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However, the cellular functions of PS1 are unknown. We showed predominant localization of PS1 to cell-cell contacts of the plasma" /> <meta name="twitter:image" content="http://a.academia-assets.com/images/twitter-card.jpeg" /> <meta property="fb:app_id" content="2369844204" /> <meta property="og:type" content="article" /> <meta property="og:url" content="https://www.academia.edu/23569397/The_Role_of_Alzheimers_Disease_Related_Presenilin_1_in_Intercellular_Adhesion" /> <meta property="og:title" content="The Role of Alzheimer's Disease-Related Presenilin 1 in Intercellular Adhesion" /> <meta property="og:image" content="http://a.academia-assets.com/images/open-graph-icons/fb-paper.gif" /> <meta property="og:description" content="Most cases of familial early-onset Alzheimer&#39;s disease are caused by mutations in the presenilin 1 (PS1) gene. However, the cellular functions of PS1 are unknown. We showed predominant localization of PS1 to cell-cell contacts of the plasma" /> <meta property="article:author" content="https://independent.academia.edu/MVitek" /> <meta name="description" content="Most cases of familial early-onset Alzheimer&#39;s disease are caused by mutations in the presenilin 1 (PS1) gene. However, the cellular functions of PS1 are unknown. 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window.loswp.work = {"work":{"id":23569397,"created_at":"2016-03-22T08:26:03.369-07:00","from_world_paper_id":150861356,"updated_at":"2024-11-16T08:16:37.849-08:00","_data":{"grobid_abstract":"Most cases of familial early-onset Alzheimer's disease are caused by mutations in the presenilin 1 (PS1) gene. However, the cellular functions of PS1 are unknown. We showed predominant localization of PS1 to cell-cell contacts of the plasma membrane in human prostate epithelial tissue and in a human epithelial cell line HEp2 stably transfected with an inducible PS1 construct. PS1 co-immunoprecipitated with ␤-catenin from cell lysates of stable transfectants. Conversely, PS1 lacking the PS1-␤-catenin interaction site did not co-immunoprecipitate with ␤-catenin and was not recruited to the cell-cell contacts. L cells, which do not form tight intercellular contacts, formed clusters of adhered cells after stable transfection with GFP-PS1 cDNA and demonstrated a clear preference for independent aggregation in the mixed cultures. However, L cells transfected with mutant GFP-PS1 constructs, which had a truncated N-terminus of PS1 or deleted PS1-␤-catenin interaction site, failed to form intercellular contacts. In addition, in primary cultures of mouse cortical neurons PS1 was highly concentrated on the surface of extended growth cones. Taken together, our results suggest an important role of PS1 in intercellular adhesion in epithelial cells and neurons.","publication_date":"2001,,","publication_name":"Experimental Cell Research","grobid_abstract_attachment_id":"43993901"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"The Role of Alzheimer's Disease-Related Presenilin 1 in Intercellular Adhesion","broadcastable":false,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [45602722]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "full_page_mobile_sutd_modal"; window.loswp.useOptimizedScribd4genScript = false; window.loginModal = {}; window.loginModal.appleClientId = 'edu.academia.applesignon'; window.userInChina = "false";</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":43993901,"attachmentType":"pdf"}"><img alt="First page of “The Role of Alzheimer's Disease-Related Presenilin 1 in Intercellular Adhesion”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/43993901/mini_magick20190215-479-4yksvu.png?1550235465" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">The Role of Alzheimer's Disease-Related Presenilin 1 in Intercellular Adhesion</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="45602722" href="https://independent.academia.edu/MVitek"><img alt="Profile image of Michael Vitek" class="ds-work-card--author-avatar" src="//a.academia-assets.com/images/s65_no_pic.png" />Michael Vitek</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">2001, Experimental Cell Research</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">13 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 23569397; const worksViewsPath = "/v0/works/views?subdomain_param=api&work_ids%5B%5D=23569397"; const getWorkViews = async (workId) => { const response = await fetch(worksViewsPath); if (!response.ok) { throw new Error('Failed to load work views'); } const data = await response.json(); return data.views[workId]; }; // Get the view count for the work - we send this immediately rather than waiting for // the DOM to load, so it can be available as soon as possible (but without holding up // the backend or other resource requests, because it's a bit expensive and not critical). const viewCount = await getWorkViews(workId); const updateViewCount = (viewCount) => { try { const viewCountNumber = parseInt(viewCount, 10); if (viewCountNumber === 0) { // Remove the whole views element if there are zero views. