74780,"name":"Mutation","url":"https://www.academia.edu/Documents/in/Mutation?f_ri=1816594"},{"id":82978,"name":"Reactive Oxygen Species","url":"https://www.academia.edu/Documents/in/Reactive_Oxygen_Species?f_ri=1816594"},{"id":139007,"name":"Catalase","url":"https://www.academia.edu/Documents/in/Catalase?f_ri=1816594"},{"id":141395,"name":"Glutathione Peroxidase","url":"https://www.academia.edu/Documents/in/Glutathione_Peroxidase?f_ri=1816594"},{"id":146326,"name":"Cerebellar ataxia","url":"https://www.academia.edu/Documents/in/Cerebellar_ataxia?f_ri=1816594"},{"id":290205,"name":"Mitochondrial Diseases","url":"https://www.academia.edu/Documents/in/Mitochondrial_Diseases?f_ri=1816594"},{"id":295257,"name":"Antioxidant enzyme","url":"https://www.academia.edu/Documents/in/Antioxidant_enzyme?f_ri=1816594"},{"id":427871,"name":"Oxidative Damage","url":"https://www.academia.edu/Documents/in/Oxidative_Damage?f_ri=1816594"},{"id":434453,"name":"Oxidative phosphorylation","url":"https://www.academia.edu/Documents/in/Oxidative_phosphorylation?f_ri=1816594"},{"id":583568,"name":"Enzyme activity","url":"https://www.academia.edu/Documents/in/Enzyme_activity?f_ri=1816594"},{"id":1239755,"name":"Neurosciences","url":"https://www.academia.edu/Documents/in/Neurosciences?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1920779,"name":"Matrix Metalloproteinase","url":"https://www.academia.edu/Documents/in/Matrix_Metalloproteinase?f_ri=1816594"},{"id":2445801,"name":"Mitochondrial Proteins","url":"https://www.academia.edu/Documents/in/Mitochondrial_Proteins?f_ri=1816594"},{"id":2533047,"name":"fibroblasts","url":"https://www.academia.edu/Documents/in/fibroblasts?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_33835997" data-work_id="33835997" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/33835997/Blood_vessel_adaptation_to_gravity_in_a_semi_arboreal_snake">Blood vessel adaptation to gravity in a semi-arboreal snake</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The effects of vasoactive agonists on systemic blood vessels were examined with respect to anatomical location and gravity acclimation in the semi-arboreal snake, Elaphe Obsoleta. Major blood vessels were reactive to putative... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_33835997" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The effects of vasoactive agonists on systemic blood vessels were examined with respect to anatomical location and gravity acclimation in the semi-arboreal snake, Elaphe Obsoleta. Major blood vessels were reactive to putative neurotransmitters, hormones or local factors in vessel specific patterns. Catecholamines, adenosine triphosphate, histamine and high potassium (80mM) stimulated significantly greater tension per unit vessel mass in posterior than anterior arteries. Anterior vessels were significantly more sensitive to catecholamines than midbody and posterior vessels. Angiotensin II stimulated significantly greater tension in carotid artery than in midbody and posterior dorsal aorta. Arginine vasotocin strongly contracted the left and right aortic arches and anterior dorsal aorta. Veins were strongly contracted by catecholamines, high potassium and angiotensin II, but less so by adenosine triphosphate, arginine vasotocin and histamine. Precontracted vessels were relaxed by acetylcholine and sodium nitroprusside, but not by atrial natriuretic peptide or bradykinin. Chronic exposure of snakes to intermittent hypergravity stress (+1.5 Gz at tail) did not affect the majority of vessel responses. These data demonstrate that in vitro tension correlates with known patterns of sympathetic innervation and suggest Abbreviations ACH acetylcholine -ADA anterior dorsal aorta" ANG II salmon asnl-valS-angiotensin II' ANP rat ileZ6-atrial natriuretic peptide 9 A TP adenosine triphosphate -A V T arginine vasotocin 9 BK human bradykinin 9 BL total body length 9 CA carotid artery 9 CONT control -ECso effective concentration producing 50% maximal response 9 EPI epinephrine 9 + Gz earth's gravity force 9 HI-G high gravity acclimation 9 HI K + 80 mM high potassium 9 JV jugular vein -LAA left aortic arch -MDA midbody dorsal aorta -MPV midbody portal vein-MS Mackenzie's solution" NEPI norepinephrine; pDz-log ECs0 9 PDA posterior dorsal aorta. PPV posterior portal vein-RAA right aortic arch 9 SNP sodium nitroprusside</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/33835997" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="92b092f20f8767661dffae091f5f2250" rel="nofollow" data-download="{"attachment_id":53818371,"asset_id":33835997,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/53818371/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="66293907" href="https://independent.academia.edu/KennethOlson6">Kenneth Olson</a><script data-card-contents-for-user="66293907" type="text/json">{"id":66293907,"first_name":"Kenneth","last_name":"Olson","domain_name":"independent","page_name":"KennethOlson6","display_name":"Kenneth Olson","profile_url":"https://independent.academia.edu/KennethOlson6?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_33835997 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="33835997"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 33835997, container: ".js-paper-rank-work_33835997", }); 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$(".js-view-count[data-work-id=33835997]").text(description); $(".js-view-count-work_33835997").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_33835997").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="33835997"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">20</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="167" rel="nofollow" href="https://www.academia.edu/Documents/in/Physiology">Physiology</a>, <script data-card-contents-for-ri="167" type="text/json">{"id":167,"name":"Physiology","url":"https://www.academia.edu/Documents/in/Physiology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="173" rel="nofollow" href="https://www.academia.edu/Documents/in/Zoology">Zoology</a>, <script data-card-contents-for-ri="173" type="text/json">{"id":173,"name":"Zoology","url":"https://www.academia.edu/Documents/in/Zoology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="1246" rel="nofollow" href="https://www.academia.edu/Documents/in/Gravitation">Gravitation</a>, <script data-card-contents-for-ri="1246" type="text/json">{"id":1246,"name":"Gravitation","url":"https://www.academia.edu/Documents/in/Gravitation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="51569" rel="nofollow" href="https://www.academia.edu/Documents/in/Histamine">Histamine</a><script data-card-contents-for-ri="51569" type="text/json">{"id":51569,"name":"Histamine","url":"https://www.academia.edu/Documents/in/Histamine?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=33835997]'), work: {"id":33835997,"title":"Blood vessel adaptation to gravity in a semi-arboreal snake","created_at":"2017-07-10T09:33:56.711-07:00","url":"https://www.academia.edu/33835997/Blood_vessel_adaptation_to_gravity_in_a_semi_arboreal_snake?f_ri=1816594","dom_id":"work_33835997","summary":"The effects of vasoactive agonists on systemic blood vessels were examined with respect to anatomical location and gravity acclimation in the semi-arboreal snake, Elaphe Obsoleta. Major blood vessels were reactive to putative neurotransmitters, hormones or local factors in vessel specific patterns. Catecholamines, adenosine triphosphate, histamine and high potassium (80mM) stimulated significantly greater tension per unit vessel mass in posterior than anterior arteries. Anterior vessels were significantly more sensitive to catecholamines than midbody and posterior vessels. Angiotensin II stimulated significantly greater tension in carotid artery than in midbody and posterior dorsal aorta. Arginine vasotocin strongly contracted the left and right aortic arches and anterior dorsal aorta. Veins were strongly contracted by catecholamines, high potassium and angiotensin II, but less so by adenosine triphosphate, arginine vasotocin and histamine. Precontracted vessels were relaxed by acetylcholine and sodium nitroprusside, but not by atrial natriuretic peptide or bradykinin. Chronic exposure of snakes to intermittent hypergravity stress (+1.5 Gz at tail) did not affect the majority of vessel responses. These data demonstrate that in vitro tension correlates with known patterns of sympathetic innervation and suggest Abbreviations ACH acetylcholine -ADA anterior dorsal aorta\" ANG II salmon asnl-valS-angiotensin II' ANP rat ileZ6-atrial natriuretic peptide 9 A TP adenosine triphosphate -A V T arginine vasotocin 9 BK human bradykinin 9 BL total body length 9 CA carotid artery 9 CONT control -ECso effective concentration producing 50% maximal response 9 EPI epinephrine 9 + Gz earth's gravity force 9 HI-G high gravity acclimation 9 HI K + 80 mM high potassium 9 JV jugular vein -LAA left aortic arch -MDA midbody dorsal aorta -MPV midbody portal vein-MS Mackenzie's solution\" NEPI norepinephrine; pDz-log ECs0 9 PDA posterior dorsal aorta. PPV posterior portal vein-RAA right aortic arch 9 SNP sodium nitroprusside","downloadable_attachments":[{"id":53818371,"asset_id":33835997,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":66293907,"first_name":"Kenneth","last_name":"Olson","domain_name":"independent","page_name":"KennethOlson6","display_name":"Kenneth Olson","profile_url":"https://independent.academia.edu/KennethOlson6?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":167,"name":"Physiology","url":"https://www.academia.edu/Documents/in/Physiology?f_ri=1816594","nofollow":true},{"id":173,"name":"Zoology","url":"https://www.academia.edu/Documents/in/Zoology?f_ri=1816594","nofollow":true},{"id":1246,"name":"Gravitation","url":"https://www.academia.edu/Documents/in/Gravitation?f_ri=1816594","nofollow":true},{"id":51569,"name":"Histamine","url":"https://www.academia.edu/Documents/in/Histamine?f_ri=1816594","nofollow":true},{"id":104853,"name":"Hormones","url":"https://www.academia.edu/Documents/in/Hormones?f_ri=1816594"},{"id":134021,"name":"Snakes","url":"https://www.academia.edu/Documents/in/Snakes?f_ri=1816594"},{"id":159958,"name":"Acetylcholine","url":"https://www.academia.edu/Documents/in/Acetylcholine?f_ri=1816594"},{"id":160656,"name":"Potassium","url":"https://www.academia.edu/Documents/in/Potassium?f_ri=1816594"},{"id":277236,"name":"Veins","url":"https://www.academia.edu/Documents/in/Veins?f_ri=1816594"},{"id":413194,"name":"Analysis of Variance","url":"https://www.academia.edu/Documents/in/Analysis_of_Variance?f_ri=1816594"},{"id":954841,"name":"Angiotensin II","url":"https://www.academia.edu/Documents/in/Angiotensin_II?f_ri=1816594"},{"id":969448,"name":"Carotid Artery","url":"https://www.academia.edu/Documents/in/Carotid_Artery?f_ri=1816594"},{"id":1166957,"name":"Catecholamines","url":"https://www.academia.edu/Documents/in/Catecholamines?f_ri=1816594"},{"id":1251210,"name":"Blood Vessel","url":"https://www.academia.edu/Documents/in/Blood_Vessel?f_ri=1816594"},{"id":1559764,"name":"Vasotocin","url":"https://www.academia.edu/Documents/in/Vasotocin?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1971602,"name":"Sodium Nitroprusside","url":"https://www.academia.edu/Documents/in/Sodium_Nitroprusside?f_ri=1816594"},{"id":2090731,"name":"Aortic arch","url":"https://www.academia.edu/Documents/in/Aortic_arch?f_ri=1816594"},{"id":2562018,"name":"Arteries","url":"https://www.academia.edu/Documents/in/Arteries?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_3659044" data-work_id="3659044" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/3659044/Antifolate_resistance_mediated_by_the_multidrug_resistance_proteins_MRP1_and_MRP2">Antifolate resistance mediated by the multidrug resistance proteins MRP1 and MRP2</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Transfection of multidrug resistance proteins (MRPs) MRP1 and MRP2 in human ovarian carcinoma 2008 cells conferred a marked level of resistance to short-term (1-4 h) exposure to the polyglutamatable antifolates methotrexate (MTX;... