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class="vector-toc-numb">2</span> <span>Structure and function</span> </div> </a> <ul id="toc-Structure_and_function-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Mechanism" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Mechanism"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Mechanism</span> </div> </a> <ul id="toc-Mechanism-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-History" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#History"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>History</span> </div> </a> <ul id="toc-History-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Role_in_homeostasis" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Role_in_homeostasis"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Role in homeostasis</span> </div> </a> <button aria-controls="toc-Role_in_homeostasis-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Role in homeostasis subsection</span> </button> <ul id="toc-Role_in_homeostasis-sublist" class="vector-toc-list"> <li id="toc-Sodium-calcium_exchanger" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Sodium-calcium_exchanger"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.1</span> <span>Sodium-calcium exchanger</span> </div> </a> <ul id="toc-Sodium-calcium_exchanger-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Sodium-hydrogen_antiporter" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Sodium-hydrogen_antiporter"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.2</span> <span>Sodium-hydrogen antiporter</span> </div> </a> <ul id="toc-Sodium-hydrogen_antiporter-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chloride-bicarbonate_antiporter" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chloride-bicarbonate_antiporter"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.3</span> <span>Chloride-bicarbonate antiporter</span> </div> </a> <ul id="toc-Chloride-bicarbonate_antiporter-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chloride-hydrogen_antiporter" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chloride-hydrogen_antiporter"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.4</span> <span>Chloride-hydrogen antiporter</span> </div> </a> <ul id="toc-Chloride-hydrogen_antiporter-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Reduced_folate_carrier_protein" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Reduced_folate_carrier_protein"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.5</span> <span>Reduced folate carrier protein</span> </div> </a> <ul id="toc-Reduced_folate_carrier_protein-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Vesicle_neurotransmitter_antiporters" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Vesicle_neurotransmitter_antiporters"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.6</span> <span>Vesicle neurotransmitter antiporters</span> </div> </a> <ul id="toc-Vesicle_neurotransmitter_antiporters-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Further_reading" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Further_reading"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Further reading</span> </div> </a> <ul id="toc-Further_reading-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" title="Table of Contents" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span 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title="Antiportador – Spanish" lang="es" hreflang="es" data-title="Antiportador" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D9%86%D8%A7%D9%87%D9%85%D8%B3%D9%88%D8%A8%D8%B1" title="ناهمسوبر – Persian" lang="fa" hreflang="fa" data-title="ناهمسوبر" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Antiport" title="Antiport – French" lang="fr" hreflang="fr" data-title="Antiport" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EC%97%AD%EC%88%98%EC%86%A1%EC%B2%B4" title="역수송체 – Korean" lang="ko" hreflang="ko" data-title="역수송체" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-kk mw-list-item"><a href="https://kk.wikipedia.org/wiki/%D0%90%D0%BD%D1%82%D0%B8%D0%BF%D0%BE%D1%80%D1%82" title="Антипорт – Kazakh" lang="kk" hreflang="kk" data-title="Антипорт" data-language-autonym="Қазақша" data-language-local-name="Kazakh" class="interlanguage-link-target"><span>Қазақша</span></a></li><li class="interlanguage-link interwiki-mk mw-list-item"><a href="https://mk.wikipedia.org/wiki/%D0%90%D0%BD%D1%82%D0%B8%D0%BF%D0%BE%D1%80%D1%82%D0%B5%D1%80" title="Антипортер – Macedonian" lang="mk" hreflang="mk" data-title="Антипортер" data-language-autonym="Македонски" data-language-local-name="Macedonian" class="interlanguage-link-target"><span>Македонски</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E4%BA%A4%E6%8F%9B%E8%BC%B8%E9%80%81%E4%BD%93" title="交換輸送体 – Japanese" lang="ja" hreflang="ja" data-title="交換輸送体" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Antyport" title="Antyport – Polish" lang="pl" hreflang="pl" data-title="Antyport" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%90%D0%BD%D1%82%D0%B8%D0%BF%D0%BE%D1%80%D1%82" title="Антипорт – Russian" lang="ru" hreflang="ru" data-title="Антипорт" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Antiporter" title="Antiporter – Serbian" lang="sr" hreflang="sr" data-title="Antiporter" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Antiporter" title="Antiporter – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Antiporter" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Antiportteri" title="Antiportteri – Finnish" lang="fi" hreflang="fi" data-title="Antiportteri" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li> </ul> <div class="after-portlet 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src="//upload.wikimedia.org/wikipedia/commons/thumb/1/18/Active_Transport_Proteins.png/220px-Active_Transport_Proteins.png" decoding="async" width="220" height="204" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/18/Active_Transport_Proteins.png/330px-Active_Transport_Proteins.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/18/Active_Transport_Proteins.png/440px-Active_Transport_Proteins.png 2x" data-file-width="804" data-file-height="745" /></a><figcaption>A comparison of transport proteins<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></figcaption></figure><p> An <b>antiporter</b> (also called <b>exchanger</b> or <b>counter-transporter</b>) is an <a href="/wiki/Integral_membrane_protein" title="Integral membrane protein">integral membrane protein</a> that uses <a href="/wiki/Secondary_active_transport" class="mw-redirect" title="Secondary active transport">secondary active transport</a> to move two or more molecules in opposite directions across a <a href="/wiki/Phospholipid_membrane" class="mw-redirect" title="Phospholipid membrane">phospholipid membrane</a>. It is a type of <a href="/wiki/Cotransporter" title="Cotransporter">cotransporter</a>, which means that uses the <a href="/wiki/Exergonic_reaction" title="Exergonic reaction">energetically favorable</a> movement of one molecule down its <a href="/wiki/Electrochemical_gradient" title="Electrochemical gradient">electrochemical gradient</a> to power the <a href="/wiki/Endergonic_reaction" title="Endergonic reaction">energetically unfavorable</a> movement of another molecule up its electrochemical gradient. This is in contrast to <a href="/wiki/Symporter" title="Symporter">symporters</a>, which are another type of cotransporter that moves two or more ions in the same direction, and <a href="/wiki/Primary_active_transport" class="mw-redirect" title="Primary active transport">primary active transport</a>, which is directly powered by <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>.<sup id="cite_ref-Lodish_2021_2-0" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup></p><figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Antiport.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/47/Antiport.png/220px-Antiport.png" decoding="async" width="220" height="107" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/47/Antiport.png/330px-Antiport.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/47/Antiport.png/440px-Antiport.png 2x" data-file-width="827" data-file-height="401" /></a><figcaption>Illustration of an antiporter and the concentration gradients of its transport substances<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup></figcaption></figure> <p>Transport may involve one or more of each type of solute. For example, the <a href="/wiki/Sodium-calcium_exchanger" title="Sodium-calcium exchanger">Na<sup>+</sup>/Ca<sup>2+</sup> exchanger</a>, found in the plasma membrane of many cells, moves three sodium ions in one direction, and one calcium ion in the other. As with sodium in this example, antiporters rely on an established gradient that makes entry of one ion energetically favorable to force the unfavorable movement of a second molecule in the opposite direction.<sup id="cite_ref-Yu_1997_4-0" class="reference"><a href="#cite_note-Yu_1997-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Through their diverse functions, antiporters are involved in various important physiological processes, such as regulation of the strength of cardiac muscle contraction, transport of carbon dioxide by <a href="/wiki/Red_blood_cell" title="Red blood cell">erythrocytes</a>, regulation of cytosolic pH, and accumulation of sucrose in plant <a href="/wiki/Vacuole" title="Vacuole">vacuoles</a>.<sup id="cite_ref-Lodish_2021_2-1" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Background">Background</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=1" title="Edit section: Background"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Cotransporter" title="Cotransporter">Cotransporters</a> are found in all organisms<sup id="cite_ref-Lodish_2021_2-2" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> and fall under the broader category of <a href="/wiki/Transport_protein" title="Transport protein">transport proteins</a>, a diverse group of transmembrane proteins that includes uniporters, symporters, and antiporters. Each of them are responsible for providing a means of movement for water-soluble molecules that otherwise would not be able to pass through lipid-based plasma membrane. The simplest of these are the <a href="/wiki/Uniporters" class="mw-redirect" title="Uniporters">uniporters</a>, which facilitate the movement of one type of molecule in the direction that follows its <a href="/wiki/Concentration_gradient" class="mw-redirect" title="Concentration gradient">concentration gradient</a>.