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); return; } const commaizedViewCount = viewCountNumber.toLocaleString(); const viewCountBody = document.getElementById('work-metadata-view-count'); if (!viewCountBody) { throw new Error('Failed to find work views element'); } viewCountBody.textContent = `${commaizedViewCount} views`; } catch (error) { // Remove the whole views element if there was some issue parsing. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); throw new Error(`Failed to parse view count: ${viewCount}`, error); } }; // If the DOM is still loading, wait for it to be ready before updating the view count. if (document.readyState === "loading") { document.addEventListener('DOMContentLoaded', () => { updateViewCount(viewCount); }); // Otherwise, just update it immediately. } else { updateViewCount(viewCount); } })();</script></div><p class="ds-work-card--work-abstract ds-work-card--detail ds2-5-body-md">Most cases of familial early-onset Alzheimer's disease are caused by mutations in the presenilin 1 (PS1) gene. However, the cellular functions of PS1 are unknown. We showed predominant localization of PS1 to cell-cell contacts of the plasma membrane in human prostate epithelial tissue and in a human epithelial cell line HEp2 stably transfected with an inducible PS1 construct. PS1 co-immunoprecipitated with ␤-catenin from cell lysates of stable transfectants. Conversely, PS1 lacking the PS1-␤-catenin interaction site did not co-immunoprecipitate with ␤-catenin and was not recruited to the cell-cell contacts. L cells, which do not form tight intercellular contacts, formed clusters of adhered cells after stable transfection with GFP-PS1 cDNA and demonstrated a clear preference for independent aggregation in the mixed cultures. However, L cells transfected with mutant GFP-PS1 constructs, which had a truncated N-terminus of PS1 or deleted PS1-␤-catenin interaction site, failed to form intercellular contacts. In addition, in primary cultures of mouse cortical neurons PS1 was highly concentrated on the surface of extended growth cones. Taken together, our results suggest an important role of PS1 in intercellular adhesion in epithelial cells and neurons.</p><div class="ds-work-card--button-container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--work-card","attachmentId":43993901,"attachmentType":"pdf","workUrl":"https://www.academia.edu/23569397/The_Role_of_Alzheimers_Disease_Related_Presenilin_1_in_Intercellular_Adhesion"}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--work-card","attachmentId":43993901,"attachmentType":"pdf","workUrl":"https://www.academia.edu/23569397/The_Role_of_Alzheimers_Disease_Related_Presenilin_1_in_Intercellular_Adhesion"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div><div class="ds-signup-banner-trigger-container"><div class="ds-signup-banner-trigger ds-signup-banner-trigger-control"></div></div><div class="ds-signup-banner ds-signup-banner-control"><div id="ds-signup-banner-close-button"><button class="ds2-5-button ds2-5-button--secondary ds2-5-button--inverse"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">close</span></button></div><div class="ds-signup-banner-ctas"><img src="//a.academia-assets.com/images/academia-logo-capital-white.svg" /><h4 class="ds2-5-heading-serif-sm">Sign up for access to the world's latest research</h4><button class="ds2-5-button ds2-5-button--inverse ds2-5-button--full-width js-swp-download-button" data-signup-modal="{"location":"signup-banner"}">Sign up for free<span class="material-symbols-outlined" style="font-size: 20px" translate="no">arrow_forward</span></button></div><div class="ds-signup-banner-divider"></div><div class="ds-signup-banner-reasons"><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Get notified about relevant papers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Save papers to use in your research</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Join the discussion with peers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Track your impact</span></div></div></div><script>(() => { // Set up signup banner show/hide behavior: // 1. 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They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Cell surface expression of the Alzheimer disease-related presenilin proteins","attachmentId":89328845,"attachmentType":"pdf","work_url":"https://www.academia.edu/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="126441223" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/126441223/Specific_intercellular_binding_of_the_amyloid_precursor_protein_to_the_presenilins_induces_intercellular_signaling_Its_significance_for_Alzheimers_disease">Specific intercellular binding of the -amyloid precursor protein to the presenilins induces intercellular signaling: Its significance for Alzheimer's disease</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="35510034" href="https://independent.academia.edu/NazneenDewji">Nazneen Dewji</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Proceedings of the National Academy of Sciences of the United States of America, 1998</p><p class="ds-related-work--abstract