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_3659044" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Transfection of multidrug resistance proteins (MRPs) MRP1 and MRP2 in human ovarian carcinoma 2008 cells conferred a marked level of resistance to short-term (1-4 h) exposure to the polyglutamatable antifolates methotrexate (MTX; 21-74-fold), ZD1694 (4 -138-fold), and GW1843 (101-156-fold). Evidence for MRP-mediated antifolate efflux relies upon the following findings: (a) a 2-3.3-fold lower accumulation of [ 3 H]MTX and subsequent reduced formation of long-chain polyglutamate forms of MTX; (b) reversal of MTX resistance by probenecid in both transfectants, and (c) ATP-dependent uptake of [ 3 H]MTX in inside-out vesicles of MRP1 and MRP2 transfectants. This report provides a mechanistic basis for resistance to polyglutamatable antifolates through an MRP-mediated drug extrusion. . 3 The abbreviations used are: MTX, methotrexate; DHFR, dihydrofolate reductase; RFC, reduced folate carrier; FPGS, folylpoly-␥-glutamate synthetase; MRP, multidrug resistance protein; HBS, HEPES-buffered saline. 4 M. Kool et al., manuscript in preparation.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/3659044" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="ef2bb1a96049d3a25ec18977f0eb3fe6" rel="nofollow" data-download="{"attachment_id":31351158,"asset_id":3659044,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/31351158/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="4444753" href="https://independent.academia.edu/RikKool">Rik Kool</a><script data-card-contents-for-user="4444753" type="text/json">{"id":4444753,"first_name":"Rik","last_name":"Kool","domain_name":"independent","page_name":"RikKool","display_name":"Rik Kool","profile_url":"https://independent.academia.edu/RikKool?f_ri=1816594","photo":"https://0.academia-photos.com/4444753/1815330/2162510/s65_rik.kool.jpg"}</script></span></span></li><li class="js-paper-rank-work_3659044 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="3659044"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 3659044, container: ".js-paper-rank-work_3659044", }); 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$(".js-view-count[data-work-id=3659044]").text(description); $(".js-view-count-work_3659044").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_3659044").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="3659044"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">7</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="6021" rel="nofollow" href="https://www.academia.edu/Documents/in/Cancer">Cancer</a>, <script data-card-contents-for-ri="6021" type="text/json">{"id":6021,"name":"Cancer","url":"https://www.academia.edu/Documents/in/Cancer?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="126972" rel="nofollow" href="https://www.academia.edu/Documents/in/P-glycoprotein">P-glycoprotein</a>, <script data-card-contents-for-ri="126972" type="text/json">{"id":126972,"name":"P-glycoprotein","url":"https://www.academia.edu/Documents/in/P-glycoprotein?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="438985" rel="nofollow" href="https://www.academia.edu/Documents/in/Methotrexate">Methotrexate</a>, <script data-card-contents-for-ri="438985" type="text/json">{"id":438985,"name":"Methotrexate","url":"https://www.academia.edu/Documents/in/Methotrexate?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="525429" rel="nofollow" href="https://www.academia.edu/Documents/in/Ovarian_Carcinoma">Ovarian Carcinoma</a><script data-card-contents-for-ri="525429" type="text/json">{"id":525429,"name":"Ovarian Carcinoma","url":"https://www.academia.edu/Documents/in/Ovarian_Carcinoma?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=3659044]'), work: {"id":3659044,"title":"Antifolate resistance mediated by the multidrug resistance proteins MRP1 and MRP2","created_at":"2013-06-05T06:47:44.918-07:00","url":"https://www.academia.edu/3659044/Antifolate_resistance_mediated_by_the_multidrug_resistance_proteins_MRP1_and_MRP2?f_ri=1816594","dom_id":"work_3659044","summary":"Transfection of multidrug resistance proteins (MRPs) MRP1 and MRP2 in human ovarian carcinoma 2008 cells conferred a marked level of resistance to short-term (1-4 h) exposure to the polyglutamatable antifolates methotrexate (MTX; 21-74-fold), ZD1694 (4 -138-fold), and GW1843 (101-156-fold). Evidence for MRP-mediated antifolate efflux relies upon the following findings: (a) a 2-3.3-fold lower accumulation of [ 3 H]MTX and subsequent reduced formation of long-chain polyglutamate forms of MTX; (b) reversal of MTX resistance by probenecid in both transfectants, and (c) ATP-dependent uptake of [ 3 H]MTX in inside-out vesicles of MRP1 and MRP2 transfectants. This report provides a mechanistic basis for resistance to polyglutamatable antifolates through an MRP-mediated drug extrusion. . 3 The abbreviations used are: MTX, methotrexate; DHFR, dihydrofolate reductase; RFC, reduced folate carrier; FPGS, folylpoly-␥-glutamate synthetase; MRP, multidrug resistance protein; HBS, HEPES-buffered saline. 4 M. Kool et al., manuscript in preparation.","downloadable_attachments":[{"id":31351158,"asset_id":3659044,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":4444753,"first_name":"Rik","last_name":"Kool","domain_name":"independent","page_name":"RikKool","display_name":"Rik Kool","profile_url":"https://independent.academia.edu/RikKool?f_ri=1816594","photo":"https://0.academia-photos.com/4444753/1815330/2162510/s65_rik.kool.jpg"}],"research_interests":[{"id":6021,"name":"Cancer","url":"https://www.academia.edu/Documents/in/Cancer?f_ri=1816594","nofollow":true},{"id":126972,"name":"P-glycoprotein","url":"https://www.academia.edu/Documents/in/P-glycoprotein?f_ri=1816594","nofollow":true},{"id":438985,"name":"Methotrexate","url":"https://www.academia.edu/Documents/in/Methotrexate?f_ri=1816594","nofollow":true},{"id":525429,"name":"Ovarian Carcinoma","url":"https://www.academia.edu/Documents/in/Ovarian_Carcinoma?f_ri=1816594","nofollow":true},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1947600,"name":"Quinazolines","url":"https://www.academia.edu/Documents/in/Quinazolines?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_7805815" data-work_id="7805815" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/7805815/Calcium_transport_by_cardiac_sarcoplasmic_reticulum_and_phosphorylation_of_phospholamban">Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Active calcium transport by cardiac sarcoplasmic reticulum assumes a central role in the excitation-concentration coupling of the myocardium, in that Ca2+-dependent ATPase (mol.wt. 100 000) of cardiac sarcoplasmic reticulum serves as an... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_7805815" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Active calcium transport by cardiac sarcoplasmic reticulum assumes a central role in the excitation-concentration coupling of the myocardium, in that Ca2+-dependent ATPase (mol.wt. 100 000) of cardiac sarcoplasmic reticulum serves as an energy transducer and a translocator of Ca2+ across the membrane. During the translocation of Ca2+, the ATPase undergoes a complex series of reactions during which the phosphorylated intermediate EP is formed. We documented how the elementary steps of the ATPase reaction are coupled with calcium translocation, and provided evidences to indicate that two key steps of ATPase correspond to the conformational change of the enzyme, and appear to alter the affinity of the enzyme for Ca2+. A line of evidence also indicated that Ca2+-dependent ATPase of cardiac sarcoplasmic reticulum is regulated by a specific protein named phospholamban (mol.wt. 22 000), which serves as a substrate for cyclic AMP-dependent protein kinase. Cyclic AMP-dependent phosphorylation of phospholamban resulted in a marked increase in the rate of turnover of the ATPase, by enhancing the rates of the key elementary steps, i.e. the steps at which the intermediate EP is formed and decomposed. Thus phospholamban is putatively thought to serve as a modulator of Cat2+-dependent ATPase of cardiac sarcoplasmic reticulum. A working model was proposed to interpret the mechanism. Also documented is a possibility that another protein kinase activatable by Ca2+ and calmodulin is functional in regulating the phospholamban-ATPase system, thus suggesting the existence of a dual control system, in which both cyclic AMP- and calmodulin-dependent phosphorylation are in control of the Cat2+-dependent ATPase. Such a control mechanism may provide the interpretation, at the cellular level, that catecholamines exert actions on myocardial contractility. Thus, catecholamine-mediated increases in intracellular cyclic AMP could enhance calcium fluxes across the membrane of sarcoplasmic reticulum, thus resulting in the increased rates of relaxation and, at the same time, the increased rate and extent of contraction. Such a mechanism could also be operational in the tissues, other than the myocardium, in which catecholamines and other hormones serve as the ‘first messenger’, producing intracellular cyclic AMP as the ‘second messenger’.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/7805815" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="c60564155f172a17f7bd756874ef030a" rel="nofollow" data-download="{"attachment_id":48335017,"asset_id":7805815,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/48335017/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="14458805" href="https://yamaguchi-u.academia.edu/MakotoInui">Makoto Inui</a><script data-card-contents-for-user="14458805" type="text/json">{"id":14458805,"first_name":"Makoto","last_name":"Inui","domain_name":"yamaguchi-u","page_name":"MakotoInui","display_name":"Makoto Inui","profile_url":"https://yamaguchi-u.academia.edu/MakotoInui?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_7805815 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="7805815"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 7805815, container: ".js-paper-rank-work_7805815", }); });</script></li><li class="js-percentile-work_7805815 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 7805815; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_7805815"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_7805815 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="7805815"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 7805815; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=7805815]").text(description); $(".js-view-count-work_7805815").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_7805815").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="7805815"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">13</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="92680" rel="nofollow" href="https://www.academia.edu/Documents/in/cyclic_AMP">cyclic AMP</a>, <script data-card-contents-for-ri="92680" type="text/json">{"id":92680,"name":"cyclic AMP","url":"https://www.academia.edu/Documents/in/cyclic_AMP?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="122188" rel="nofollow" href="https://www.academia.edu/Documents/in/Cell_Fractionation">Cell Fractionation</a>, <script data-card-contents-for-ri="122188" type="text/json">{"id":122188,"name":"Cell Fractionation","url":"https://www.academia.edu/Documents/in/Cell_Fractionation?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="172083" rel="nofollow" href="https://www.academia.edu/Documents/in/Phosphorylation">Phosphorylation</a><script data-card-contents-for-ri="172083" type="text/json">{"id":172083,"name":"Phosphorylation","url":"https://www.academia.edu/Documents/in/Phosphorylation?