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> In mammals, they are most commonly responsible for bringing glucose and amino acids into cells.<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>Symporters and antiporters are more complex because they move more than one ion and the movement of one of those ions is in an energetically unfavorable direction. As multiple molecules are involved, multiple binding processes must occur as the transporter undergoes a cycle of <a href="/wiki/Conformational_change" title="Conformational change">conformational changes</a> to move them from one side of the membrane to the other.<sup id="cite_ref-Forrest_2011_7-0" class="reference"><a href="#cite_note-Forrest_2011-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> The mechanism used by these transporters limits their functioning to moving only a few molecules at a time. As a result, symporters and antiporters are characterized by a slower transport speed, moving between 10<sup>2</sup> and 10<sup>4</sup> molecules per second. Compare this to <a href="/wiki/Channel_protein" class="mw-redirect" title="Channel protein">ion channels</a> that provide a means for facilitated diffusion to occur and allow between 10<sup>7</sup> and 10<sup>8</sup> ions pass through the plasma membrane per second.<sup id="cite_ref-Lodish_2021_2-3" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p><p>Though <a href="/wiki/Sodium%E2%80%93potassium_pump" title="Sodium–potassium pump">ATP-powered</a> pumps also move molecules in an energetically unfavorable direction and undergo conformational changes to do so, they fall under a different category of membrane proteins because they couple the energy derived from <a href="/wiki/ATP_hydrolysis" title="ATP hydrolysis">ATP hydrolysis</a> to transport their respective ions. These ion pumps are very selective, consisting of a double gating system where at least one of the gates is always shut. The ion is allowed to enter from one side of the membrane while one of the gates is open, after which it will shut. Only then will the second gate open to allow the ion to leave on the membrane's opposite side. The time between the alternating gate opening is referred to as the occluded state, where the ions are bound and both gates are shut.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> These gating reactions limit the speed of these pumps, causing them to function even slower than transport proteins, moving between 10<sup>0</sup> and 10<sup>3</sup> ions per second.<sup id="cite_ref-Lodish_2021_2-4" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Structure_and_function">Structure and function</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=2" title="Edit section: Structure and function"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>To function in active transport, a membrane protein must meet certain requirements. The first of these is that the interior of the protein must contain a cavity that is able to contain its corresponding molecule or ion. Next, the protein must be able to assume at least two different <a href="/wiki/Conformational_change" title="Conformational change">conformations</a>, one with its cavity open to the <a href="/wiki/Extracellular_space" title="Extracellular space">extracellular space</a> and the other with its cavity open to the <a href="/wiki/Cytosol" title="Cytosol">cytosol</a>. This is crucial for the movement of molecules from one side of the membrane to the other. Finally, the cavity of the protein must contain binding sites for its <a href="/wiki/Ligand_(biochemistry)" title="Ligand (biochemistry)">ligands</a>, and these binding sites must have a different affinity for the ligand in each of the protein's conformations. Without this, the ligand will not be able to bind to the transporter on one side of the plasma membrane and be released from it on the other side.<sup id="cite_ref-Jardetzky_1966_9-0" class="reference"><a href="#cite_note-Jardetzky_1966-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> As transporters, antiporters have all of these features. </p><p>Because antiporters are highly diverse, their structure can vary widely depending upon the type of molecules being transported and their location in the cell. However, there are some common features that all antiporters share. One of these is multiple <a href="/wiki/Transmembrane_region" class="mw-redirect" title="Transmembrane region">transmembrane regions</a> that span the <a href="/wiki/Lipid_bilayer" title="Lipid bilayer">lipid bilayer</a> of the plasma membrane and form a channel through which <a href="/wiki/Hydrophile" title="Hydrophile">hydrophilic</a> molecules can pass. These transmembrane regions are typically structured from <a href="/wiki/Alpha_helix" title="Alpha helix">alpha helices</a> and are connected by loops in both the extracellular space and cytosol. These loops are what contain the binding sites for the molecules associated with the antiporter.<sup id="cite_ref-Forrest_2011_7-1" class="reference"><a href="#cite_note-Forrest_2011-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p><p>These features of antiporters allow them to carry out their function in maintaining cellular <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a>. They provide a space where a hydrophilic molecule can pass through the hydrophobic lipid bilayer, allowing them to bypass the hydrophobic interactions of the plasma membrane. This enables the efficient movement of molecules needed for the environment of the cell, such as in the acidification of organelles.<sup id="cite_ref-Lodish_2021_2-5" class="reference"><a href="#cite_note-Lodish_2021-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> The varying affinity of the antiporter for each ion or molecule on either side of the plasma membrane allows it to bind to and release its ligands on the appropriate side of the membrane according to the electrochemical gradient of the ion being harnessed for its energetically favorable concentration.<sup id="cite_ref-Jardetzky_1966_9-1" class="reference"><a href="#cite_note-Jardetzky_1966-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Mechanism">Mechanism</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=3" title="Edit section: Mechanism"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Antiport.gif" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/bf/Antiport.gif/220px-Antiport.gif" decoding="async" width="220" height="229" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/bf/Antiport.gif/330px-Antiport.gif 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/bf/Antiport.gif/440px-Antiport.gif 2x" data-file-width="480" data-file-height="500" /></a><figcaption>A simplified illustration of the mechanism of an antiporter<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup></figcaption></figure> <p>The mechanism of antiporter transport involves several key steps and a series of conformational changes that are dictated by the structural element described above:<sup id="cite_ref-Forrest_2011_7-2" class="reference"><a href="#cite_note-Forrest_2011-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <ol><li>The <a href="/wiki/Substrate_(chemistry)" title="Substrate (chemistry)">substrate</a> binds to its specific <a href="/wiki/Binding_site" title="Binding site">binding site</a> on the extracellular side of the plasma membrane, forming a temporary substrate-bound open form of the antiporter.</li> <li>This becomes an occluded, substrate-bound state that is still facing the extracellular space.</li> <li>The antiporter undergoes a conformational change to become an occluded, substrate-bound protein that is now facing the cytosol. As it does so, it passes through a temporary fully-occluded intermediate stage.</li> <li>The substrate is released from the antiporter as it takes on an open, inward-facing conformation.</li> <li>The antiporter can now bind to its second substrate and transport it in the opposite direction by taking on its transient substrate-bound open state.</li> <li>This is followed by an occluded, substrate-bound state that is still facing the cytosol, a conformation change with a temporary fully-occluded intermediate stage, and a return to the antiporter's open, outward-facing conformation.</li> <li>The second substrate is released and the antiporter can return to its original conformation state, where it is ready to bind to new molecules or ions and repeat its transport process.<sup id="cite_ref-Forrest_2011_7-3" class="reference"><a href="#cite_note-Forrest_2011-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup></li></ol> <div class="mw-heading mw-heading2"><h2 id="History">History</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=4" title="Edit section: History"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Antiporters were discovered as scientists were exploring ion transport mechanisms across biological membranes. The early studies took place in the mid-20th century and were focused on the mechanisms that transported ions such as sodium, potassium, and calcium across the plasma membrane. Researchers made the observation that these ions were moved in opposite directions and hypothesized the existence of membrane proteins that could facilitate this type of transport.