ds2-5-body-sm">Genetic evidence has implicated three proteins, the ␤-amyloid precursor protein (␤-APP) and the two homologous presenilins (PS-1 and PS-2), in the etiology of Alzheimer's disease (AD). How these three proteins jointly contribute to AD, however, is not clear. Nor is any of their normal physiological functions known. Herein, we demonstrate, confirming a prediction made earlier, that ␤-APP and either PS-1 or PS-2 act as a specific membrane-bound ligand binding intercellularly with either of its two membrane receptors. This results in a cell-cell adhesion, after which rapid transient increases in protein tyrosine kinase activity and protein tyrosine phosphorylation occur coordinately inside one or both of the two adherent cells. The spectrum of proteins modified by tyrosine phosphorylation differs depending on whether PS-1 or PS-2 is involved in the specific intercellular binding to ␤-APP, which implies that PS-1 and PS-2 have distinct, rather than redundant, functions in normal physiology. The relevance of this intercellular interaction and signaling process to AD is discussed.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Specific intercellular binding of the -amyloid precursor protein to the presenilins induces intercellular signaling: Its significance for Alzheimer's disease","attachmentId":120318062,"attachmentType":"pdf","work_url":"https://www.academia.edu/126441223/Specific_intercellular_binding_of_the_amyloid_precursor_protein_to_the_presenilins_induces_intercellular_signaling_Its_significance_for_Alzheimers_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/126441223/Specific_intercellular_binding_of_the_amyloid_precursor_protein_to_the_presenilins_induces_intercellular_signaling_Its_significance_for_Alzheimers_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="26536039" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/26536039/Presenilin_1_A_Component_of_Synaptic_and_Endothelial_Adherens_Junctions">Presenilin-1: A Component of Synaptic and Endothelial Adherens Junctions</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="3271495" href="https://mssm.academia.edu/JunichiShioi">Junichi Shioi</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="50504143" href="https://independent.academia.edu/AnastasiosGeorgakopoulos">Anastasios Georgakopoulos</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Annals of the New York Academy of Sciences, 2006</p><p class="ds-related-work--abstract ds2-5-body-sm">Presenilin-1 (PS1) is an integral membrane protein involved in the development of familial Alzheimer disease (FAD). Cadherin-based cell-cell interactions control critical events in cell-cell adhesion and recognition. We obtained evidence that PS1 accumulates at cell-cell contact sites where it colocalizes with components of the cadherin-based adherens junctions. At these sites, PS1 is linked to the cortical cytosksleton and is found at intercellular junctions. PS1 fragments form detergentstable complexes with E-cadherin, β-catenin, and α-catenin, all components of adherens junctions. PS1 overexpression in human kidney cells enhances cell-cell adhesion. Together, our data show that PS1 incorporates into the cadherin/catenin adhesion system and modulates cell-cell adhesion. PS1 concentrates at synaptic contacts and forms complexes with brain E-and N-cadherin, known synaptic components. The PS1 incorporation into the cadherin/catenin complex makes it a potential target for PS1 FAD mutations. Presenilin-1 (PS1) mutations are responsible for most cases of early-onset autosomal dominant familial Alzheimer disease (FAD). PS1 protein is a polytopic transmembrane peptide expressed in many tissues including brain where it is enriched in neurons. Structural studies suggest that PS1 crosses the membrane six or eight times with the N-and C-termini and the large hydrophilic loop all located in the cytoplasm. PS1 has been mainly localized in the endoplasmic reticulum (ER)/Golgi system and in vesicular structures. Most cellular full-length PS1 is cleaved within the large cytoplasmic loop to yield N-terminal fragments of approximately 30 kDa and C-terminal fragments of approximately 20 kDa. Following cleavage of the full-length protein, PS1 fragments stay together as a stable 1:1 heterodimer. Recently it was shown that PS1 binds members of the armadillo family of proteins including δand β-catenin and promotes processing and signaling of Notch1 receptor. Other studies suggest that PS1 functions in protein trafficking, neuroprotection, chromosome segregation, and processing of selected proteins including APP (for a comprehensive review and reference list of the cellular biology of PS1, see Ref.