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=7805815]'), work: {"id":7805815,"title":"Calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of phospholamban","created_at":"2014-07-28T20:35:20.053-07:00","url":"https://www.academia.edu/7805815/Calcium_transport_by_cardiac_sarcoplasmic_reticulum_and_phosphorylation_of_phospholamban?f_ri=1816594","dom_id":"work_7805815","summary":"Active calcium transport by cardiac sarcoplasmic reticulum assumes a central role in the excitation-concentration coupling of the myocardium, in that Ca2+-dependent ATPase (mol.wt. 100 000) of cardiac sarcoplasmic reticulum serves as an energy transducer and a translocator of Ca2+ across the membrane. During the translocation of Ca2+, the ATPase undergoes a complex series of reactions during which the phosphorylated intermediate EP is formed. We documented how the elementary steps of the ATPase reaction are coupled with calcium translocation, and provided evidences to indicate that two key steps of ATPase correspond to the conformational change of the enzyme, and appear to alter the affinity of the enzyme for Ca2+. A line of evidence also indicated that Ca2+-dependent ATPase of cardiac sarcoplasmic reticulum is regulated by a specific protein named phospholamban (mol.wt. 22 000), which serves as a substrate for cyclic AMP-dependent protein kinase. Cyclic AMP-dependent phosphorylation of phospholamban resulted in a marked increase in the rate of turnover of the ATPase, by enhancing the rates of the key elementary steps, i.e. the steps at which the intermediate EP is formed and decomposed. Thus phospholamban is putatively thought to serve as a modulator of Cat2+-dependent ATPase of cardiac sarcoplasmic reticulum. A working model was proposed to interpret the mechanism. Also documented is a possibility that another protein kinase activatable by Ca2+ and calmodulin is functional in regulating the phospholamban-ATPase system, thus suggesting the existence of a dual control system, in which both cyclic AMP- and calmodulin-dependent phosphorylation are in control of the Cat2+-dependent ATPase. Such a control mechanism may provide the interpretation, at the cellular level, that catecholamines exert actions on myocardial contractility. Thus, catecholamine-mediated increases in intracellular cyclic AMP could enhance calcium fluxes across the membrane of sarcoplasmic reticulum, thus resulting in the increased rates of relaxation and, at the same time, the increased rate and extent of contraction. Such a mechanism could also be operational in the tissues, other than the myocardium, in which catecholamines and other hormones serve as the ‘first messenger’, producing intracellular cyclic AMP as the ‘second messenger’.","downloadable_attachments":[{"id":48335017,"asset_id":7805815,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":14458805,"first_name":"Makoto","last_name":"Inui","domain_name":"yamaguchi-u","page_name":"MakotoInui","display_name":"Makoto Inui","profile_url":"https://yamaguchi-u.academia.edu/MakotoInui?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":92680,"name":"cyclic AMP","url":"https://www.academia.edu/Documents/in/cyclic_AMP?f_ri=1816594","nofollow":true},{"id":122188,"name":"Cell Fractionation","url":"https://www.academia.edu/Documents/in/Cell_Fractionation?f_ri=1816594","nofollow":true},{"id":172083,"name":"Phosphorylation","url":"https://www.academia.edu/Documents/in/Phosphorylation?f_ri=1816594","nofollow":true},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme?f_ri=1816594"},{"id":392828,"name":"Myocardium","url":"https://www.academia.edu/Documents/in/Myocardium?f_ri=1816594"},{"id":426260,"name":"Calmodulin","url":"https://www.academia.edu/Documents/in/Calmodulin?f_ri=1816594"},{"id":889628,"name":"Calcium Binding Proteins","url":"https://www.academia.edu/Documents/in/Calcium_Binding_Proteins?f_ri=1816594"},{"id":1274450,"name":"Conformational Change","url":"https://www.academia.edu/Documents/in/Conformational_Change?f_ri=1816594"},{"id":1296969,"name":"Molecular and Cellular Biochemistry","url":"https://www.academia.edu/Documents/in/Molecular_and_Cellular_Biochemistry?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2350842,"name":"Sarcoplasmic reticulum","url":"https://www.academia.edu/Documents/in/Sarcoplasmic_reticulum?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_10098393" data-work_id="10098393" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/10098393/Acidosis_induced_relaxation_of_human_internal_mammary_artery_is_due_to_activation_of_ATP_sensitive_potassium_channels">Acidosis-induced relaxation of human internal mammary artery is due to activation of ATP-sensitive potassium channels</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Metabolic acidosis is associated with various clinical situations including diabetes mellitus and renal diseases. The aim of this study was to investigate the effects of acidosis on the resting as well as precontracted human left internal... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_10098393" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Metabolic acidosis is associated with various clinical situations including diabetes mellitus and renal diseases. The aim of this study was to investigate the effects of acidosis on the resting as well as precontracted human left internal mammary artery. The vessels were obtained from the patients undergoing coronary artery bypass grafting surgery at The Aga Khan University Hospital, Karachi. Left internal mammary artery was cut into rings and isometric tension recording experiments were performed. Decrease in pH of the bathing solution from 7.4 to 6.8 had no effect on the resting tension of left internal mammary artery, whereas, acidic pH markedly relaxed the contractions to 24.8 mM KCl and 300 nM phenylephrine. Interestingly, when the KCl-or phenylephrine-contracted rings were treated with 3 AM glibenclamide; an inhibitor of ATP-sensitive potassium (K ATP ) channels, the relaxant effect of acidosis was abolished. Similarly, acidosis failed to cause relaxation of 100 nM endothelin-1-induced contraction in Ca 2+ -free bathing solution or in the presence of a voltage-dependent Ca 2+ channel inhibitor, verapamil (10 AM), whereas, endothelin-1-induced contraction was attenuated by acidosis in Ca 2+ -containing normal solution. From all these data, it is concluded that under the acidic pH conditions, opening of K ATP channels occurs; resulting in the hyperpolarization, decrease in Ca 2+ influx via voltage-dependent Ca 2+ channels and subsequent relaxation of human left internal mammary artery. D</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/10098393" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="dbb2eaf717a0685b10a9b26d5cef3ff4" rel="nofollow" data-download="{"attachment_id":47532658,"asset_id":10098393,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/47532658/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="24608824" href="https://independent.academia.edu/HZubairi">Hina Zubairi</a><script data-card-contents-for-user="24608824" type="text/json">{"id":24608824,"first_name":"Hina","last_name":"Zubairi","domain_name":"independent","page_name":"HZubairi","display_name":"Hina Zubairi","profile_url":"https://independent.academia.edu/HZubairi?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_10098393 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="10098393"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 10098393, container: ".js-paper-rank-work_10098393", }); 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$(".js-view-count[data-work-id=10098393]").text(description); $(".js-view-count-work_10098393").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_10098393").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="10098393"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">15</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="71511" rel="nofollow" href="https://www.academia.edu/Documents/in/Diabetes_mellitus">Diabetes mellitus</a>, <script data-card-contents-for-ri="71511" type="text/json">{"id":71511,"name":"Diabetes mellitus","url":"https://www.academia.edu/Documents/in/Diabetes_mellitus?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="84278" href="https://www.academia.edu/Documents/in/Ph">Ph</a>, <script data-card-contents-for-ri="84278" type="text/json">{"id":84278,"name":"Ph","url":"https://www.academia.edu/Documents/in/Ph?f_ri=1816594","nofollow":false}</script><a class="InlineList-item-text" data-has-card-for-ri="160656" rel="nofollow" href="https://www.academia.edu/Documents/in/Potassium">Potassium</a><script data-card-contents-for-ri="160656" type="text/json">{"id":160656,"name":"Potassium","url":"https://www.academia.edu/Documents/in/Potassium?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=10098393]'), work: {"id":10098393,"title":"Acidosis-induced relaxation of human internal mammary artery is due to activation of ATP-sensitive potassium channels","created_at":"2015-01-10T05:00:30.732-08:00","url":"https://www.academia.edu/10098393/Acidosis_induced_relaxation_of_human_internal_mammary_artery_is_due_to_activation_of_ATP_sensitive_potassium_channels?f_ri=1816594","dom_id":"work_10098393","summary":"Metabolic acidosis is associated with various clinical situations including diabetes mellitus and renal diseases. The aim of this study was to investigate the effects of acidosis on the resting as well as precontracted human left internal mammary artery. The vessels were obtained from the patients undergoing coronary artery bypass grafting surgery at The Aga Khan University Hospital, Karachi. Left internal mammary artery was cut into rings and isometric tension recording experiments were performed. Decrease in pH of the bathing solution from 7.4 to 6.8 had no effect on the resting tension of left internal mammary artery, whereas, acidic pH markedly relaxed the contractions to 24.8 mM KCl and 300 nM phenylephrine. Interestingly, when the KCl-or phenylephrine-contracted rings were treated with 3 AM glibenclamide; an inhibitor of ATP-sensitive potassium (K ATP ) channels, the relaxant effect of acidosis was abolished. Similarly, acidosis failed to cause relaxation of 100 nM endothelin-1-induced contraction in Ca 2+ -free bathing solution or in the presence of a voltage-dependent Ca 2+ channel inhibitor, verapamil (10 AM), whereas, endothelin-1-induced contraction was attenuated by acidosis in Ca 2+ -containing normal solution. From all these data, it is concluded that under the acidic pH conditions, opening of K ATP channels occurs; resulting in the hyperpolarization, decrease in Ca 2+ influx via voltage-dependent Ca 2+ channels and subsequent relaxation of human left internal mammary artery. D","downloadable_attachments":[{"id":47532658,"asset_id":10098393,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":24608824,"first_name":"Hina","last_name":"Zubairi","domain_name":"independent","page_name":"HZubairi","display_name":"Hina Zubairi","profile_url":"https://independent.academia.edu/HZubairi?