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>In the 1960's, biochemist Efraim Racker made a breakthrough in the discovery of antiporters. Through purification from bovine heart mitochondria, Racker and his colleagues found a mitochondrial protein that could exchange inorganic phosphate for hydroxide ions. The protein is located in the inner mitochondrial membrane and transports phosphate ions for use in <a href="/wiki/Oxidative_phosphorylation" title="Oxidative phosphorylation">oxidative phosphorylation</a>. It became known as the phosphate-hydroxide antiporter, or <a href="/wiki/Phosphate_carrier_protein,_mitochondrial" title="Phosphate carrier protein, mitochondrial">mitochondrial phosphate carrier protein</a>, and was the first example of an antiporter identified in living cells.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p><p>As time went on, researchers discovered other antiporters in different membranes and in various organisms. This includes the <a href="/wiki/Sodium-calcium_exchanger" title="Sodium-calcium exchanger">sodium-calcium exchanger</a> (NCX), another crucial antiporter that regulates intracellular calcium levels through the exchange of sodium ions for calcium ions across the plasma membrane. It was discovered in the 1970s and is now a well-characterized antiporter known to be found in many different types of cells.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> </p><p>Advances in the fields of <a href="/wiki/Biochemistry" title="Biochemistry">biochemistry</a> and <a href="/wiki/Molecular_biology" title="Molecular biology">molecular biology</a> have enabled the identification and characterization of a wide range of antiporters. Understanding the transport processes of various molecules and ions has provided insight into cellular transport mechanisms, as well as the role of antiporters in various physiological functions and in the maintenance of homeostasis </p> <div class="mw-heading mw-heading2"><h2 id="Role_in_homeostasis">Role in homeostasis</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=5" title="Edit section: Role in homeostasis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Sodium-calcium_exchanger">Sodium-calcium exchanger</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=6" title="Edit section: Sodium-calcium exchanger"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Sodium-calcium_exchanger" title="Sodium-calcium exchanger">sodium-calcium exchanger</a>, also known as the Na<sup>+</sup>/Ca<sup>2+</sup> exchanger or NCX, is an antiporter responsible for removing calcium from cells. This title encompasses a class of ion transporters that are commonly found in the heart, kidney, and brain. They use the energy stored in the electrochemical gradient of sodium to exchange the flow of three sodium ions into the cell for the export of one calcium ion.<sup id="cite_ref-Yu_1997_4-1" class="reference"><a href="#cite_note-Yu_1997-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Though this exchanger is most common in the membranes of the <a href="/wiki/Mitochondrion" title="Mitochondrion">mitochondria</a> and the <a href="/wiki/Endoplasmic_reticulum" title="Endoplasmic reticulum">endoplasmic reticulum</a> of <a href="/wiki/Excitable_cell" class="mw-redirect" title="Excitable cell">excitable cells</a>, it can be found in many different cell types in various species.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> </p><p>Although the sodium-calcium exchanger has a low affinity for calcium ions, it can transport a high amount of the ion in a short period of time. Because of these properties, it is useful in situations where there is an urgent need to export high amounts of calcium, such as after an <a href="/wiki/Action_potential" title="Action potential">action potential</a> has occurred.<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> Its characteristics also enable NCX to work with other proteins that have a greater affinity for calcium ions without interfering with their functions. NCX works with these proteins to carry out functions such as cardiac muscle relaxation, <a href="/wiki/Excitation-contraction_coupling" class="mw-redirect" title="Excitation-contraction coupling">excitation-contraction coupling</a>, and <a href="/wiki/Photoreceptor_cell" title="Photoreceptor cell">photoreceptor</a> activity. They also maintain the concentration of calcium ions in the sarcoplasmic reticulum of cardiac cells, endoplasmic reticulum of excitable and nonexcitable cells, and the mitochondria.<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p><p>Another key characteristic of this antiporter is its reversibility. This means that if the cell is <a href="/wiki/Depolarization" title="Depolarization">depolarized</a> enough, the extracellular sodium level is low enough, or the intracellular level of sodium is high enough, NCX will operate in the reverse direction and begin bringing calcium into the cell.<sup id="cite_ref-Yu_1997_4-2" class="reference"><a href="#cite_note-Yu_1997-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> For example, when NCX functions during <a href="/wiki/Excitotoxicity" title="Excitotoxicity">excitotoxicity</a>, this characteristic allows it to have a protective effect because the accompanying increase in intracellular calcium levels enables the exchanger to work in its normal direction regardless of the sodium concentration.<sup id="cite_ref-Yu_1997_4-3" class="reference"><a href="#cite_note-Yu_1997-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Another example is the depolarization of cardiac muscle cells, which is accompanied by a large increase in the intracellular sodium concentration that causes NCX to work in reverse. Because the concentration of calcium is carefully regulated during the cardiac action potential, this is only a temporary effect as calcium is pumped out of the cell.<sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> </p><p>The sodium-calcium exchanger's role in maintaining calcium homeostasis in <a href="/wiki/Cardiac_muscle_cells" class="mw-redirect" title="Cardiac muscle cells">cardiac muscle cells</a> allows it to help relax the heart muscle as it exports calcium during <a href="/wiki/Diastole" title="Diastole">diastole</a>. Therefore, its dysfunction can result in abnormal calcium movement and the development of various cardiac diseases. Abnormally high intracellular calcium levels can hinder diastole and cause abnormal <a href="/wiki/Systole" title="Systole">systole</a> and <a href="/wiki/Arrhythmia" title="Arrhythmia">arrhythmias</a>.<sup id="cite_ref-21" class="reference"><a href="#cite_note-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Arrhythmias can occur when calcium is not properly exported by NCX, causing delayed afterdepolarizations and triggering abnormal activity that can possibly lead to <a href="/wiki/Atrial_fibrillation" title="Atrial fibrillation">atrial fibrillation</a> and <a href="/wiki/Ventricular_tachycardia" title="Ventricular tachycardia">ventricular tachycardia</a>.<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> </p><p>If the heart experiences <a href="/wiki/Ischemia" title="Ischemia">ischemia</a>, the inadequate oxygen supply can disrupt ion homeostasis. When the body tries to stabilize this by returning blood to the area, <a href="/wiki/Ischemia-reperfusion_injury" class="mw-redirect" title="Ischemia-reperfusion injury">ischemia-reperfusion injury</a>, a type of oxidative stress, occurs. If NCX is dysfunctional, it can exacerbate the increase of calcium that accompanies <a href="/wiki/Reperfusion_therapy" title="Reperfusion therapy">reperfusion</a>, causing cell death and tissue damage.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> Similarly, NCX dysfunction has found to be involved in <a href="/wiki/Ischemic_stroke" class="mw-redirect" title="Ischemic stroke">ischemic strokes</a>. Its activity is upregulated, causing a increased cytosolic calcium level, which can lead to neuronal cell death.<sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> </p><p>The Na<sup>+</sup>/Ca<sup>2+</sup> exchanger has also been implicated in neurological disorders such as <a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Alzheimer's disease</a> and <a href="/wiki/Parkinson%27s_disease" title="Parkinson's disease">Parkinson's disease</a>. Its dysfunction can result in <a href="/wiki/Oxidative_stress" title="Oxidative stress">oxidative stress</a> and neuronal cell death, contributing to the cognitive decline that characterizes Alzheimer's disease. The dysregulation of calcium homeostasis has been found to be a key part of neuron death and Alzheimer's <a href="/wiki/Pathogenesis" title="Pathogenesis">pathogenesis</a>. For example, neurons that have <a href="/wiki/Neurofibrillary_tangle" title="Neurofibrillary tangle">neurofibrillary tangles</a> contain high levels of calcium and show hyperactivation of calcium-dependent proteins.<sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> The abnormal calcium handling of atypical NCX function can also cause the mitochondrial dysfunction, oxidative stress, and neuronal cell death that characterize Parkinson's. In this case, if <a href="/wiki/Dopaminergic_neurons" class="mw-redirect" title="Dopaminergic neurons">dopaminergic neurons</a> of the <a href="/wiki/Substantia_nigra" title="Substantia nigra">substantia nigra</a> are affected, it can contribute to the onset and development of Parkinson's disease.<sup id="cite_ref-26" class="reference"><a href="#cite_note-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> Although the mechanism is not entirely understood, disease models have shown a link between NCX and Parkinson's and that NCX inhibitors can prevent death of dopaminergic neurons.<sup id="cite_ref-27" class="reference"><a href="#cite_note-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-28" class="reference"><a href="#cite_note-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Sodium-hydrogen_antiporter">Sodium-hydrogen antiporter</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=7" title="Edit section: Sodium-hydrogen antiporter"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Sodium%E2%80%93hydrogen_antiporter" title="Sodium–hydrogen antiporter">sodium–hydrogen antiporter</a>, also known as the sodium-proton exchanger, Na+/H+ exchanger, or NHE, is an antiporter responsible for transporting sodium into the cell and hydrogen out of the cell. As such, it is important in the regulation of cellular pH and sodium levels.