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Presenilin-1: A Component of Synaptic and Endothelial Adherens Junctions","attachmentId":46830108,"attachmentType":"pdf","work_url":"https://www.academia.edu/26536039/Presenilin_1_A_Component_of_Synaptic_and_Endothelial_Adherens_Junctions","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/26536039/Presenilin_1_A_Component_of_Synaptic_and_Endothelial_Adherens_Junctions"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="64646253" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/64646253/Lack_of_specific_association_of_presenilin_1_PS_1_protein_with_plaques_and_tangles_in_Alzheimers_disease">Lack of specific association of presenilin 1 (PS-1) protein with plaques and tangles in Alzheimer's disease</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="103612531" href="https://harvard.academia.edu/RudyTanzi">Rudy Tanzi</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of the Neurological Sciences, 1998</p><p class="ds-related-work--abstract ds2-5-body-sm">Missense mutations in the presenilin-1 (PS-1) gene are causally related to the majority of familial early-onset Alzheimer's disease (FAD). PS-1 immunohistochemical expression in normal human brain and in brains with Alzheimer's disease (AD) has so far been controversial. Here, we report a study of PS-1 expression in brains, cell lines and peripheral blood mononuclear cells using a panel of well characterized PS-1-specific antibodies. These antibodies were characterized by immunofluorescent staining of PS-1 transfectants followed by flow cytometric analysis. In human brain, widespread neuronal staining was observed. PS-1 immunoreactivity was primarily confined to neuronal cell bodies and proximal dendrites. Weaker staining of microglia was also detected, in accord with the finding of PS-1 immunoreactivity in monocytes. PS-1 expression is not particularly associated with neurons either containing or spared from neurofibrillary tangles, nor with senile plaques. The level of PS-1 expression does not differ between normal and AD brains. Immunoprecipitation from AD, FAD and control brains revealed only a 32 kDa N-terminal fragment and an 18-20 kDa C-terminal fragment. Little or no full length PS-1 was detected. The enriched presence of PS-1 in neurons implies an important role in neuronal function, however, the lack of apparent association of its expression with AD pathology signifies the need for a better understanding of its pathophysiological role.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Lack of specific association of presenilin 1 (PS-1) protein with plaques and tangles in Alzheimer's disease","attachmentId":76585144,"attachmentType":"pdf","work_url":"https://www.academia.edu/64646253/Lack_of_specific_association_of_presenilin_1_PS_1_protein_with_plaques_and_tangles_in_Alzheimers_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/64646253/Lack_of_specific_association_of_presenilin_1_PS_1_protein_with_plaques_and_tangles_in_Alzheimers_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="28970890" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/28970890/Interaction_between_amyloid_precursor_protein_and_presenilins_in_mammalian_cells_Implications_for_the_pathogenesis_of_Alzheimer_disease">Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="733194" href="https://ttuhsc.academia.edu/RuthPerez">Ruth Perez</a></div><p class="ds-related-work--abstract ds2-5-body-sm">Mutations in the presenilin 1 (PS1) and pre-senilin 2 (PS2) genes increase the production of the highly amyloidogenic 42-residue form of amyloid-protein (A 42) in a variety of cell lines and transgenic mice. To elucidate the molecular mechanism of this effect, wild-type (wt) or mutant PS1 and PS2 genes were stably transfected into Chinese hamster ovary cells expressing endogenous or transfected-amyloid precursor protein (APP). By immunoprecipita-tionWestern blot analysis, APP was consistently found to coimmunoprecipitate with PS1 or PS2 proteins. Several distinct PS1, PS2, or APP antibodies precipitated PS–APP complexes that were detectable by blotting with either APP or PS antibodies. Importantly, complex formation could be detected at endogenous protein levels in nontransfected cells. In various Chinese hamster ovary cell lines, the amounts of APP coprecipitated by PS antibodies were proportional to the expression levels of both APP and PS. APP–PS complexes also were recovered from human 293 and HS683 cells. Full mat-uration of APP was not required for the interaction; most APP molecules complexed with PS were solely N-glycosylated. Treatment of cells with brefeldin A or incubation at 20°C did not block complex formation, suggesting that the association between APP and PS occurs in part in the endoplasmic reticulum. Complex formation was detected for both wt and mutant PS and APP proteins. Deletion of the APP C-terminal domain did not abrogate complex formation, suggesting that the interaction does not occur in the cytoplasmic domains of the proteins. Our results demonstrate that wt and mutant PS1 and PS2 proteins form complexes with APP in living cells, strongly supporting the hypothesis that mutant PS interacts with APP in a way that enhances the intramembranous proteolysis of the latter by a-secretase cleaving at A 42 .