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":71511,"name":"Diabetes mellitus","url":"https://www.academia.edu/Documents/in/Diabetes_mellitus?f_ri=1816594","nofollow":true},{"id":84278,"name":"Ph","url":"https://www.academia.edu/Documents/in/Ph?f_ri=1816594","nofollow":false},{"id":160656,"name":"Potassium","url":"https://www.academia.edu/Documents/in/Potassium?f_ri=1816594","nofollow":true},{"id":204388,"name":"Vasoconstriction","url":"https://www.academia.edu/Documents/in/Vasoconstriction?f_ri=1816594"},{"id":279027,"name":"European","url":"https://www.academia.edu/Documents/in/European?f_ri=1816594"},{"id":557691,"name":"Potassium Channels","url":"https://www.academia.edu/Documents/in/Potassium_Channels?f_ri=1816594"},{"id":612864,"name":"Metabolic Acidosis","url":"https://www.academia.edu/Documents/in/Metabolic_Acidosis?f_ri=1816594"},{"id":910989,"name":"Acidosis","url":"https://www.academia.edu/Documents/in/Acidosis?f_ri=1816594"},{"id":1035420,"name":"Vasodilation","url":"https://www.academia.edu/Documents/in/Vasodilation?f_ri=1816594"},{"id":1137254,"name":"Hydrogen-Ion Concentration","url":"https://www.academia.edu/Documents/in/Hydrogen-Ion_Concentration?f_ri=1816594"},{"id":1180098,"name":"Renal disease","url":"https://www.academia.edu/Documents/in/Renal_disease?f_ri=1816594"},{"id":1722637,"name":"Verapamil","url":"https://www.academia.edu/Documents/in/Verapamil?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2277783,"name":"Vascular Smooth Muscle","url":"https://www.academia.edu/Documents/in/Vascular_Smooth_Muscle?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_24967536" data-work_id="24967536" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/24967536/A_Rab1_homologue_with_a_novel_isoprenylation_signal_provides_insight_into_the_secretory_pathway_of_Theileria_parva">A Rab1 homologue with a novel isoprenylation signal provides insight into the secretory pathway of Theileria parva</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">As a first step in developing compartment-specific markers for protein trafficking within Theileria par6a, we have isolated cDNAs encoding homologues of the small GTP binding proteins Rab1 and Rab4. The T. par6a homologue of Rab1... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_24967536" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">As a first step in developing compartment-specific markers for protein trafficking within Theileria par6a, we have isolated cDNAs encoding homologues of the small GTP binding proteins Rab1 and Rab4. The T. par6a homologue of Rab1 (TpRab1), a protein which regulates vesicular transport between the endoplasmic reticulum and cis golgi in other organisms, was unusual in that it contained a unique 17 amino acid C-terminal extension. The C-terminal motif sequence KCT (XCX) contrasted with the CXC or XCC motifs which act as as signals for isoprenylation by geranylgeranyl in most Rab proteins, including all known Rab1 homologues, in containing only a single cysteine. [C 14 ]mevalonic acid lactone and [H 3 ]geranylgeranyl pyrophosphate were specifically incorporated into recombinant TpRab1 in vitro, demonstrating that the novel motif was functional for isoprenylation. Recombinant TpRab1 bound radiolabeled GTP, and this binding was inhibited by excess unlabeled GTP and GDP and also partially by ATP. The TpRab1 gene contained four short (34-67 bp) introns with a distinct pattern of occurrence within the protein sequence as compared to the introns of other lower eukaryote Rab1 genes. Immunofluorescence microscopy using antiserum specific for the novel C-terminal peptide in combination with labelling of cells using the nucleic acid-staining dye DAPI, indicated that TpRab1 was located in the vicinity of the schizont nucleus within the infected lymphocyte.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/24967536" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="f1bb78581885d954a92c5f62467b0442" rel="nofollow" data-download="{"attachment_id":45299072,"asset_id":24967536,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45299072/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="47948121" href="https://independent.academia.edu/AnthonyMusoke">Anthony Musoke</a><script data-card-contents-for-user="47948121" type="text/json">{"id":47948121,"first_name":"Anthony","last_name":"Musoke","domain_name":"independent","page_name":"AnthonyMusoke","display_name":"Anthony Musoke","profile_url":"https://independent.academia.edu/AnthonyMusoke?f_ri=1816594","photo":"https://0.academia-photos.com/47948121/12677681/14101964/s65_anthony.musoke.jpg"}</script></span></span></li><li class="js-paper-rank-work_24967536 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="24967536"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 24967536, container: ".js-paper-rank-work_24967536", }); });</script></li><li class="js-percentile-work_24967536 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 24967536; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_24967536"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_24967536 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="24967536"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 24967536; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=24967536]").text(description); $(".js-view-count-work_24967536").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_24967536").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="24967536"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">18</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="38831" rel="nofollow" href="https://www.academia.edu/Documents/in/Signal_Transduction">Signal Transduction</a>, <script data-card-contents-for-ri="38831" type="text/json">{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="47884" rel="nofollow" href="https://www.academia.edu/Documents/in/Biological_Sciences">Biological Sciences</a>, <script data-card-contents-for-ri="47884" type="text/json">{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="87023" rel="nofollow" href="https://www.academia.edu/Documents/in/Secretory_Pathway">Secretory Pathway</a>, <script data-card-contents-for-ri="87023" type="text/json">{"id":87023,"name":"Secretory Pathway","url":"https://www.academia.edu/Documents/in/Secretory_Pathway?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="122187" rel="nofollow" href="https://www.academia.edu/Documents/in/Endoplasmic_Reticulum">Endoplasmic Reticulum</a><script data-card-contents-for-ri="122187" type="text/json">{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=24967536]'), work: {"id":24967536,"title":"A Rab1 homologue with a novel isoprenylation signal provides insight into the secretory pathway of Theileria parva","created_at":"2016-05-02T23:24:15.339-07:00","url":"https://www.academia.edu/24967536/A_Rab1_homologue_with_a_novel_isoprenylation_signal_provides_insight_into_the_secretory_pathway_of_Theileria_parva?f_ri=1816594","dom_id":"work_24967536","summary":"As a first step in developing compartment-specific markers for protein trafficking within Theileria par6a, we have isolated cDNAs encoding homologues of the small GTP binding proteins Rab1 and Rab4. The T. par6a homologue of Rab1 (TpRab1), a protein which regulates vesicular transport between the endoplasmic reticulum and cis golgi in other organisms, was unusual in that it contained a unique 17 amino acid C-terminal extension. The C-terminal motif sequence KCT (XCX) contrasted with the CXC or XCC motifs which act as as signals for isoprenylation by geranylgeranyl in most Rab proteins, including all known Rab1 homologues, in containing only a single cysteine. [C 14 ]mevalonic acid lactone and [H 3 ]geranylgeranyl pyrophosphate were specifically incorporated into recombinant TpRab1 in vitro, demonstrating that the novel motif was functional for isoprenylation. Recombinant TpRab1 bound radiolabeled GTP, and this binding was inhibited by excess unlabeled GTP and GDP and also partially by ATP. The TpRab1 gene contained four short (34-67 bp) introns with a distinct pattern of occurrence within the protein sequence as compared to the introns of other lower eukaryote Rab1 genes. Immunofluorescence microscopy using antiserum specific for the novel C-terminal peptide in combination with labelling of cells using the nucleic acid-staining dye DAPI, indicated that TpRab1 was located in the vicinity of the schizont nucleus within the infected lymphocyte.","downloadable_attachments":[{"id":45299072,"asset_id":24967536,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":47948121,"first_name":"Anthony","last_name":"Musoke","domain_name":"independent","page_name":"AnthonyMusoke","display_name":"Anthony Musoke","profile_url":"https://independent.academia.edu/AnthonyMusoke?f_ri=1816594","photo":"https://0.academia-photos.com/47948121/12677681/14101964/s65_anthony.musoke.jpg"}],"research_interests":[{"id":38831,"name":"Signal Transduction","url":"https://www.academia.edu/Documents/in/Signal_Transduction?f_ri=1816594","nofollow":true},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences?f_ri=1816594","nofollow":true},{"id":87023,"name":"Secretory Pathway","url":"https://www.academia.edu/Documents/in/Secretory_Pathway?f_ri=1816594","nofollow":true},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum?f_ri=1816594","nofollow":true},{"id":202207,"name":"Protein Trafficking","url":"https://www.academia.edu/Documents/in/Protein_Trafficking?f_ri=1816594"},{"id":283547,"name":"Introns","url":"https://www.academia.edu/Documents/in/Introns?f_ri=1816594"},{"id":295728,"name":"Molecular cloning","url":"https://www.academia.edu/Documents/in/Molecular_cloning?f_ri=1816594"},{"id":300829,"name":"Protein Sequence Analysis","url":"https://www.academia.edu/Documents/in/Protein_Sequence_Analysis?f_ri=1816594"},{"id":323597,"name":"Fluorescent Antibody Technique","url":"https://www.academia.edu/Documents/in/Fluorescent_Antibody_Technique?f_ri=1816594"},{"id":585573,"name":"Amino Acid Profile","url":"https://www.academia.edu/Documents/in/Amino_Acid_Profile?f_ri=1816594"},{"id":602609,"name":"Intron","url":"https://www.academia.edu/Documents/in/Intron?f_ri=1816594"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence?f_ri=1816594"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence?f_ri=1816594"},{"id":868560,"name":"Lymphocytes","url":"https://www.academia.edu/Documents/in/Lymphocytes?f_ri=1816594"},{"id":990417,"name":"Recombinant Proteins","url":"https://www.academia.edu/Documents/in/Recombinant_Proteins?f_ri=1816594"},{"id":1321979,"name":"Theileria parva","url":"https://www.academia.edu/Documents/in/Theileria_parva?f_ri=1816594"},{"id":1727314,"name":"Nucleic Acid","url":"https://www.academia.edu/Documents/in/Nucleic_Acid?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_14034447" data-work_id="14034447" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/14034447/Agonist_binding_evokes_extensive_conformational_changes_in_the_extracellular_domain_of_the_ATP_gated_human_P2X1_receptor_ion_channel">Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">P2X receptors for ATP have a wide range of physiological roles and comprise a structurally distinct family of ligand-gated trimeric ion channels. The crystal structure of a P2X4 receptor, in combination with mutagenesis studies, has... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_14034447" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">P2X receptors for ATP have a wide range of physiological roles and comprise a structurally distinct family of ligand-gated trimeric ion channels. The crystal structure of a P2X4 receptor, in combination with mutagenesis studies, has provided a model of the intersubunit ATP-binding sites and identified an extracellular lateral portal, adjacent to the membrane, that funnels ions to the channel pore. However, little is known about the extent of ATP-induced conformational changes in the extracellular domain of the receptor. To address this issue, we have used MTSEA-biotinylation (N-Biotinoylaminoethyl methanethiosulfonate) to show ATP-sensitive accessibility of cysteine mutants at the human P2X1 receptor. Mapping these data to a P2X1 receptor homology model identifies significant conformational rearrangement. Electron microscopy of purified P2X1 receptors showed marked changes in structure on ATP binding, and introducing disulphide bonds between adjacent subunits to restrict intersubunit movements inhibited channel function. These results are consistent with agonist-induced rotation of the propeller-head domain of the receptor, sliding of adjacent subunits leading to restricted access to the upper vestibule, movement in the ion conducting lateral portals, and gating of the channel pore.