<sup id="cite_ref-Padan_2016_29-0" class="reference"><a href="#cite_note-Padan_2016-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> There are differences among the types of NHE antiporter families present in eukaryotes and prokaryotes. The 9 <a href="/wiki/Protein_isoform" title="Protein isoform">isoforms</a> of this transporter that are found in the human genome fall under several families, including the cation-proton antiporters (<a href="/wiki/Monovalent_cation:proton_antiporter-1" title="Monovalent cation:proton antiporter-1">CPA 1</a>, <a href="/wiki/Monovalent_cation:proton_antiporter-2" title="Monovalent cation:proton antiporter-2">CPA 2</a>, and <a href="/wiki/Monovalent_cation:proton_antiporter-3" title="Monovalent cation:proton antiporter-3">CPA 3</a>) and <a href="/wiki/Sodium-transporting_carboxylic_acid_decarboxylase" title="Sodium-transporting carboxylic acid decarboxylase">sodium-transporting carboxylic acid decarboxylase</a> (NaT-DC).<sup id="cite_ref-pmid31196609_30-0" class="reference"><a href="#cite_note-pmid31196609-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> Prokaryotic organisms contain the Na+/H+ antiporter families <a href="/wiki/NhaA_family" title="NhaA family">NhaA</a>, <a href="/wiki/NhaB_family" title="NhaB family">NhaB</a>, <a href="/wiki/NhaC_family" title="NhaC family">NhaC</a>, <a href="/wiki/NhaD_family" title="NhaD family">NhaD</a>, and <a href="/wiki/NhaE_family" title="NhaE family">NhaE</a>.<sup id="cite_ref-Padan_2001_31-0" class="reference"><a href="#cite_note-Padan_2001-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> </p><p>Because enzymes can only function at certain pH ranges, it is critical for cells to tightly regulate <a href="/wiki/PH" title="PH">cytosolic pH</a>. When a cell's pH is outside of the optimal range, the sodium-hydrogen antiporter detects this and is activated to transport ions as a <a href="/wiki/Homeostatic_mechanism" class="mw-redirect" title="Homeostatic mechanism">homeostatic mechanism</a> to restore pH balance.<sup id="cite_ref-32" class="reference"><a href="#cite_note-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> Since ion flux can be reversed in mammalian cells, NHE can also be used to transport sodium out of the cell to prevent excess sodium from accumulating and causing <a href="/wiki/Toxicity" title="Toxicity">toxicity</a>.<sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </p><p>As suggested by its functions, this antiporter is located in the <a href="/wiki/Kidney" title="Kidney">kidney</a> for <a href="/wiki/Sodium_reabsorption" class="mw-redirect" title="Sodium reabsorption">sodium reabsorption</a> regulation and in the heart for intracellular pH and <a href="/wiki/Contractility_of_the_heart" class="mw-redirect" title="Contractility of the heart">contractility</a> regulation. NHE plays an important role in the <a href="/wiki/Nephron" title="Nephron">nephron</a> of the kidney, especially in the cells of the <a href="/wiki/Proximal_convoluted_tubule" class="mw-redirect" title="Proximal convoluted tubule">proximal convoluted tubule</a> and <a href="/wiki/Collecting_duct_system" title="Collecting duct system">collecting duct</a>. The sodium-hydrogen antiporter's function is upregulated by <a href="/wiki/Angiotensin" title="Angiotensin">Angiotensin II</a> in the proximal convoluted tubule when the body needs to reabsorb sodium and excrete hydrogen.<sup id="cite_ref-Bobulescu_2006_34-0" class="reference"><a href="#cite_note-Bobulescu_2006-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> </p><p>Plants are sensitive to high amounts of salt, which can halt certain necessary functions of the eukaryotic organism, including <a href="/wiki/Photosynthesis" title="Photosynthesis">photosynthesis</a>.<sup id="cite_ref-Padan_2001_31-1" class="reference"><a href="#cite_note-Padan_2001-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> For the organisms to maintain homeostasis and carry out crucial functions, Na+/H+ antiporters are used to rid the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a> of excess sodium by pumping Na+ out of the cell.<sup id="cite_ref-Padan_2001_31-2" class="reference"><a href="#cite_note-Padan_2001-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> These antiporters can also close their channel to stop sodium from entering the cell, along with allowing excess sodium within the cell to enter into a <a href="/wiki/Vacuole" title="Vacuole">vacuole</a>.<sup id="cite_ref-Padan_2001_31-3" class="reference"><a href="#cite_note-Padan_2001-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> </p><p>Dysregulation of the sodium-hydrogen antiporter's activity has been linked to cardiovascular diseases, renal disorders, and neurological conditions <sup id="cite_ref-Padan_2016_29-1" class="reference"><a href="#cite_note-Padan_2016-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> NHE inhibitors are being developed to treat these issues.<sup id="cite_ref-Karmazyn_2005_35-0" class="reference"><a href="#cite_note-Karmazyn_2005-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> One of the isoforms of the antiporter, NHE1, is essential to the function of the mammalian <a href="/wiki/Myocardium" class="mw-redirect" title="Myocardium">myocardium</a>. NHE is involved in the case of <a href="/wiki/Hypertrophy" title="Hypertrophy">hypertrophy</a> and when damage to the heart muscle occurs, such as during <a href="/wiki/Ischemia" title="Ischemia">ischemia</a> and <a href="/wiki/Reperfusion_injury" title="Reperfusion injury">reperfusion</a>. Studies have shown that NHE1 is more active in animal models experiencing <a href="/wiki/Myocardial_infarction" title="Myocardial infarction">myocardial infarction</a> and <a href="/wiki/Left_ventricular_hypertrophy" title="Left ventricular hypertrophy">left ventricular hypertrophy</a>.<sup id="cite_ref-Karmazyn_2005_35-1" class="reference"><a href="#cite_note-Karmazyn_2005-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> During these cardiac events, the function of the sodium-hydrogen antiporter causes an increase in the sodium levels of <a href="/wiki/Cardiac_muscle_cells" class="mw-redirect" title="Cardiac muscle cells">cardiac muscle cells</a>. In turn, the work of the sodium-calcium antiporter leads to more calcium being brought into the cell, which is what results in damage to the myocardium.<sup id="cite_ref-Karmazyn_2005_35-2" class="reference"><a href="#cite_note-Karmazyn_2005-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> </p><p>Five isoforms of NHE are found in kidney's epithelial cells. The best studied one is NHE3, which is mainly located in the <a href="/wiki/Proximal_tubule" title="Proximal tubule">proximal tubules</a> of the kidney and plays a key role in acid-base homeostasis. Issues with NHE3 disrupt the reabsorption of sodium and secretion of hydrogen.<sup id="cite_ref-Bobulescu_2006_34-1" class="reference"><a href="#cite_note-Bobulescu_2006-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> The main conditions that NHE3 dysregulation can cause are hypertension and <a href="/wiki/Renal_tubular_acidosis" title="Renal tubular acidosis">renal tubular acidosis</a> (RTA). <a href="/wiki/Hypertension" title="Hypertension">Hypertension</a> can occur when more sodium is reabsorbed in the kidneys because water will follow the sodium ions and create an elevated blood volume. This, in turn, leads to elevated blood pressure.<sup id="cite_ref-Bobulescu_2006_34-2" class="reference"><a href="#cite_note-Bobulescu_2006-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> RTA is characterized by the inability of the kidneys to acidify the urine due to underactive NHE3 and reduced secretion of hydrogen ions, resulting in <a href="/wiki/Metabolic_acidosis" title="Metabolic acidosis">metabolic acidosis</a>. On the other hand, overactive NHE3 can lead to excess secretion of hydrogen ions and <a href="/wiki/Metabolic_alkalosis" title="Metabolic alkalosis">metabolic alkalosis</a>, where the blood is too alkaline.<sup id="cite_ref-Bobulescu_2006_34-3" class="reference"><a href="#cite_note-Bobulescu_2006-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> </p><p>NHE can also be linked to <a href="/wiki/Neurodegeneration" class="mw-redirect" title="Neurodegeneration">neurodegeneration</a>. The dysregulation or loss of the isoform NHE6 can lead to pathological changes in the <a href="/wiki/Tau_protein" title="Tau protein">tau proteins</a> of human <a href="/wiki/Neuron" title="Neuron">neurons</a>, which can have huge consequences.<sup id="cite_ref-Fernandez_2022_36-0" class="reference"><a href="#cite_note-Fernandez_2022-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> For example, <a href="/wiki/Christianson_syndrome" title="Christianson syndrome">Christianson Syndrome</a> (CS) is an <a href="/wiki/X-linked" class="mw-redirect" title="X-linked">X-linked disorder</a> caused by a loss-of-function mutation in NHE6, which leads to the over acidification of <a href="/wiki/Endosome" title="Endosome">endosomes</a>.<sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup> In studies done on postmortem brains of individuals with CS, lower NHE6 function was linked to higher levels of tau deposition. The level of tau phosphorylation was also found to be elevated, which leads to the formation of insoluble tangles that can cause neuronal damage and death.<sup id="cite_ref-Fernandez_2022_36-1" class="reference"><a href="#cite_note-Fernandez_2022-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> Tau proteins are also implicated in other neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases. </p> <div class="mw-heading mw-heading3"><h3 id="Chloride-bicarbonate_antiporter">Chloride-bicarbonate antiporter</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=8" title="Edit section: Chloride-bicarbonate antiporter"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/w/index.php?title=Chloride-bicarbonate_antiporter&action=edit&redlink=1" class="new" title="Chloride-bicarbonate antiporter (page does not exist)">chloride-bicarbonate antiporter</a> is crucial to maintaining pH and fluid balance through its function of exchanging <a href="/wiki/Bicarbonate" title="Bicarbonate">bicarbonate</a> and <a href="/wiki/Chloride" title="Chloride">chloride</a> ions through cell membranes. This exchange occurs in many different types of body cells.