</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease","attachmentId":49412176,"attachmentType":"pdf","work_url":"https://www.academia.edu/28970890/Interaction_between_amyloid_precursor_protein_and_presenilins_in_mammalian_cells_Implications_for_the_pathogenesis_of_Alzheimer_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/28970890/Interaction_between_amyloid_precursor_protein_and_presenilins_in_mammalian_cells_Implications_for_the_pathogenesis_of_Alzheimer_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="8764559" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/8764559/Presenilin_1_binds_cytoplasmic_epithelial_cadherin_inhibits_cadherin_p120_association_and_regulates_stability_and_function_of_the_cadherin_catenin_adhesion_complex">Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="18834357" href="https://independent.academia.edu/wencui">wen cui</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Proceedings of The National Academy of Sciences, 2001</p><p class="ds-related-work--abstract ds2-5-body-sm">Here we show that presenilin-1 (PS1), a protein involved in Alzheimer's disease, binds directly to epithelial cadherin (E-cadherin). This binding is mediated by the large cytoplasmic loop of PS1 and requires the membrane-proximal cytoplasmic sequence 604 -615 of mature E-cadherin. This sequence is also required for E-cadherin binding of protein p120, a known regulator of cadherin-mediated cell adhesion. Using wild-type and PS1 knockout cells, we found that increasing PS1 levels suppresses p120͞E-cadherin binding, and increasing p120 levels suppresses PS1͞E-cadherin binding. Thus PS1 and p120 bind to and mutually compete for cellular E-cadherin. Furthermore, PS1 stimulates E-cadherin binding to ␤and ␥-catenin, promotes cytoskeletal association of the cad-herin͞catenin complexes, and increases Ca 2؉ -dependent cell-cell aggregation. Remarkably, PS1 familial Alzheimer disease mutant ⌬E9 increased neither the levels of cadherin͞catenin complexes nor cell aggregation, suggesting that this familial Alzheimer disease mutation interferes with cadherin-based cell-cell adhesion. These data identify PS1 as an E-cadherin-binding protein and a regulator of E-cadherin function in vivo.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex","attachmentId":48010229,"attachmentType":"pdf","work_url":"https://www.academia.edu/8764559/Presenilin_1_binds_cytoplasmic_epithelial_cadherin_inhibits_cadherin_p120_association_and_regulates_stability_and_function_of_the_cadherin_catenin_adhesion_complex","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/8764559/Presenilin_1_binds_cytoplasmic_epithelial_cadherin_inhibits_cadherin_p120_association_and_regulates_stability_and_function_of_the_cadherin_catenin_adhesion_complex"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="123944230" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/123944230/Presenilin_1_expression_on_the_cell_surface_in_motile_polarized_cells">Presenilin 1 expression on the cell surface in motile polarized cells</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="101425838" href="https://independent.academia.edu/VitekMichael">Michael Vitek</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biophysics, 2006</p><p class="ds-related-work--abstract ds2-5-body-sm">Most cases of early-onset familial Alzheimer's disease are caused by mutations in the presenilin 1 gene. Nonetheless, the function of presenilin 1 are not yet completely understood. It was shown that endogenous presenilin 1, as well as the adhesion protein CD44, is concentrated on the surface of lamellipodia of polarized T cells (Jurkat cells) after adhesion to a collagen matrix. This phenomenon was not observed for another surface protein of T cells, T cell receptor, which is not involved in cell adhesion processes. In cultures of primary mouse cortical neurons, presenilin 1 was concentrated on the surface of the growth cone and at neurite contact sites. The concentration of presenilin 1 on the surface of structures that determine cell motility and intercellular contacts suggests that presenilin 1 plays an important role in cell adhesion in motile polarized cells.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Presenilin 1 expression on the cell surface in motile polarized cells","attachmentId":118262085,"attachmentType":"pdf","work_url":"https://www.academia.edu/123944230/Presenilin_1_expression_on_the_cell_surface_in_motile_polarized_cells","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/123944230/Presenilin_1_expression_on_the_cell_surface_in_motile_polarized_cells"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="17391762" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/17391762/Neuronal_localization_of_presenilin_1_and_association_with_amyloid_plaques_and_neurofibrillary_tangles_in_Alzheimers_disease">Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="37118796" href="https://boehringer-ingelheim.academia.edu/BerndSommer">Bernd Sommer</a></div><p class="ds-related-work--metadata ds2-5-body-xs">The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997</p><p class="ds-related-work--abstract ds2-5-body-sm">Mutations in the presenilin-1 (PS1) gene is a cause of early- onset familial Alzheimer&#39;s disease (AD). Endogenous PS1 is associated with the endoplasmic reticulum in the cell body of undifferentiated SH-SY5Y neuroblastoma cells. At early stages of neuronal differentiation in rat hippocampal culture, PS1 appears in all neuritic processes and in growth cones. In mature differentiated neurons, PS1 is concentrated in the somatodendritic compartment but is also present at lower levels in axons. A similar localization of PS1 is observed in vivo in neurons of the adult human cerebral cortex. In sporadic AD, PS1 appears in the dystrophic neurites of mature amyloid plaques and co-localizes with a subset of intraneuronal neurofibrillary tangles (NFTs). About 30% of hippocampal NFTs are labeled with a highly specific antibody to the PS1 C-terminal loop domain but not with an antibody to the PS1 N terminus. This observation is consistent with a potential association of the PS1 C-terminal fr...