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/14034447" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="e90eaae55cecee7d965cafc7e534c8a3" rel="nofollow" data-download="{"attachment_id":44681143,"asset_id":14034447,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/44681143/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33060581" href="https://montana.academia.edu/MarkYoung">Mark Young</a><script data-card-contents-for-user="33060581" type="text/json">{"id":33060581,"first_name":"Mark","last_name":"Young","domain_name":"montana","page_name":"MarkYoung","display_name":"Mark Young","profile_url":"https://montana.academia.edu/MarkYoung?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_14034447 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="14034447"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 14034447, container: ".js-paper-rank-work_14034447", }); });</script></li><li class="js-percentile-work_14034447 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 14034447; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_14034447"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_14034447 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="14034447"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 14034447; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=14034447]").text(description); $(".js-view-count-work_14034447").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_14034447").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="14034447"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">11</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="2184" rel="nofollow" href="https://www.academia.edu/Documents/in/Electron_Microscopy">Electron Microscopy</a>, <script data-card-contents-for-ri="2184" type="text/json">{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="28235" rel="nofollow" href="https://www.academia.edu/Documents/in/Multidisciplinary">Multidisciplinary</a>, <script data-card-contents-for-ri="28235" type="text/json">{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="57440" rel="nofollow" href="https://www.academia.edu/Documents/in/Xenopus">Xenopus</a>, <script data-card-contents-for-ri="57440" type="text/json">{"id":57440,"name":"Xenopus","url":"https://www.academia.edu/Documents/in/Xenopus?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="67401" rel="nofollow" href="https://www.academia.edu/Documents/in/Mutagenesis">Mutagenesis</a><script data-card-contents-for-ri="67401" type="text/json">{"id":67401,"name":"Mutagenesis","url":"https://www.academia.edu/Documents/in/Mutagenesis?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=14034447]'), work: {"id":14034447,"title":"Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel","created_at":"2015-07-14T07:27:34.832-07:00","url":"https://www.academia.edu/14034447/Agonist_binding_evokes_extensive_conformational_changes_in_the_extracellular_domain_of_the_ATP_gated_human_P2X1_receptor_ion_channel?f_ri=1816594","dom_id":"work_14034447","summary":"P2X receptors for ATP have a wide range of physiological roles and comprise a structurally distinct family of ligand-gated trimeric ion channels. The crystal structure of a P2X4 receptor, in combination with mutagenesis studies, has provided a model of the intersubunit ATP-binding sites and identified an extracellular lateral portal, adjacent to the membrane, that funnels ions to the channel pore. However, little is known about the extent of ATP-induced conformational changes in the extracellular domain of the receptor. To address this issue, we have used MTSEA-biotinylation (N-Biotinoylaminoethyl methanethiosulfonate) to show ATP-sensitive accessibility of cysteine mutants at the human P2X1 receptor. Mapping these data to a P2X1 receptor homology model identifies significant conformational rearrangement. Electron microscopy of purified P2X1 receptors showed marked changes in structure on ATP binding, and introducing disulphide bonds between adjacent subunits to restrict intersubunit movements inhibited channel function. These results are consistent with agonist-induced rotation of the propeller-head domain of the receptor, sliding of adjacent subunits leading to restricted access to the upper vestibule, movement in the ion conducting lateral portals, and gating of the channel pore.","downloadable_attachments":[{"id":44681143,"asset_id":14034447,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":33060581,"first_name":"Mark","last_name":"Young","domain_name":"montana","page_name":"MarkYoung","display_name":"Mark Young","profile_url":"https://montana.academia.edu/MarkYoung?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":2184,"name":"Electron Microscopy","url":"https://www.academia.edu/Documents/in/Electron_Microscopy?f_ri=1816594","nofollow":true},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary?f_ri=1816594","nofollow":true},{"id":57440,"name":"Xenopus","url":"https://www.academia.edu/Documents/in/Xenopus?f_ri=1816594","nofollow":true},{"id":67401,"name":"Mutagenesis","url":"https://www.academia.edu/Documents/in/Mutagenesis?f_ri=1816594","nofollow":true},{"id":649537,"name":"Molecular Conformation","url":"https://www.academia.edu/Documents/in/Molecular_Conformation?f_ri=1816594"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation?f_ri=1816594"},{"id":956315,"name":"Oocytes","url":"https://www.academia.edu/Documents/in/Oocytes?f_ri=1816594"},{"id":1010725,"name":"Protein Binding","url":"https://www.academia.edu/Documents/in/Protein_Binding?f_ri=1816594"},{"id":1257974,"name":"Ions","url":"https://www.academia.edu/Documents/in/Ions?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":1835689,"name":"Biotinylation","url":"https://www.academia.edu/Documents/in/Biotinylation?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_13399205" data-work_id="13399205" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/13399205/Metabolic_Approaches_to_Treatment_of_Melanoma">Metabolic Approaches to Treatment of Melanoma</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Purpose: Lactate dehydrogenase (LDH) levels in blood of patients with melanoma have proven to be an accurate predictor of prognosis and response to some treatments. Exclusion of patients with high LDH levels from many trials of new... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_13399205" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Purpose: Lactate dehydrogenase (LDH) levels in blood of patients with melanoma have proven to be an accurate predictor of prognosis and response to some treatments. Exclusion of patients with high LDH levels from many trials of new treatments has created a need for treatments aimed at patients with high LDH levels. This article reviews the metabolic basis for the association of LDH with prognosis and the treatment initiatives that may be successful in this patient group. Experimental Design: Review of current literature on the topic. Results: A number of new treatment initiatives based on manipulation of metabolic pathways in melanoma cells are now available and await evaluation in well-designed clinical trials. Conclusions: Different cancers may require different metabolic approaches for effective treatment. In view of the high rate of glycolysis in most melanoma cells, approaches based on inhibition of acid excretion from the cells seem particularly attractive. (Clin Cancer Res 2009;15(21):6490-4)</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/13399205" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="cbcc719a982adc10972b27f2e52b18c0" rel="nofollow" data-download="{"attachment_id":45386798,"asset_id":13399205,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/45386798/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32625045" href="https://sydney.academia.edu/PeterHersey">Peter Hersey</a><script data-card-contents-for-user="32625045" type="text/json">{"id":32625045,"first_name":"Peter","last_name":"Hersey","domain_name":"sydney","page_name":"PeterHersey","display_name":"Peter Hersey","profile_url":"https://sydney.academia.edu/PeterHersey?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_13399205 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="13399205"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 13399205, container: ".js-paper-rank-work_13399205", }); 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$(".js-view-count[data-work-id=13399205]").text(description); $(".js-view-count-work_13399205").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_13399205").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="13399205"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">6</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="99023" rel="nofollow" href="https://www.academia.edu/Documents/in/Melanoma">Melanoma</a>, <script data-card-contents-for-ri="99023" type="text/json">{"id":99023,"name":"Melanoma","url":"https://www.academia.edu/Documents/in/Melanoma?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="172897" rel="nofollow" href="https://www.academia.edu/Documents/in/Glycolysis">Glycolysis</a>, <script data-card-contents-for-ri="172897" type="text/json">{"id":172897,"name":"Glycolysis","url":"https://www.academia.edu/Documents/in/Glycolysis?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="489727" rel="nofollow" href="https://www.academia.edu/Documents/in/Prognosis">Prognosis</a>, <script data-card-contents-for-ri="489727" type="text/json">{"id":489727,"name":"Prognosis","url":"https://www.academia.edu/Documents/in/Prognosis?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="1074508" rel="nofollow" href="https://www.academia.edu/Documents/in/Lactic_Acid">Lactic Acid</a><script data-card-contents-for-ri="1074508" type="text/json">{"id":1074508,"name":"Lactic Acid","url":"https://www.academia.edu/Documents/in/Lactic_Acid?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=13399205]'), work: {"id":13399205,"title":"Metabolic Approaches to Treatment of Melanoma","created_at":"2015-06-28T22:09:52.413-07:00","url":"https://www.academia.edu/13399205/Metabolic_Approaches_to_Treatment_of_Melanoma?f_ri=1816594","dom_id":"work_13399205","summary":"Purpose: Lactate dehydrogenase (LDH) levels in blood of patients with melanoma have proven to be an accurate predictor of prognosis and response to some treatments. Exclusion of patients with high LDH levels from many trials of new treatments has created a need for treatments aimed at patients with high LDH levels. This article reviews the metabolic basis for the association of LDH with prognosis and the treatment initiatives that may be successful in this patient group. Experimental Design: Review of current literature on the topic. Results: A number of new treatment initiatives based on manipulation of metabolic pathways in melanoma cells are now available and await evaluation in well-designed clinical trials. Conclusions: Different cancers may require different metabolic approaches for effective treatment. In view of the high rate of glycolysis in most melanoma cells, approaches based on inhibition of acid excretion from the cells seem particularly attractive. (Clin Cancer Res 2009;15(21):6490-4)","downloadable_attachments":[{"id":45386798,"asset_id":13399205,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32625045,"first_name":"Peter","last_name":"Hersey","domain_name":"sydney","page_name":"PeterHersey","display_name":"Peter Hersey","profile_url":"https://sydney.academia.edu/PeterHersey?