<sup id="cite_ref-Alper_1991_38-0" class="reference"><a href="#cite_note-Alper_1991-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> In the cardiac <a href="/wiki/Purkinje_fibers" title="Purkinje fibers">Purkinje fibers</a> and <a href="/wiki/Smooth_muscle_cells" class="mw-redirect" title="Smooth muscle cells">smooth muscle cells</a> of the <a href="/wiki/Ureter" title="Ureter">ureters</a>, this antiporter is the main mechanism of chloride transport into the cells. <a href="/wiki/Epithelial_cells" class="mw-redirect" title="Epithelial cells">Epithelial cells</a> such as those of the kidney use chloride-bicarbonate exchange to regulate their volume, intracellular pH, and extracellular pH. Gastric <a href="/wiki/Parietal_cell" title="Parietal cell">parietal cells</a>, <a href="/wiki/Osteoclast" title="Osteoclast">osteoclasts</a>, and other acid-secreting cells have chloride-bicarbonate antiporters that function in the basolateral membrane to dispose of excess bicarbonate left behind by the function of <a href="/wiki/Carbonic_anhydrase" title="Carbonic anhydrase">carbonic anhydrase</a> and apical proton pumps. However, base-secreting cells exhibit apical chloride-bicarbonate exchange and basolateral proton pumps.<sup id="cite_ref-Alper_1991_38-1" class="reference"><a href="#cite_note-Alper_1991-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> </p><p>An example of a chloride-bicarbonate antiporter is the <a href="/wiki/Chloride_anion_exchanger" title="Chloride anion exchanger">chloride anion exchanger</a>, also known as down-regulated in adenoma (protein DRA). It is found in the <a href="/wiki/Intestinal_mucosa" class="mw-redirect" title="Intestinal mucosa">intestinal mucosa</a>, especially in the <a href="/wiki/Columnar_epithelium" class="mw-redirect" title="Columnar epithelium">columnar epithelium</a> and <a href="/wiki/Goblet_cell" title="Goblet cell">goblet cells</a> of the apical surface of the membrane, where it carries out the function of chloride and bicarbonate exchange.<sup id="cite_ref-39" class="reference"><a href="#cite_note-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> Protein DRA's reuptake of chloride is critical to creating an <a href="/wiki/Osmotic_gradient" class="mw-redirect" title="Osmotic gradient">osmotic gradient</a> that allows the intestine to reabsorb water.<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup> </p><p>Another well-studied chloride-bicarbonate antiporter is anion exchanger 1 (AE1), which is also known as <a href="/wiki/Band_3_anion_transport_protein" title="Band 3 anion transport protein">band 3 anion transport protein</a> or solute carrier family 4 member 1 (SLC4A1). This exchanger is found in <a href="/wiki/Red_blood_cell" title="Red blood cell">red blood cells</a>, where it helps transport bicarbonate and carbon dioxide between the lungs and tissues to maintain acid-base homeostasis.<sup id="cite_ref-Alper_1991_38-2" class="reference"><a href="#cite_note-Alper_1991-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> AE1 also expressed in the basolateral side of cells of the renal tubules. It is crucial in the <a href="/wiki/Collecting_duct_system" title="Collecting duct system">collecting duct</a> of the nephron, which is where its acid-secreting <a href="/wiki/%CE%91-intercalated_cells" class="mw-redirect" title="Α-intercalated cells">α-intercalated cells</a> are located. These cells use carbon dioxide and water to generate hydrogen and bicarbonate ions, which is catalyzed by carbonic anhydrase. The hydrogen is exchanged across the membrane into the lumen of the collecting duct, and thus acid is excreted into the urine.<sup id="cite_ref-Bruce_1997_41-0" class="reference"><a href="#cite_note-Bruce_1997-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> </p><p>Because of its importance to the reabsorption of water in the intestine, mutations in protein DRA cause a condition called <a href="/wiki/Congenital_chloride_diarrhea" title="Congenital chloride diarrhea">congenital chloride diarrhea</a> (CCD).<sup id="cite_ref-42" class="reference"><a href="#cite_note-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup> This disorder is caused by an autosomal recessive mutation in the DRA gene on chromosome 7.<sup id="cite_ref-43" class="reference"><a href="#cite_note-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup> CCD symptoms in newborns are chronic diarrhea with failure to thrive, and the disorder is characterized by diarrhea that causes <a href="/wiki/Metabolic_alkalosis" title="Metabolic alkalosis">metabolic alkalosis</a>. </p><p>Mutations of kidney AE1 can lead to <a href="/wiki/Distal_renal_tubular_acidosis" title="Distal renal tubular acidosis">distal renal tubular acidosis</a>, a disorder characterized by the inability to secrete acid into the urine. This causes <a href="/wiki/Metabolic_acidosis" title="Metabolic acidosis">metabolic acidosis</a>, where the blood is too acidic. A chronic state of metabolic acidosis can the health of the bones, kidneys, muscles, and cardiovascular system.<sup id="cite_ref-Bruce_1997_41-1" class="reference"><a href="#cite_note-Bruce_1997-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> Mutations in <a href="/wiki/Erythrocyte" class="mw-redirect" title="Erythrocyte">erythrocyte</a> AE1 cause alterations of its function, leading to changes in red blood cell <a href="/wiki/Morphology_(biology)" title="Morphology (biology)">morphology</a> and function. This can have serious consequences because the shape of red blood cells is closely tied to their function of gas exchange in the lungs and tissues. One such condition is <a href="/wiki/Hereditary_spherocytosis" title="Hereditary spherocytosis">hereditary spherocytosis</a>, a genetic disorder characterized by spherical red blood cells. Another is <a href="/wiki/Southeast_Asian_ovalocytosis" title="Southeast Asian ovalocytosis">Southeast Asian ovalocytosis</a>, where a deletion in the AE1 gene generates oval-shaped erythrocytes.<sup id="cite_ref-44" class="reference"><a href="#cite_note-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> Finally, <a href="/wiki/Overhydrated_hereditary_stomatocytosis" class="mw-redirect" title="Overhydrated hereditary stomatocytosis">overhydrated hereditary stomatocytosis</a> is a rare genetic disorder where red blood cells have an abnormally high volume, leading to changes in hydration status.<sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup> </p><p>The proper function of AE2, an isoform of AE1, is important in gastric secretion, osteoclast differentiation and function, and the synthesis of <a href="/wiki/Enamel_organ" title="Enamel organ">enamel</a>. The hydrochloric acid secretion at the apical surface of both gastric parietal cells and osteoclasts relies on chloride-bicarbonate exchange in the basolateral surface.<sup id="cite_ref-Cordat_2009_46-0" class="reference"><a href="#cite_note-Cordat_2009-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Wu_2008_47-0" class="reference"><a href="#cite_note-Wu_2008-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> Studies found that mice with nonfunctional AE2 did not secrete <a href="/wiki/Hydrochloric_acid" title="Hydrochloric acid">hydrochloric acid</a>, and it was concluded that the exchanger is necessary for hydrochloric acid loading in parietal cells.<sup id="cite_ref-Cordat_2009_46-1" class="reference"><a href="#cite_note-Cordat_2009-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> When AE2 expression was suppressed in an animal model, cell lines were unable to differentiate into osteoclasts and perform their functions. Additionally, cells that had osteoclast markers but were deficient in AE2 were abnormal compared to the wild-type cells and were unable to resorb mineralized tissue. This demonstrates the importance of AE2 in osteoclast function.<sup id="cite_ref-Wu_2008_47-1" class="reference"><a href="#cite_note-Wu_2008-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> Finally, as the <a href="/wiki/Hydroxyapatite" title="Hydroxyapatite">hydroxyapatite crystals</a> of enamel are being formed, a lot of hydrogen is produced, which must be neutralized so that mineralization can proceed. Mice with inactivated AE2 were toothless and suffered from incomplete enamel maturation.<sup id="cite_ref-Cordat_2009_46-2" class="reference"><a href="#cite_note-Cordat_2009-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Chloride-hydrogen_antiporter">Chloride-hydrogen antiporter</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=9" title="Edit section: Chloride-hydrogen antiporter"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The chloride-hydrogen antiporter facilitates the exchange of chloride ions for hydrogen ions across plasma membranes, thus playing a critical role in maintaining acid-base balance and chloride homeostasis. It is found in various tissues, including the gastrointestinal tract, kidneys, and <a href="/wiki/Pancreas" title="Pancreas">pancreas</a>.<sup id="cite_ref-Jentsch_2018_48-0" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> The well-known chloride-hydrogen antiporters belong in the CLC family, which have isoforms from CLC-1 to CLC-7, each with a distinct tissue distribution. Their structure involves two CLC proteins coming together to form a homodimer or a heterodimer where both monomers contain an ion translocation pathway. CLC proteins can either be ion channels or anion-proton exchangers, so CLC-1 and CLC-2 are membrane chloride channels, while CLC-3 through CLC-7 are chloride-hydrogen exchangers.