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease","attachmentId":39482720,"attachmentType":"pdf","work_url":"https://www.academia.edu/17391762/Neuronal_localization_of_presenilin_1_and_association_with_amyloid_plaques_and_neurofibrillary_tangles_in_Alzheimers_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/17391762/Neuronal_localization_of_presenilin_1_and_association_with_amyloid_plaques_and_neurofibrillary_tangles_in_Alzheimers_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="30529691" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/30529691/Alzheimer_s_disease_presenilin_1_expression_modulates_the_assembly_of_neurofilaments">Alzheimer’s disease presenilin-1 expression modulates the assembly of neurofilaments</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="58189284" href="https://independent.academia.edu/WieslawDowjat">Wieslaw Dowjat</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Neuroscience, 2001</p><p class="ds-related-work--abstract ds2-5-body-sm">AbstractÐMutations in presenilin-1 gene are responsible for the majority of early-onset familial Alzheimer's disease cases. The function of this protein and the mechanism underlying the pathogenicity of its mutations are still unclear. To elucidate the role of presenilin-1 in the Alzheimer's disease pathology, we tested two such mutations (P117L and M146L) for their effect in stably transfected mouse neuroblastoma cell lines. Over-expression of the wild-type presenilin-1 gene induced formation of a well-extended, orderly organized network consisting of neuro®laments assembled from the L and H subunits, while in cells with the mutant gene this network was markedly reduced to short ®laments concentrated in structures resembling cups. Cells expressing the mutant gene displayed altered processing of the transgene protein and neuro®lament-H, suggesting that presenilin-1 is the mediator of changes targeted at neuro®laments. The two different mutations produced similar alterations, implying that this is a common pathogenic mechanism. Presenilin-1, neuro®lament-H and tau proteins showed co-localization as evidenced by confocal microscopy, suggesting a possible physiological connection between these three proteins.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Alzheimer’s disease presenilin-1 expression modulates the assembly of neurofilaments","attachmentId":50972891,"attachmentType":"pdf","work_url":"https://www.academia.edu/30529691/Alzheimer_s_disease_presenilin_1_expression_modulates_the_assembly_of_neurofilaments","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/30529691/Alzheimer_s_disease_presenilin_1_expression_modulates_the_assembly_of_neurofilaments"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="102430209" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/102430209/Altered_binding_of_mutated_presenilin_with_cytoskeleton_interacting_proteins">Altered binding of mutated presenilin with cytoskeleton-interacting proteins</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="38210458" href="https://independent.academia.edu/LeszekKotula">Leszek Kotula</a></div><p class="ds-related-work--metadata ds2-5-body-xs">FEBS Letters, 1999</p><p class="ds-related-work--abstract ds2-5-body-sm">The majority of familial Alzheimer's disease (AD) cases are linked to mutations on presenilin 1 and 2 genes (PS1 and PS2). The normal function of the proteins and the mechanisms underlying early-onset AD are currently unknown. To address this, we screened an expression library for proteins that bind differentially to the wild-type PS1 and mutant in the large cytoplasmic loop (PS1L). Thus we isolated the C-terminal tail of the 170 kDa cytoplasmic linker protein (CLIP-170) and Reed^Sternberg cells of Hodgkin's disease-expressed intermediate filament-associated protein (Restin), cytoplasmic proteins linking vesicles to the cytoskeleton. PS1L binding to CLIP-170/ restin requires Ca 2+. Treating cells with thapsigargin or ionomycin increased the mutated PS1 in CLIP-170 immunoprecipitates. Further, PS1 and CLIP-170 co-localize in transfected cells and neuronal cultures.