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":99023,"name":"Melanoma","url":"https://www.academia.edu/Documents/in/Melanoma?f_ri=1816594","nofollow":true},{"id":172897,"name":"Glycolysis","url":"https://www.academia.edu/Documents/in/Glycolysis?f_ri=1816594","nofollow":true},{"id":489727,"name":"Prognosis","url":"https://www.academia.edu/Documents/in/Prognosis?f_ri=1816594","nofollow":true},{"id":1074508,"name":"Lactic Acid","url":"https://www.academia.edu/Documents/in/Lactic_Acid?f_ri=1816594","nofollow":true},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":2177223,"name":"Skin Neoplasms","url":"https://www.academia.edu/Documents/in/Skin_Neoplasms?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_23973102" data-work_id="23973102" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/23973102/Endothelium_dependent_and_independent_effects_of_exogenous_ATP_adenosine_GTP_and_guanosine_on_vascular_tone_and_cyclic_nucleotide_accumulation_of_rat_mesenteric_artery">Endothelium-dependent and -independent effects of exogenous ATP, adenosine, GTP and guanosine on vascular tone and cyclic nucleotide accumulation of rat mesenteric artery</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">1 The effects of exogenous guanosine 5'-triphosphate (GTP) and guanosine on vascular tone and cyclic nucleotide accumulation of noradrenaline-precontracted endothelium-intact and endothelium-denuded rat mesenteric artery rings were... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_23973102" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">1 The effects of exogenous guanosine 5'-triphosphate (GTP) and guanosine on vascular tone and cyclic nucleotide accumulation of noradrenaline-precontracted endothelium-intact and endothelium-denuded rat mesenteric artery rings were compared with the effects of the known purinoceptor agonists adenosine 5'-triphosphate (ATP) and adenosine.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div 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data-has-card-for-ri="4083" rel="nofollow" href="https://www.academia.edu/Documents/in/Complementary_and_Alternative_Medicine">Complementary and Alternative Medicine</a>, <script data-card-contents-for-ri="4083" type="text/json">{"id":4083,"name":"Complementary and Alternative Medicine","url":"https://www.academia.edu/Documents/in/Complementary_and_Alternative_Medicine?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="5541" rel="nofollow" href="https://www.academia.edu/Documents/in/Plant_Biology">Plant Biology</a>, <script data-card-contents-for-ri="5541" type="text/json">{"id":5541,"name":"Plant Biology","url":"https://www.academia.edu/Documents/in/Plant_Biology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="14032" rel="nofollow" href="https://www.academia.edu/Documents/in/Ethnopharmacology">Ethnopharmacology</a>, <script data-card-contents-for-ri="14032" type="text/json">{"id":14032,"name":"Ethnopharmacology","url":"https://www.academia.edu/Documents/in/Ethnopharmacology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="15019" rel="nofollow" href="https://www.academia.edu/Documents/in/Medicinal_Plants">Medicinal Plants</a><script data-card-contents-for-ri="15019" type="text/json">{"id":15019,"name":"Medicinal Plants","url":"https://www.academia.edu/Documents/in/Medicinal_Plants?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=23973102]'), work: {"id":23973102,"title":"Endothelium-dependent and -independent effects of exogenous ATP, adenosine, GTP and guanosine on vascular tone and cyclic nucleotide accumulation of rat mesenteric artery","created_at":"2016-04-03T13:49:35.231-07:00","url":"https://www.academia.edu/23973102/Endothelium_dependent_and_independent_effects_of_exogenous_ATP_adenosine_GTP_and_guanosine_on_vascular_tone_and_cyclic_nucleotide_accumulation_of_rat_mesenteric_artery?f_ri=1816594","dom_id":"work_23973102","summary":"1 The effects of exogenous guanosine 5'-triphosphate (GTP) and guanosine on vascular tone and cyclic nucleotide accumulation of noradrenaline-precontracted endothelium-intact and endothelium-denuded rat mesenteric artery rings were compared with the effects of the known purinoceptor agonists adenosine 5'-triphosphate (ATP) and adenosine.","downloadable_attachments":[{"id":44362816,"asset_id":23973102,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":13588842,"first_name":"Yusuf","last_name":"Öztürk","domain_name":"aydin","page_name":"YusufÖztürk","display_name":"Yusuf Öztürk","profile_url":"https://aydin.academia.edu/Yusuf%C3%96zt%C3%BCrk?f_ri=1816594","photo":"https://0.academia-photos.com/13588842/3798116/140974022/s65_yusuf._zt_rk.jpg"}],"research_interests":[{"id":4083,"name":"Complementary and Alternative Medicine","url":"https://www.academia.edu/Documents/in/Complementary_and_Alternative_Medicine?f_ri=1816594","nofollow":true},{"id":5541,"name":"Plant Biology","url":"https://www.academia.edu/Documents/in/Plant_Biology?f_ri=1816594","nofollow":true},{"id":14032,"name":"Ethnopharmacology","url":"https://www.academia.edu/Documents/in/Ethnopharmacology?f_ri=1816594","nofollow":true},{"id":15019,"name":"Medicinal Plants","url":"https://www.academia.edu/Documents/in/Medicinal_Plants?f_ri=1816594","nofollow":true},{"id":61232,"name":"Adenosine","url":"https://www.academia.edu/Documents/in/Adenosine?f_ri=1816594"},{"id":92680,"name":"cyclic AMP","url":"https://www.academia.edu/Documents/in/cyclic_AMP?f_ri=1816594"},{"id":93922,"name":"Nitric oxide","url":"https://www.academia.edu/Documents/in/Nitric_oxide?f_ri=1816594"},{"id":138877,"name":"Vascular endothelium","url":"https://www.academia.edu/Documents/in/Vascular_endothelium?f_ri=1816594"},{"id":159958,"name":"Acetylcholine","url":"https://www.academia.edu/Documents/in/Acetylcholine?f_ri=1816594"},{"id":269567,"name":"Garlic","url":"https://www.academia.edu/Documents/in/Garlic?f_ri=1816594"},{"id":354056,"name":"Plant extracts","url":"https://www.academia.edu/Documents/in/Plant_extracts?f_ri=1816594"},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats?f_ri=1816594"},{"id":418954,"name":"Guanosine Triphosphate","url":"https://www.academia.edu/Documents/in/Guanosine_Triphosphate?f_ri=1816594"},{"id":555120,"name":"Arginine","url":"https://www.academia.edu/Documents/in/Arginine?f_ri=1816594"},{"id":1031515,"name":"Mesenteric Arteries","url":"https://www.academia.edu/Documents/in/Mesenteric_Arteries?f_ri=1816594"},{"id":1035092,"name":"Aorta","url":"https://www.academia.edu/Documents/in/Aorta?f_ri=1816594"},{"id":1272871,"name":"Muscle Relaxation","url":"https://www.academia.edu/Documents/in/Muscle_Relaxation?f_ri=1816594"},{"id":1597877,"name":"Nucleotides","url":"https://www.academia.edu/Documents/in/Nucleotides?f_ri=1816594"},{"id":1621881,"name":"cyclic GMP","url":"https://www.academia.edu/Documents/in/cyclic_GMP?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_56341281" data-work_id="56341281" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/56341281/The_role_of_mitochondria_in_energy_production_for_human_sperm_motility">The role of mitochondria in energy production for human sperm motility</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Mitochondria of spermatozoa are different from the corresponding organelles of somatic cells, in both their morphology and biochemistry. The biochemical differences are essentially related to the existence of specific enzyme isoforms,... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_56341281" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Mitochondria of spermatozoa are different from the corresponding organelles of somatic cells, in both their morphology and biochemistry. The biochemical differences are essentially related to the existence of specific enzyme isoforms, which are characterized by peculiar kinetic and regulatory properties. As mitochondrial energy metabolism is a key factor supporting several sperm functions, these organelles host critical metabolic pathways during germ cell development and fertilization. Furthermore, spermatozoa can use different substrates, and therefore activate different metabolic pathways, depending on the available substrates and the physico-chemical conditions in which they operate. This versatility is critical to ensure fertilization success. However, the most valuable aspect of mitochondria function in all types of cells is the production of chemical energy in the form of ATP which can be used, in the case of spermatozoa, for sustaining sperm motility. The latter, on the other hand, represents one of the major determinants of male fertility. Accordingly, the presence of structural and functional alterations in mitochondria from asthenozoospermic subjects confirms the important role played by these organelles in energy maintenance of sperm motility. The present study gives an overview of the current knowledge on the energy-producing metabolic pathways operating inside human sperm mitochondria and critically analyse the differences with respect to somatic mitochondria. Such a comparison has also been carried out between the functional characteristics of human sperm mitochondria and those of other mammalian species. A deeper understanding of mitochondrial energy metabolism could open up new avenues of investigation in bioenergetics of human sperm mitochondria, both in physiological and pathological conditions.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/56341281" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="84b60825f05b53ef29e0e447302ecbe1" rel="nofollow" data-download="{"attachment_id":71774311,"asset_id":56341281,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/71774311/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="32463735" href="https://unisalento.academia.edu/AFerramosca">A. Ferramosca</a><script data-card-contents-for-user="32463735" type="text/json">{"id":32463735,"first_name":"A.","last_name":"Ferramosca","domain_name":"unisalento","page_name":"AFerramosca","display_name":"A. Ferramosca","profile_url":"https://unisalento.academia.edu/AFerramosca?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_56341281 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="56341281"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 56341281, container: ".js-paper-rank-work_56341281", }); });</script></li><li class="js-percentile-work_56341281 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 56341281; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_56341281"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_56341281 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="56341281"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 56341281; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=56341281]").text(description); $(".js-view-count-work_56341281").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_56341281").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="56341281"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">12</a>  </div><span class="InlineList-item-text u-textTruncate u-pl10x"><a class="InlineList-item-text" data-has-card-for-ri="654" rel="nofollow" href="https://www.academia.edu/Documents/in/Andrology">Andrology</a>, <script data-card-contents-for-ri="654" type="text/json">{"id":654,"name":"Andrology","url":"https://www.academia.edu/Documents/in/Andrology?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="9534" rel="nofollow" href="https://www.academia.edu/Documents/in/Calcium">Calcium</a>, <script data-card-contents-for-ri="9534" type="text/json">{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="15719" rel="nofollow" href="https://www.academia.edu/Documents/in/Mitochondria">Mitochondria</a>, <script data-card-contents-for-ri="15719" type="text/json">{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="36213" rel="nofollow" href="https://www.academia.edu/Documents/in/Energy_Metabolism">Energy Metabolism</a><script data-card-contents-for-ri="36213" type="text/json">{"id":36213,"name":"Energy Metabolism","url":"https://www.academia.edu/Documents/in/Energy_Metabolism?