<sup id="cite_ref-Jentsch_2018_48-1" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p><p>CLC-4 is a member of the CLC family that is prominent in the brain, but is also located in the liver, kidneys, heart, skeletal muscle, and intestine. It likely resides in <a href="/wiki/Endosome" title="Endosome">endosomes</a> and participates in their acidification, but can also be expressed in the endoplasmic reticulum and plasma membrane. Its roles are not entirely clear, but CLC-4 has been found to possibly participate in endosomal acidification, <a href="/wiki/Transferrin" title="Transferrin">transferrin</a> trafficking, renal <a href="/wiki/Endocytosis" title="Endocytosis">endocytosis</a>, and the hepatic <a href="/wiki/Secretory_pathway" class="mw-redirect" title="Secretory pathway">secretory pathway</a>.<sup id="cite_ref-Jentsch_2018_48-2" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p><p>CLC-5 is one of the best-studied members of this protein family. It shares 80% of its amino acid sequence with CLC-3 and CLC-4, but it is mainly found in the kidney, especially in the <a href="/wiki/Proximal_tubule" title="Proximal tubule">proximal tubule</a>, <a href="/wiki/Collecting_duct_system" title="Collecting duct system">collecting duct</a>, and <a href="/wiki/Ascending_limb_of_loop_of_Henle" title="Ascending limb of loop of Henle">ascending limb of the loop of Henle</a>. It functions to transport substances through the endosomal membrane, so it is crucial for <a href="/wiki/Pinocytosis" title="Pinocytosis">pinocytosis</a>, <a href="/wiki/Receptor-mediated_endocytosis" title="Receptor-mediated endocytosis">receptor-mediated endocytosis</a>, and endocytosis of plasma membrane proteins from the apical surface.<sup id="cite_ref-Jentsch_2018_48-3" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p><p>CLC-7 is another example of a CLC family protein. It is ubiquitously expressed as the chloride-hydrogen antiporter in <a href="/wiki/Lysosome" title="Lysosome">lysosomes</a> and in the ruffled border of osteoclasts. CLC-7 may be important for regulating to concentration of chloride in lysosomes. It is associated with a protein called Ostm1, forming a complex that allows CLC-7 to carry out its functions. For example, these proteins are crucial to the process of acidifying the resorption lacuna, which enables <a href="/wiki/Bone_remodeling" title="Bone remodeling">bone remodeling</a> to occur.<sup id="cite_ref-Jentsch_2018_48-4" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p><p>CLC-4 has been connected with mental retardation involving <a href="/wiki/Seizure_disorders" class="mw-redirect" title="Seizure disorders">seizure disorders</a>, facial abnormalities, and behavior disorders. Studies found <a href="/wiki/Frameshift_mutation" title="Frameshift mutation">frameshift</a> and <a href="/wiki/Missense_mutation" title="Missense mutation">missense mutations</a> in patients exhibiting these symptoms. Because these symptoms were mostly exhibited in males, with less severe pathology in females, it is likely <a href="/wiki/X-linked" class="mw-redirect" title="X-linked">X-linked</a>. Studies done on animal models have also shown the possibility of a connection between nonfunctional CLC-4 and impaired neural branching of hippocampus neurons.<sup id="cite_ref-Jentsch_2018_48-5" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p><p>Defects in the CLC-5 gene were shown to be the cause of 60% of cases of <a href="/wiki/Dent%27s_disease" title="Dent's disease">Dent's disease</a>, which is characterized by <a href="/wiki/Tubular_proteinuria" title="Tubular proteinuria">tubular proteinuria</a>, formation of <a href="/wiki/Kidney_stones" class="mw-redirect" title="Kidney stones">kidney stones</a>, excess calcium in the urine, <a href="/wiki/Nephrocalcinosis" title="Nephrocalcinosis">nephrocalcinosis</a>, and <a href="/wiki/Chronic_kidney_failure" class="mw-redirect" title="Chronic kidney failure">chronic kidney failure</a>. This is caused by abnormalities that occur in the endocytosis process when CLC-5 is mutated.<sup id="cite_ref-Jentsch_2018_48-6" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-49" class="reference"><a href="#cite_note-49"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup> Dent's disease itself is one of the causes of <a href="/wiki/Fanconi_syndrome" title="Fanconi syndrome">Fanconi syndrome</a>, which occurs when the <a href="/wiki/Proximal_convoluted_tubules" class="mw-redirect" title="Proximal convoluted tubules">proximal convoluted tubules</a> of the kidney do not perform an adequate level of reabsorption. It causes molecules produced by metabolic pathways, such as amino acids, glucose, and <a href="/wiki/Uric_acid" title="Uric acid">uric acid</a> to be excreted in the urine instead of being reabsorbed. The result is <a href="/wiki/Polyuria" title="Polyuria">polyuria</a>, <a href="/wiki/Dehydration" title="Dehydration">dehydration</a>, <a href="/wiki/Rickets" title="Rickets">rickets</a> in children, <a href="/wiki/Osteomalacia" title="Osteomalacia">osteomalacia</a> in adults, <a href="/wiki/Acidosis" title="Acidosis">acidosis</a>, and <a href="/wiki/Hypokalemia" title="Hypokalemia">hypokalemia</a>.<sup id="cite_ref-50" class="reference"><a href="#cite_note-50"><span class="cite-bracket">[</span>50<span class="cite-bracket">]</span></a></sup> </p><p>CLC-7's role in osteoclast function was revealed by studies on knockout mice that developed severe <a href="/wiki/Osteopetrosis" title="Osteopetrosis">osteopetrosis</a>. These mice were smaller, had shortened long bones, disorganized <a href="/wiki/Trabecula" title="Trabecula">trabecular</a> structure, a missing <a href="/wiki/Medullary_cavity" title="Medullary cavity">medullary cavity</a>, and their teeth did not erupt. This was found to be caused by <a href="/wiki/Deletion_mutation" class="mw-redirect" title="Deletion mutation">deletion mutations</a>, missense mutations, and <a href="/wiki/Gain-of-function_mutation" class="mw-redirect" title="Gain-of-function mutation">gain-of-function mutations</a> that sped up the gating of CLC-7.<sup id="cite_ref-Jentsch_2018_48-7" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-51" class="reference"><a href="#cite_note-51"><span class="cite-bracket">[</span>51<span class="cite-bracket">]</span></a></sup> CLC-7 is expressed in almost every neuronal cell type, and its loss led to widespread neurodegeneration in mice, especially in the hippocampus. In longer-lived models, the <a href="/wiki/Cerebral_cortex" title="Cerebral cortex">cortex</a> and <a href="/wiki/Hippocampus" title="Hippocampus">hippocampus</a> had almost entirely disappeared after 1.5 years.<sup id="cite_ref-Jentsch_2018_48-8" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> Finally, because of its importance in lysosomes, altered expression of CLC-7 can lead to <a href="/wiki/Lysosomal_storage_disorders" class="mw-redirect" title="Lysosomal storage disorders">lysosomal storage disorders</a>. Mice with a mutation introduced to the CLC-7 gene developed lysosomal storage disease and <a href="/w/index.php?title=Retinal_degeneration_(rhodopsin_mutation)&action=edit&redlink=1" class="new" title="Retinal degeneration (rhodopsin mutation) (page does not exist)">retinal degeneration</a>.<sup id="cite_ref-Jentsch_2018_48-9" class="reference"><a href="#cite_note-Jentsch_2018-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Reduced_folate_carrier_protein">Reduced folate carrier protein</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=10" title="Edit section: Reduced folate carrier protein"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The reduced folate carrier protein (RFC) is a transmembrane protein responsible for the transport of <a href="/wiki/Folate" title="Folate">folate</a>, or <a href="/wiki/Vitamin_B9" class="mw-redirect" title="Vitamin B9">vitamin B9</a>, into cells. It uses the large gradient of organic phosphate to move folate into the cell against its concentration gradient. The RFC protein can transport folates, reduced folates, the derivatives of reduced folate, and the drug <a href="/wiki/Methotrexate" title="Methotrexate">methotrexate</a>. The transporter is encoded by the <a href="/wiki/SLC19A1" class="mw-redirect" title="SLC19A1">SLC19A1</a> gene and is ubiquitously expressed in human cells. Its peak activity occurs at pH 7.4, with no activity occurring below pH 6.4.<sup id="cite_ref-52" class="reference"><a href="#cite_note-52"><span class="cite-bracket">[</span>52<span class="cite-bracket">]</span></a></sup> The RFC protein is critical because folates take the form of <a href="/wiki/Hydrophile" title="Hydrophile">hydrophilic</a> anions at physiological pH, so they do not diffuse naturally across biological membranes. Folate is essential for processes such as <a href="/wiki/DNA_synthesis" title="DNA synthesis">DNA synthesis</a>, <a href="/wiki/DNA_repair" title="DNA repair">repair</a>, and <a href="/wiki/Methylation" title="Methylation">methylation</a>, and without entry into cells, these could not occur.<sup id="cite_ref-Liu_2003_53-0" class="reference"><a href="#cite_note-Liu_2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </p><p>Because folates are essential for various life-sustaining processes, a deficiency in this molecule can lead to fetal abnormalities, neurological disorders, cardiovascular disease, and cancer. Folates cannot be synthesized in the body, so it must be taken in through diet and moved into cells. Without the RFC protein facilitating this movement, processes such as embryological development and DNA repair cannot occur.<sup id="cite_ref-Liu_2003_53-1" class="reference"><a href="#cite_note-Liu_2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </p><p>Adequate folate levels are required for the development of the <a href="/wiki/Neural_tube" title="Neural tube">neural tube</a> in the fetus. Folate deficiency during pregnancy increases the risk of defects such as <a href="/wiki/Spina_bifida" title="Spina bifida">spina bifida</a> and <a href="/wiki/Anencephaly" title="Anencephaly">anencephaly</a>.<sup id="cite_ref-54" class="reference"><a href="#cite_note-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> In mouse models, inactivating both alleles of the FRC protein gene causes death of the embryo. Even if folate is supplemented during gestation, the mice died within two weeks of birth from the failure of hematopoietic tissues.