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Altered binding of mutated presenilin with cytoskeleton-interacting proteins","attachmentId":102703367,"attachmentType":"pdf","work_url":"https://www.academia.edu/102430209/Altered_binding_of_mutated_presenilin_with_cytoskeleton_interacting_proteins","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/102430209/Altered_binding_of_mutated_presenilin_with_cytoskeleton_interacting_proteins"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":43993901,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":43993901,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_43993901" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. You can download the paper by clicking the button above.</p></div></div></div></div><div class="ds-sidebar--container js-work-sidebar"><div class="ds-related-content--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="0" data-entity-id="78116120" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/78116120/Carboxyl_Terminal_Fragments_of_Presenilin_1_Are_Closely_Related_to_Cytoskeletal_Abnormalities_in_Alzheimers_Brains">Carboxyl-Terminal Fragments of Presenilin-1 Are Closely Related to Cytoskeletal Abnormalities in Alzheimer's Brains</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="222368011" href="https://independent.academia.edu/MitsuyasuKanai">Mitsuyasu Kanai</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochemical and Biophysical Research Communications, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Carboxyl-Terminal Fragments of Presenilin-1 Are Closely Related to Cytoskeletal Abnormalities in Alzheimer's Brains","attachmentId":85276487,"attachmentType":"pdf","work_url":"https://www.academia.edu/78116120/Carboxyl_Terminal_Fragments_of_Presenilin_1_Are_Closely_Related_to_Cytoskeletal_Abnormalities_in_Alzheimers_Brains","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/78116120/Carboxyl_Terminal_Fragments_of_Presenilin_1_Are_Closely_Related_to_Cytoskeletal_Abnormalities_in_Alzheimers_Brains"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="1" data-entity-id="30529692" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/30529692/Inhibition_of_neurite_outgrowth_by_familial_Alzheimers_disease_linked_presenilin_1_mutations">Inhibition of neurite outgrowth by familial Alzheimer's disease-linked presenilin-1 mutations</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="58189284" href="https://independent.academia.edu/WieslawDowjat">Wieslaw Dowjat</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Neuroscience Letters, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Inhibition of neurite outgrowth by familial Alzheimer's disease-linked presenilin-1 mutations","attachmentId":50972889,"attachmentType":"pdf","work_url":"https://www.academia.edu/30529692/Inhibition_of_neurite_outgrowth_by_familial_Alzheimers_disease_linked_presenilin_1_mutations","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/30529692/Inhibition_of_neurite_outgrowth_by_familial_Alzheimers_disease_linked_presenilin_1_mutations"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="2" data-entity-id="52348563" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/52348563/Cell_adhesion_molecules_in_Alzheimer_and_39_s_disease">Cell adhesion molecules in Alzheimer&#39;s disease</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="113446450" href="https://su-se.academia.edu/HenriettaNielsen">Henrietta Nielsen</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Degenerative Neurological and Neuromuscular Disease, 2012</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Cell adhesion molecules in Alzheimer\u0026#39;s disease","attachmentId":69654569,"attachmentType":"pdf","work_url":"https://www.academia.edu/52348563/Cell_adhesion_molecules_in_Alzheimer_and_39_s_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/52348563/Cell_adhesion_molecules_in_Alzheimer_and_39_s_disease"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="3" data-entity-id="8764558" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/8764558/Presenilin_1_Forms_Complexes_with_the_Cadherin_Catenin_Cell_Cell_Adhesion_System_and_Is_Recruited_to_Intercellular_and_Synaptic_Contacts">Presenilin-1 Forms Complexes with the Cadherin/Catenin Cell–Cell Adhesion System and Is Recruited to Intercellular and Synaptic Contacts</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="18834357" href="https://independent.academia.edu/wencui">wen cui</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular Cell, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Presenilin-1 Forms Complexes with the Cadherin/Catenin Cell–Cell Adhesion System and Is Recruited to Intercellular and Synaptic Contacts","attachmentId":48010217,"attachmentType":"pdf","work_url":"https://www.academia.edu/8764558/Presenilin_1_Forms_Complexes_with_the_Cadherin_Catenin_Cell_Cell_Adhesion_System_and_Is_Recruited_to_Intercellular_and_Synaptic_Contacts","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/8764558/Presenilin_1_Forms_Complexes_with_the_Cadherin_Catenin_Cell_Cell_Adhesion_System_and_Is_Recruited_to_Intercellular_and_Synaptic_Contacts"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="4" data-entity-id="17226694" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/17226694/Immunohistochemical_analysis_of_presenilin_2_expression_in_the_mouse_brain_distribution_pattern_and_co_localization_with_presenilin_1_protein">Immunohistochemical analysis of