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=56341281]'), work: {"id":56341281,"title":"The role of mitochondria in energy production for human sperm motility","created_at":"2021-10-07T08:41:34.027-07:00","url":"https://www.academia.edu/56341281/The_role_of_mitochondria_in_energy_production_for_human_sperm_motility?f_ri=1816594","dom_id":"work_56341281","summary":"Mitochondria of spermatozoa are different from the corresponding organelles of somatic cells, in both their morphology and biochemistry. The biochemical differences are essentially related to the existence of specific enzyme isoforms, which are characterized by peculiar kinetic and regulatory properties. As mitochondrial energy metabolism is a key factor supporting several sperm functions, these organelles host critical metabolic pathways during germ cell development and fertilization. Furthermore, spermatozoa can use different substrates, and therefore activate different metabolic pathways, depending on the available substrates and the physico-chemical conditions in which they operate. This versatility is critical to ensure fertilization success. However, the most valuable aspect of mitochondria function in all types of cells is the production of chemical energy in the form of ATP which can be used, in the case of spermatozoa, for sustaining sperm motility. The latter, on the other hand, represents one of the major determinants of male fertility. Accordingly, the presence of structural and functional alterations in mitochondria from asthenozoospermic subjects confirms the important role played by these organelles in energy maintenance of sperm motility. The present study gives an overview of the current knowledge on the energy-producing metabolic pathways operating inside human sperm mitochondria and critically analyse the differences with respect to somatic mitochondria. Such a comparison has also been carried out between the functional characteristics of human sperm mitochondria and those of other mammalian species. A deeper understanding of mitochondrial energy metabolism could open up new avenues of investigation in bioenergetics of human sperm mitochondria, both in physiological and pathological conditions.","downloadable_attachments":[{"id":71774311,"asset_id":56341281,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":32463735,"first_name":"A.","last_name":"Ferramosca","domain_name":"unisalento","page_name":"AFerramosca","display_name":"A. Ferramosca","profile_url":"https://unisalento.academia.edu/AFerramosca?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":654,"name":"Andrology","url":"https://www.academia.edu/Documents/in/Andrology?f_ri=1816594","nofollow":true},{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":15719,"name":"Mitochondria","url":"https://www.academia.edu/Documents/in/Mitochondria?f_ri=1816594","nofollow":true},{"id":36213,"name":"Energy Metabolism","url":"https://www.academia.edu/Documents/in/Energy_Metabolism?f_ri=1816594","nofollow":true},{"id":82978,"name":"Reactive Oxygen Species","url":"https://www.academia.edu/Documents/in/Reactive_Oxygen_Species?f_ri=1816594"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences?f_ri=1816594"},{"id":348029,"name":"Fertilization","url":"https://www.academia.edu/Documents/in/Fertilization?f_ri=1816594"},{"id":862371,"name":"Spermatozoa","url":"https://www.academia.edu/Documents/in/Spermatozoa?f_ri=1816594"},{"id":897073,"name":"Sperm Motility","url":"https://www.academia.edu/Documents/in/Sperm_Motility?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"},{"id":3158629,"name":"Asthenozoospermia","url":"https://www.academia.edu/Documents/in/Asthenozoospermia?f_ri=1816594"},{"id":3789883,"name":"Paediatrics and reproductive medicine","url":"https://www.academia.edu/Documents/in/Paediatrics_and_reproductive_medicine?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_5415611" data-work_id="5415611" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/5415611/Molecular_Properties_of_ClpAP_Protease_of_Escherichia_coli_ATP_Dependent_Association_of_ClpA_and_ClpP">Molecular Properties of ClpAP Protease of Escherichia coli : ATP-Dependent Association of ClpA and ClpP</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">The ClpAP protease from Escherichia coli consists of the ATP-binding regulatory component, ClpA (subunit M r 84 165), and the proteolytic component, ClpP (subunit M r 21 563). Our hydrodynamic studies demonstrate that the predominant... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_5415611" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">The ClpAP protease from Escherichia coli consists of the ATP-binding regulatory component, ClpA (subunit M r 84 165), and the proteolytic component, ClpP (subunit M r 21 563). Our hydrodynamic studies demonstrate that the predominant forms of these proteins in solution correspond to those observed by electron microscopy. ClpP and proClpP(SA), which in electron micrographs appear to have subunits arranged in rings of seven subunits, were found by ultracentrifugation to have s 20,w values of 12.2 and 13.2 S and molecular weights of 300 000 and 324 000 ( 3000, respectively, indicating that the native form of each consists of two such rings. The two intact rings of ClpP were separated in the presence of g0.1 M sulfate at low temperatures, suggesting that ring-ring contacts are polar in nature and more easily disrupted than subunit contacts within individual rings. Sedimentation equilibrium analysis indicated that ClpA purified without nucleotide exists as an equilibrium mixture of monomers and dimers with K a ) (1.0 ( 0.2) × 10 5 M -1 and that, upon addition of MgATP or adenosine 5′-O-(3-thiotriphosphate), ClpA subunits associated to a form with M r 505 000 ( 5000, consistent with the hexameric structure seen by electron microscopy. Sedimentation velocity and gel-filtration analysis showed that the nucleotidepromoted hexamer of ClpA (s 20,w ) 17.2 S) binds tightly to ClpP producing species with s 20,w values of 21 and 27 S (f/f 0 ) 1.5 and 1.8, respectively), consistent with electron micrographs of ClpAP that show a single tetradecamer of ClpP associated with either one or two ClpA hexamers [Kessel et al. (1995) J. Mol. Biol. 250, 587-594]. Under assay conditions in the presence of ATP and Mg 2+ , the apparent dissociation constant of hexameric ClpA and tetradecameric ClpP was ∼4 ( 2 nM. By the method of continuous variation, the optimal ratio of ClpA to ClpP in the active complex was 2:1. The specific activities of limiting ClpA and ClpP determined in the presence of an excess of the other component indicated that the second molecule of ClpA provides very little additional activation of ClpP.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/5415611" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="eacc83af35442af31d648ae04bdd2640" rel="nofollow" data-download="{"attachment_id":49301120,"asset_id":5415611,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/49301120/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="7564817" href="https://independent.academia.edu/SatyendraSingh15">Satyendra Singh</a><script data-card-contents-for-user="7564817" type="text/json">{"id":7564817,"first_name":"Satyendra","last_name":"Singh","domain_name":"independent","page_name":"SatyendraSingh15","display_name":"Satyendra Singh","profile_url":"https://independent.academia.edu/SatyendraSingh15?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_5415611 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="5415611"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 5415611, container: ".js-paper-rank-work_5415611", }); });</script></li><li class="js-percentile-work_5415611 InlineList-item InlineList-item--bordered hidden u-tcGrayDark"><span class="percentile-widget hidden"><span class="u-mr2x percentile-widget" style="display: none">•</span><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 5415611; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-percentile-work_5415611"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></li><li class="js-view-count-work_5415611 InlineList-item InlineList-item--bordered hidden"><div><span><span class="js-view-count view-count u-mr2x" data-work-id="5415611"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 5415611; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=5415611]").text(description); $(".js-view-count-work_5415611").attr('title', description).tooltip(); }); });</script></span><script>$(function() { $(".js-view-count-work_5415611").removeClass('hidden') })</script></div></li><li class="InlineList-item u-positionRelative" style="max-width: 250px"><div class="u-positionAbsolute" data-has-card-for-ri-list="5415611"><i class="fa fa-tag InlineList-item-icon u-positionRelative"></i>  <a class="InlineList-item-text u-positionRelative">6</a>  </div><span class="InlineList-item-text u-textTruncate u-pl9x"><a class="InlineList-item-text" data-has-card-for-ri="145" rel="nofollow" href="https://www.academia.edu/Documents/in/Biochemistry">Biochemistry</a>, <script data-card-contents-for-ri="145" type="text/json">{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="83128" rel="nofollow" href="https://www.academia.edu/Documents/in/Escherichia_coli">Escherichia coli</a>, <script data-card-contents-for-ri="83128" type="text/json">{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="695018" rel="nofollow" href="https://www.academia.edu/Documents/in/Molecular_weight">Molecular weight</a>, <script data-card-contents-for-ri="695018" type="text/json">{"id":695018,"name":"Molecular weight","url":"https://www.academia.edu/Documents/in/Molecular_weight?f_ri=1816594","nofollow":true}</script><a class="InlineList-item-text" data-has-card-for-ri="1030794" rel="nofollow" href="https://www.academia.edu/Documents/in/Hydrolysis">Hydrolysis</a><script data-card-contents-for-ri="1030794" type="text/json">{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis?f_ri=1816594","nofollow":true}</script></span></li><script>(function(){ if (true) { new Aedu.ResearchInterestListCard({ el: $('*[data-has-card-for-ri-list=5415611]'), work: {"id":5415611,"title":"Molecular Properties of ClpAP Protease of Escherichia coli : ATP-Dependent Association of ClpA and ClpP","created_at":"2013-12-13T06:34:46.634-08:00","url":"https://www.academia.edu/5415611/Molecular_Properties_of_ClpAP_Protease_of_Escherichia_coli_ATP_Dependent_Association_of_ClpA_and_ClpP?f_ri=1816594","dom_id":"work_5415611","summary":"The ClpAP protease from Escherichia coli consists of the ATP-binding regulatory component, ClpA (subunit M r 84 165), and the proteolytic component, ClpP (subunit M r 21 563). Our hydrodynamic studies demonstrate that the predominant forms of these proteins in solution correspond to those observed by electron microscopy. ClpP and proClpP(SA), which in electron micrographs appear to have subunits arranged in rings of seven subunits, were found by ultracentrifugation to have s 20,w values of 12.2 and 13.2 S and molecular weights of 300 000 and 324 000 ( 3000, respectively, indicating that the native form of each consists of two such rings. The two intact rings of ClpP were separated in the presence of g0.1 M sulfate at low temperatures, suggesting that ring-ring contacts are polar in nature and more easily disrupted than subunit contacts within individual rings. Sedimentation equilibrium analysis indicated that ClpA purified without nucleotide exists as an equilibrium mixture of monomers and dimers with K a ) (1.0 ( 0.2) × 10 5 M -1 and that, upon addition of MgATP or adenosine 5′-O-(3-thiotriphosphate), ClpA subunits associated to a form with M r 505 000 ( 5000, consistent with the hexameric structure seen by electron microscopy. Sedimentation velocity and gel-filtration analysis showed that the nucleotidepromoted hexamer of ClpA (s 20,w ) 17.2 S) binds tightly to ClpP producing species with s 20,w values of 21 and 27 S (f/f 0 ) 1.5 and 1.8, respectively), consistent with electron micrographs of ClpAP that show a single tetradecamer of ClpP associated with either one or two ClpA hexamers [Kessel et al. (1995) J. Mol. Biol. 250, 587-594]. Under assay conditions in the presence of ATP and Mg 2+ , the apparent dissociation constant of hexameric ClpA and tetradecameric ClpP was ∼4 ( 2 nM. By the method of continuous variation, the optimal ratio of ClpA to ClpP in the active complex was 2:1. The specific activities of limiting ClpA and ClpP determined in the presence of an excess of the other component indicated that the second molecule of ClpA provides very little additional activation of ClpP.","downloadable_attachments":[{"id":49301120,"asset_id":5415611,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":7564817,"first_name":"Satyendra","last_name":"Singh","domain_name":"independent","page_name":"SatyendraSingh15","display_name":"Satyendra Singh","profile_url":"https://independent.academia.edu/SatyendraSingh15?