<sup id="cite_ref-Liu_2003_53-2" class="reference"><a href="#cite_note-Liu_2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </p><p>Altered function of the RFC protein can increase folate deficiency, enhancing cardiovascular disease, neurodegenerative diseases, and cancer. In terms of cardiovascular issues, folate contributes to <a href="/wiki/Homocysteine" title="Homocysteine">homocysteine</a> metabolism. Low folate levels result in elevated homocysteine levels, which is a risk factor for cardiovascular diseases.<sup id="cite_ref-Liu_2003_53-3" class="reference"><a href="#cite_note-Liu_2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-55" class="reference"><a href="#cite_note-55"><span class="cite-bracket">[</span>55<span class="cite-bracket">]</span></a></sup> In terms of cancer, folate deficiency is related to an increased risk, especially that of colorectal cancers. In mouse models with altered RFC protein expression showed increased transcripts of genes related to colon cancer and increased proliferation of colonocytes.<sup id="cite_ref-Liu_2003_53-4" class="reference"><a href="#cite_note-Liu_2003-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> The cancer risk is likely related to the FRC protein's role in DNA synthesis because inadequate levels of folate can lead to DNA damage and aberrant DNA methylation.<sup id="cite_ref-56" class="reference"><a href="#cite_note-56"><span class="cite-bracket">[</span>56<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Vesicle_neurotransmitter_antiporters">Vesicle neurotransmitter antiporters</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=11" title="Edit section: Vesicle neurotransmitter antiporters"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/w/index.php?title=Vesicle_neurotransmitter_antiporter&action=edit&redlink=1" class="new" title="Vesicle neurotransmitter antiporter (page does not exist)">Vesicle neurotransmitter antiporters</a> are responsible for packaging <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitters</a> into vesicles in neurons. They utilize the electrochemical gradient of hydrogen protons across the membranes of <a href="/wiki/Synaptic_vesicle" title="Synaptic vesicle">synaptic vesicles</a> to move neurotransmitters into them. This is essential for the process of <a href="/wiki/Synaptic_transmission" class="mw-redirect" title="Synaptic transmission">synaptic transmission</a>, which requires neurotransmitters to be released into the <a href="/wiki/Synapse" title="Synapse">synapse</a> to bind to receptors on the next neuron.<sup id="cite_ref-Wimalasena_2011_57-0" class="reference"><a href="#cite_note-Wimalasena_2011-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p><p>One of the best characterized of these antiporters is the <a href="/wiki/Vesicular_monoamine_transporter" title="Vesicular monoamine transporter">vesicular monoamine transporter</a> (VMAT). It is responsible for the storage, sorting, and release of neurotransmitters, as well as for protecting them from autoxidation. VMAT's transport functions are dependent on the electrochemical gradient created by a vesicular hydrogen proton-ATPase.<sup id="cite_ref-Wimalasena_2011_57-1" class="reference"><a href="#cite_note-Wimalasena_2011-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> <a href="/wiki/VMAT1" class="mw-redirect" title="VMAT1">VMAT1</a> and <a href="/wiki/VMAT2" class="mw-redirect" title="VMAT2">VMAT2</a> are two isoforms that can transport <a href="/wiki/Monoamines" class="mw-redirect" title="Monoamines">monoamines</a> such as <a href="/wiki/Serotonin" title="Serotonin">serotonin</a>, <a href="/wiki/Norepinephrine" title="Norepinephrine">norepinephrine</a>, and <a href="/wiki/Dopamine" title="Dopamine">dopamine</a> in a proton-dependent fashion. VMAT1 can be found in <a href="/wiki/Neuroendocrine_cell" title="Neuroendocrine cell">neuroendocrine cells</a>, while VMAT2 can be found in the neurons of the central and peripheral nervous systems, as well as in adrenal <a href="/wiki/Chromaffin_cell" title="Chromaffin cell">chromaffin cells</a>.<sup id="cite_ref-58" class="reference"><a href="#cite_note-58"><span class="cite-bracket">[</span>58<span class="cite-bracket">]</span></a></sup> </p><p>Another important vesicle neurotransmitter antiporter is the <a href="/wiki/Vesicular_glutamate_transporter" class="mw-redirect" title="Vesicular glutamate transporter">vesicular glutamate transporter</a> (VGLUT). This family of proteins includes three isoforms, <a href="/wiki/VGlut" class="mw-redirect" title="VGlut">VGLUT1</a>, <a href="/wiki/VGlut" class="mw-redirect" title="VGlut">VGLUT2</a>, and <a href="/wiki/VGLUT3" class="mw-redirect" title="VGLUT3">VGLUT3</a>, that are responsible for packaging <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> - the most abundant excitatory neurotransmitter in the brain - into synaptic vesicles.<sup id="cite_ref-Fremeau_2004_59-0" class="reference"><a href="#cite_note-Fremeau_2004-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup> These antiporters vary by location. VGLUT1 is found in areas of the brain related to higher cognitive functions, such as the <a href="/wiki/Neocortex" title="Neocortex">neocortex</a>. VGLUT2 works to regulate basic physiological functions and is expressed in subcortical regions such as the <a href="/wiki/Brainstem" title="Brainstem">brainstem</a> and <a href="/wiki/Hypothalamus" title="Hypothalamus">hypothalamus</a>. Finally, VGLUT3 can be seen in neurons that also express other neurotransmitters.<sup id="cite_ref-Fremeau_2004_59-1" class="reference"><a href="#cite_note-Fremeau_2004-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-60" class="reference"><a href="#cite_note-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup> </p><p>VMAT2 has been found to contribute to neurological conditions such as <a href="/wiki/Mood_disorder" title="Mood disorder">mood disorders</a> and Parkinson's disease. Studies done on an animal model of <a href="/wiki/Clinical_depression" class="mw-redirect" title="Clinical depression">clinical depression</a> showed that functional alterations of VMAT2 were associated with depression. The <a href="/wiki/Nucleus_accumbens" title="Nucleus accumbens">nucleus accumbens</a>, <a href="/wiki/Pars_compacta" title="Pars compacta">pars compacta</a> of the <a href="/wiki/Substantia_nigra" title="Substantia nigra">substantia nigra</a>, and <a href="/wiki/Ventral_tegmental_area" title="Ventral tegmental area">ventral tegmental area</a> - all subregions of the brain involved in clinical depression - were found to have lower VMAT2 levels.<sup id="cite_ref-61" class="reference"><a href="#cite_note-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> The likely cause for this is VMAT's relationship with serotonin and norepinephrine, neurotransmitters that are related to depression. VMAT dysfunction may contribute to the altered levels of these neurotransmitters that occur in mood disorders.<sup id="cite_ref-62" class="reference"><a href="#cite_note-62"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup> </p><p>Lower expression of VMAT2 was found to correlate with a higher susceptibility to <a href="/wiki/Parkinson%27s_disease" title="Parkinson's disease">Parkinson's disease</a> and the antiporter's <a href="/wiki/Messenger_RNA" title="Messenger RNA">mRNA</a> was found in all cell groups damaged by Parkinson's.<sup id="cite_ref-Miller_1999_63-0" class="reference"><a href="#cite_note-Miller_1999-63"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup> This is likely because VMAT2 dysfunction can lead to a decrease in dopamine packaging into vesicles, accounting for the dopamine depletion that characterizes the disease.<sup id="cite_ref-64" class="reference"><a href="#cite_note-64"><span class="cite-bracket">[</span>64<span class="cite-bracket">]</span></a></sup> For this reason, the antiporter has been identified as a protective factor that could be targeted for the prevention of Parkinson's.<sup id="cite_ref-Miller_1999_63-1" class="reference"><a href="#cite_note-Miller_1999-63"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup> </p><p>Because alterations in glutamate release have been linked to the generation of <a href="/wiki/Seizure" title="Seizure">seizures</a> in <a href="/wiki/Epilepsy" title="Epilepsy">epilepsy</a>, alterations in the function of VGLUT may be implicated.<sup id="cite_ref-Petr_2015_65-0" class="reference"><a href="#cite_note-Petr_2015-65"><span class="cite-bracket">[</span>65<span class="cite-bracket">]</span></a></sup> A study was conducted where the VGLUT1 gene was inactivated in the <a href="/wiki/Astrocyte" title="Astrocyte">astrocytes</a> and neurons of an animal model. When the gene was inactivated in astrocytes, there was an 80% loss in the antiporter protein itself and, in turn, a reduction in glutamate uptake. The mice in this condition experienced seizures, lower body mass, and higher mortality rates. The researchers concluded that VGLUT1 function in astrocytes is therefore critical to epilepsy resistance and normal weight gain.<sup id="cite_ref-Petr_2015_65-1" class="reference"><a href="#cite_note-Petr_2015-65"><span class="cite-bracket">[</span>65<span class="cite-bracket">]</span></a></sup> </p><p>There is a lot of evidence that the glutamate system plays a role in long-term cell growth and <a href="/wiki/Synaptic_plasticity" title="Synaptic plasticity">synaptic plasticity</a>. Disturbances of these processes has been linked to the pathology of mood disorders. The link between the function of the glutamatergic neurotransmitter system and mood disorders sets up VGLUT as one of the targets for treatment.