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry?f_ri=1816594","nofollow":true},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli?f_ri=1816594","nofollow":true},{"id":695018,"name":"Molecular weight","url":"https://www.academia.edu/Documents/in/Molecular_weight?f_ri=1816594","nofollow":true},{"id":1030794,"name":"Hydrolysis","url":"https://www.academia.edu/Documents/in/Hydrolysis?f_ri=1816594","nofollow":true},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_7452305" data-work_id="7452305" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/7452305/Generation_of_reactive_oxygen_species_induced_by_electropermeabilization_of_Chinese_hamster_ovary_cells_and_their_consequence_on_cell_viability">Generation of reactive-oxygen species induced by electropermeabilization of Chinese hamster ovary cells and their consequence on cell viability</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Cells can be permeabilized transiently when pulsed by a brief intense external electric field. The molecular and cellular bases of cell electropermeabilization are still unclear. This process can be described by a local transient membrane... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_7452305" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Cells can be permeabilized transiently when pulsed by a brief intense external electric field. The molecular and cellular bases of cell electropermeabilization are still unclear. This process can be described by a local transient membrane organisation in which high permeability exists. In this study, using the chemiluminescent probe lucigenin, we showed that electropulsation of Chinese hamster ovary cells induced generation of reactive oxygen species at the electropermeabilized cell level. This generation was directly associated with the part of the membrane surface which is electrically restructured, as shown by its dependence on electric parameters. The electroinduced cell process was activated by Ca2+ and Mg2+ ions, and by exogenous adenosine 5'-triphosphate. A metal-ion-catalyzed Haber-Weiss reaction was thought to occur in the process, as shown by the action of effector molecules of Haber-Weiss reaction such as the chelating agent EDTA, and the hydroxyl radical scavenger dimethylsulfoxide. The modulation of the oxygen species electroinduction and the use of antioxidant products (dimethylsulfoxide, sodium L-ascorbate) showed that cell survival after electric treatment was directly correlated to the oxidative jump intensity. This observation had to be associated with the cell-damaging action of oxygen-reactive species.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/7452305" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="a837c6f886b9b492e04787de8e4f0875" rel="nofollow" data-download="{"attachment_id":48468164,"asset_id":7452305,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/48468164/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="13261083" href="https://independent.academia.edu/BrunoGabriel2">Bruno Gabriel</a><script data-card-contents-for-user="13261083" type="text/json">{"id":13261083,"first_name":"Bruno","last_name":"Gabriel","domain_name":"independent","page_name":"BrunoGabriel2","display_name":"Bruno Gabriel","profile_url":"https://independent.academia.edu/BrunoGabriel2?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_7452305 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="7452305"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 7452305, container: ".js-paper-rank-work_7452305", }); 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The molecular and cellular bases of cell electropermeabilization are still unclear. This process can be described by a local transient membrane organisation in which high permeability exists. In this study, using the chemiluminescent probe lucigenin, we showed that electropulsation of Chinese hamster ovary cells induced generation of reactive oxygen species at the electropermeabilized cell level. This generation was directly associated with the part of the membrane surface which is electrically restructured, as shown by its dependence on electric parameters. The electroinduced cell process was activated by Ca2+ and Mg2+ ions, and by exogenous adenosine 5'-triphosphate. A metal-ion-catalyzed Haber-Weiss reaction was thought to occur in the process, as shown by the action of effector molecules of Haber-Weiss reaction such as the chelating agent EDTA, and the hydroxyl radical scavenger dimethylsulfoxide. The modulation of the oxygen species electroinduction and the use of antioxidant products (dimethylsulfoxide, sodium L-ascorbate) showed that cell survival after electric treatment was directly correlated to the oxidative jump intensity. This observation had to be associated with the cell-damaging action of oxygen-reactive species.","downloadable_attachments":[{"id":48468164,"asset_id":7452305,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":13261083,"first_name":"Bruno","last_name":"Gabriel","domain_name":"independent","page_name":"BrunoGabriel2","display_name":"Bruno Gabriel","profile_url":"https://independent.academia.edu/BrunoGabriel2?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":9534,"name":"Calcium","url":"https://www.academia.edu/Documents/in/Calcium?f_ri=1816594","nofollow":true},{"id":43986,"name":"Electricity","url":"https://www.academia.edu/Documents/in/Electricity?f_ri=1816594","nofollow":true},{"id":51711,"name":"Antioxidants","url":"https://www.academia.edu/Documents/in/Antioxidants?f_ri=1816594","nofollow":true},{"id":70902,"name":"Magnesium","url":"https://www.academia.edu/Documents/in/Magnesium?f_ri=1816594","nofollow":true},{"id":82978,"name":"Reactive Oxygen Species","url":"https://www.academia.edu/Documents/in/Reactive_Oxygen_Species?f_ri=1816594"},{"id":165002,"name":"Cell Viability","url":"https://www.academia.edu/Documents/in/Cell_Viability?f_ri=1816594"},{"id":1157148,"name":"Cell Survival","url":"https://www.academia.edu/Documents/in/Cell_Survival?f_ri=1816594"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology?f_ri=1816594"},{"id":1816594,"name":"Adenosine Triphosphate","url":"https://www.academia.edu/Documents/in/Adenosine_Triphosphate?f_ri=1816594"}]}, }) } })();</script></ul></li></ul></div></div><div class="u-borderBottom1 u-borderColorGrayLighter"><div class="clearfix u-pv7x u-mb0x js-work-card work_24019024" data-work_id="24019024" itemscope="itemscope" itemtype="https://schema.org/ScholarlyArticle"><div class="header"><div class="title u-fontSerif u-fs22 u-lineHeight1_3"><a class="u-tcGrayDarkest js-work-link" href="https://www.academia.edu/24019024/Energy_consumption_by_phospholipid_metabolism_in_mammalian_brain">Energy consumption by phospholipid metabolism in mammalian brain</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">Until recently, brain phospholipid metabolism was thought to consume only 2% of the ATP consumed by the mammalian brain as a whole. In this paper, however, we calculate that 1.4% of total brain ATP consumption is consumed for the de novo... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_24019024" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">Until recently, brain phospholipid metabolism was thought to consume only 2% of the ATP consumed by the mammalian brain as a whole. In this paper, however, we calculate that 1.4% of total brain ATP consumption is consumed for the de novo synthesis of ether phospholipids and that another 5% is allocated to the phosphatidylinositide cycle. When added to previous estimates that fatty acid recycling within brain phospholipids and maintenance of membrane lipid asymmetries of acidic phospholipids consume, respectively, 5% and 8% of net brain ATP consumption, it appears that phospholipid metabolism can consume up to 20% of net brain ATP consumption. This new estimate is consistent with recent evidence that phospholipids actively participate in brain signaling and membrane remodeling, among other processes.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/24019024" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="1633ff9eda1639580dca269be33d55f4" rel="nofollow" data-download="{"attachment_id":44398018,"asset_id":24019024,"asset_type":"Work","always_allow_download":false,"track":null,"button_location":"work_strip","source":null,"hide_modal":null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/44398018/download_file?st=MTczOTc5ODAxMCw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by <span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="46366707" href="https://independent.academia.edu/ThadRosenberger">Thad Rosenberger</a><script data-card-contents-for-user="46366707" type="text/json">{"id":46366707,"first_name":"Thad","last_name":"Rosenberger","domain_name":"independent","page_name":"ThadRosenberger","display_name":"Thad Rosenberger","profile_url":"https://independent.academia.edu/ThadRosenberger?f_ri=1816594","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_24019024 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="24019024"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 24019024, container: ".js-paper-rank-work_24019024", }); 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In this paper, however, we calculate that 1.4% of total brain ATP consumption is consumed for the de novo synthesis of ether phospholipids and that another 5% is allocated to the phosphatidylinositide cycle. When added to previous estimates that fatty acid recycling within brain phospholipids and maintenance of membrane lipid asymmetries of acidic phospholipids consume, respectively, 5% and 8% of net brain ATP consumption, it appears that phospholipid metabolism can consume up to 20% of net brain ATP consumption. This new estimate is consistent with recent evidence that phospholipids actively participate in brain signaling and membrane remodeling, among other processes.","downloadable_attachments":[{"id":44398018,"asset_id":24019024,"asset_type":"Work","always_allow_download":false}],"ordered_authors":[{"id":46366707,"first_name":"Thad","last_name":"Rosenberger","domain_name":"independent","page_name":"ThadRosenberger","display_name":"Thad Rosenberger","profile_url":"https://independent.academia.edu/ThadRosenberger?f_ri=1816594","photo":"/images/s65_no_pic.png"}],"research_interests":[{"id":8501,"name":"Phospholipids","url":"https://www.academia.edu/Documents/in/Phospholipids?f_ri=1816594","nofollow":true},{"id":11397,"name":"Energy Consumption","url":"https://www.academia.edu/Documents/in/Energy_Consumption?f_ri=1816594","nofollow":true},{"id":36213,"name":"Energy 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