<sup id="cite_ref-66" class="reference"><a href="#cite_note-66"><span class="cite-bracket">[</span>66<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=12" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1184024115">.mw-parser-output .div-col{margin-top:0.3em;column-width:30em}.mw-parser-output .div-col-small{font-size:90%}.mw-parser-output .div-col-rules{column-rule:1px solid #aaa}.mw-parser-output .div-col dl,.mw-parser-output .div-col ol,.mw-parser-output .div-col ul{margin-top:0}.mw-parser-output .div-col li,.mw-parser-output .div-col dd{page-break-inside:avoid;break-inside:avoid-column}</style><div class="div-col" style="column-width: 20em;"> <ul><li><a href="/wiki/Active_transport" title="Active transport">Active transport</a></li> <li><a href="/wiki/Adenine_nucleotide_translocator" title="Adenine nucleotide translocator">Adenine nucleotide translocator</a></li> <li><a href="/wiki/Cotransporter" title="Cotransporter">Cotransporter</a></li> <li><a href="/wiki/Reduced_folate_carrier_family" title="Reduced folate carrier family">Reduced folate carrier family</a></li> <li><a href="/wiki/Sodium-calcium_exchanger" title="Sodium-calcium exchanger">Sodium-calcium exchanger</a></li> <li><a href="/wiki/Sodium%E2%80%93hydrogen_antiporter" title="Sodium–hydrogen antiporter">Sodium-hydrogen antiporter</a></li> <li><a href="/wiki/Symporter" title="Symporter">Symporter</a></li> <li><a href="/wiki/Uniporter" title="Uniporter">Uniporter</a></li> <li><a href="/wiki/Vesicular_monoamine_transporter" title="Vesicular monoamine transporter">Vesicular monoamine transporter</a></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=13" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFConnectivid-D2021" class="citation web cs1">Connectivid-D (2021-09-04). <a class="external text" href="https://commons.wikimedia.org/wiki/File:Active_Transport_Proteins.png">"Membrane proteins involved in active transport can function as uniporters"</a><span class="reference-accessdate">. Retrieved <span class="nowrap">2024-04-10</span></span>. <q>One molecule one direction, symporters: two molecules one direction or antiporters: two molecules opposite directions.</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=Membrane+proteins+involved+in+active+transport+can+function+as+uniporters&rft.date=2021-09-04&rft.au=Connectivid-D&rft_id=https%3A%2F%2Fcommons.wikimedia.org%2Fwiki%2FFile%3AActive_Transport_Proteins.png&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></span> </li> <li id="cite_note-Lodish_2021-2"><span class="mw-cite-backlink">^ <a href="#cite_ref-Lodish_2021_2-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Lodish_2021_2-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Lodish_2021_2-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Lodish_2021_2-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Lodish_2021_2-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Lodish_2021_2-5"><sup><i><b>f</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLodish2021" class="citation book cs1">Lodish HF (2021). <i>Molecular cell biology</i> (Ninth ed.). Austin: Macmillan Learning. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-319-20852-3" title="Special:BookSources/978-1-319-20852-3"><bdi>978-1-319-20852-3</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Molecular+cell+biology&rft.place=Austin&rft.edition=Ninth&rft.pub=Macmillan+Learning&rft.date=2021&rft.isbn=978-1-319-20852-3&rft.aulast=Lodish&rft.aufirst=HF&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></span> </li> <li id="cite_note-3"><span class="mw-cite-backlink"><b><a href="#cite_ref-3">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDittmar2017" class="citation web cs1">Dittmar E (2017-11-12). <a class="external text" href="https://commons.wikimedia.org/w/index.php?curid=64036779">"This picture represents antiport"</a><span class="reference-accessdate">. Retrieved <span class="nowrap">2024-04-10</span></span>. <q>The yellow triangle shows the concentration gradient for the yellow circles while the blue triangle shows the concentration gradient for the blue circles and the purple rods are the transport protein bundle. The blue circles are moving against their concentration gradient through a transport protein which requires energy while the yellow circles move down their concentration gradient which releases energy. The yellow circles produce more energy through chemiosmosis than what is required to move the blue circles so the movement is coupled and some energy is cancelled out. One example is the sodium-proton exchanger which allows protons to go down their concentration gradient into the cell while pumping sodium out of the cell.</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=This+picture+represents+antiport.&rft.date=2017-11-12&rft.aulast=Dittmar&rft.aufirst=E&rft_id=https%3A%2F%2Fcommons.wikimedia.org%2Fw%2Findex.php%3Fcurid%3D64036779&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></span> </li> <li id="cite_note-Yu_1997-4"><span class="mw-cite-backlink">^ <a href="#cite_ref-Yu_1997_4-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Yu_1997_4-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Yu_1997_4-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Yu_1997_4-3"><sup><i><b>d</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFYuChoi1997" class="citation journal cs1">Yu SP, Choi DW (June 1997). 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(April 2015). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4380995">"Conditional deletion of the glutamate transporter GLT-1 reveals that astrocytic GLT-1 protects against fatal epilepsy while neuronal GLT-1 contributes significantly to glutamate uptake into synaptosomes"</a>. <i>The Journal of Neuroscience</i>. <b>35</b> (13): <span class="nowrap">5187–</span>5201. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1523%2Fjneurosci.4255-14.2015">10.1523/jneurosci.4255-14.2015</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4380995">4380995</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/25834045">25834045</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Neuroscience&rft.atitle=Conditional+deletion+of+the+glutamate+transporter+GLT-1+reveals+that+astrocytic+GLT-1+protects+against+fatal+epilepsy+while+neuronal+GLT-1+contributes+significantly+to+glutamate+uptake+into+synaptosomes&rft.volume=35&rft.issue=13&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5187-%3C%2Fspan%3E5201&rft.date=2015-04&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4380995%23id-name%3DPMC&rft_id=info%3Apmid%2F25834045&rft_id=info%3Adoi%2F10.1523%2Fjneurosci.4255-14.2015&rft.aulast=Petr&rft.aufirst=GT&rft.au=Sun%2C+Y&rft.au=Frederick%2C+NM&rft.au=Zhou%2C+Y&rft.au=Dhamne%2C+SC&rft.au=Hameed%2C+MQ&rft.au=Miranda%2C+C&rft.au=Bedoya%2C+EA&rft.au=Fischer%2C+KD&rft.au=Armsen%2C+W&rft.au=Wang%2C+J&rft.au=Danbolt%2C+NC&rft.au=Rotenberg%2C+A&rft.au=Aoki%2C+CJ&rft.au=Rosenberg%2C+PA&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4380995&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></span> </li> <li id="cite_note-66"><span class="mw-cite-backlink"><b><a href="#cite_ref-66">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSanacoraZarateKrystalManji2008" class="citation journal cs1">Sanacora G, Zarate CA, Krystal JH, Manji HK (May 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2715836">"Targeting the glutamatergic system to develop novel, improved therapeutics for mood disorders"</a>. <i>Nature Reviews. Drug Discovery</i>. <b>7</b> (5): <span class="nowrap">426–</span>437. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnrd2462">10.1038/nrd2462</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2715836">2715836</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18425072">18425072</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Reviews.+Drug+Discovery&rft.atitle=Targeting+the+glutamatergic+system+to+develop+novel%2C+improved+therapeutics+for+mood+disorders&rft.volume=7&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E426-%3C%2Fspan%3E437&rft.date=2008-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2715836%23id-name%3DPMC&rft_id=info%3Apmid%2F18425072&rft_id=info%3Adoi%2F10.1038%2Fnrd2462&rft.aulast=Sanacora&rft.aufirst=G&rft.au=Zarate%2C+CA&rft.au=Krystal%2C+JH&rft.au=Manji%2C+HK&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2715836&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=14" title="Edit section: Further reading"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239549316">.mw-parser-output .refbegin{margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}@media screen{.mw-parser-output .refbegin{font-size:90%}}</style><div class="refbegin" style=""> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPakEkendéKifleO'Connell2013" class="citation journal cs1">Pak JE, Ekendé EN, Kifle EG, O'Connell JD, De Angelis F, Tessema MB, et al. (November 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3832018">"Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. <b>110</b> (46): <span class="nowrap">18484–</span>18489. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2013PNAS..11018484P">2013PNAS..11018484P</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.1318705110">10.1073/pnas.1318705110</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3832018">3832018</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/24173033">24173033</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=Structures+of+intermediate+transport+states+of+ZneA%2C+a+Zn%28II%29%2Fproton+antiporter&rft.volume=110&rft.issue=46&rft.pages=%3Cspan+class%3D%22nowrap%22%3E18484-%3C%2Fspan%3E18489&rft.date=2013-11&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3832018%23id-name%3DPMC&rft_id=info%3Apmid%2F24173033&rft_id=info%3Adoi%2F10.1073%2Fpnas.1318705110&rft_id=info%3Abibcode%2F2013PNAS..11018484P&rft.aulast=Pak&rft.aufirst=JE&rft.au=Ekend%C3%A9%2C+EN&rft.au=Kifle%2C+EG&rft.au=O%27Connell%2C+JD&rft.au=De+Angelis%2C+F&rft.au=Tessema%2C+MB&rft.au=Derfoufi%2C+KM&rft.au=Robles-Colmenares%2C+Y&rft.au=Robbins%2C+RA&rft.au=Goormaghtigh%2C+E&rft.au=Vandenbussche%2C+G&rft.au=Stroud%2C+RM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3832018&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAntiporter" class="Z3988"></span></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Antiporter&action=edit&section=15" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Antiporters">Antiporters</a> at the U.S. National Library of Medicine <a href="/wiki/Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output 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