presenilin 2 expression in the mouse brain: distribution pattern and co-localization with presenilin 1 protein</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="36835689" href="https://independent.academia.edu/LaurentPradier">Laurent Pradier</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Brain Research, 1997</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Immunohistochemical analysis of presenilin 2 expression in the mouse brain: distribution pattern and co-localization with presenilin 1 protein","attachmentId":42290252,"attachmentType":"pdf","work_url":"https://www.academia.edu/17226694/Immunohistochemical_analysis_of_presenilin_2_expression_in_the_mouse_brain_distribution_pattern_and_co_localization_with_presenilin_1_protein","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/17226694/Immunohistochemical_analysis_of_presenilin_2_expression_in_the_mouse_brain_distribution_pattern_and_co_localization_with_presenilin_1_protein"><span 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data-collection-position="6" data-entity-id="20610220" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/20610220/Presenilin_1_facilitates_the_constitutive_turnover_of_beta_catenin_differential_activity_of_Alzheimers_disease_linked_PS1_mutants_in_the_beta_catenin_signaling_pathway">Presenilin 1 facilitates the constitutive turnover of beta-catenin: differential activity of Alzheimer's disease-linked PS1 mutants in the beta-catenin-signaling pathway</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="41946641" href="https://independent.academia.edu/EdwardKo">Edward Ko</a></div><p class="ds-related-work--metadata ds2-5-body-xs">The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline 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Tanzi</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Proceedings of the …, 1997</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Evidence for phosphorylation and oligomeric assembly of presenilin 1","attachmentId":76585016,"attachmentType":"pdf","work_url":"https://www.academia.edu/64646189/Evidence_for_phosphorylation_and_oligomeric_assembly_of_presenilin_1","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/64646189/Evidence_for_phosphorylation_and_oligomeric_assembly_of_presenilin_1"><span class="ds2-5-text-link__content">View PDF</span><span 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class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix","attachmentId":43897752,"attachmentType":"pdf","work_url":"https://www.academia.edu/23459076/Endogenous_presenilin_1_redistributes_to_the_surface_of_lamellipodia_upon_adhesion_of_Jurkat_cells_to_a_collagen_matrix","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/23459076/Endogenous_presenilin_1_redistributes_to_the_surface_of_lamellipodia_upon_adhesion_of_Jurkat_cells_to_a_collagen_matrix"><span 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Psychiatry and Clinical …, 1999</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The Biological and Pathological Function of Presenilin Proteinssimple Cell Systems and a Worm In Alzheimer's Disease Research","attachmentId":51270715,"attachmentType":"pdf","work_url":"https://www.academia.edu/724912/The_Biological_and_Pathological_Function_of_Presenilin_Proteins_simple_Cell_Systems_and_a_Worm_In_Alzheimers_Disease_Research","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/724912/The_Biological_and_Pathological_Function_of_Presenilin_Proteins_simple_Cell_Systems_and_a_Worm_In_Alzheimers_Disease_Research"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="10" data-entity-id="24893951" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/24893951/Proteolytic_Fragments_of_Alzheimer_s_Disease_Associated_Presenilin_1_Are_Present_in_Synaptic_Organelles_and_Growth_Cone_Membranes_of_Rat_Brain">Proteolytic Fragments of Alzheimer’s Disease-Associated Presenilin 1 Are Present in Synaptic Organelles and Growth Cone Membranes of Rat Brain</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="39659278" href="https://independent.academia.edu/ColinMasters">Colin Masters</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Neurochemistry, 2001</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Proteolytic Fragments of Alzheimer’s Disease-Associated Presenilin 1 Are Present in Synaptic Organelles and Growth Cone Membranes of Rat Brain","attachmentId":45214176,"attachmentType":"pdf","work_url":"https://www.academia.edu/24893951/Proteolytic_Fragments_of_Alzheimer_s_Disease_Associated_Presenilin_1_Are_Present_in_Synaptic_Organelles_and_Growth_Cone_Membranes_of_Rat_Brain","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a 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href="https://independent.academia.edu/JavierSaezValero">Javier Sáez-Valero</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Acta Neuropathologica Communications, 2013</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"CSF Presenilin-1 complexes are increased in Alzheimer’s disease","attachmentId":115658152,"attachmentType":"pdf","work_url":"https://www.academia.edu/120542930/CSF_Presenilin_1_complexes_are_increased_in_Alzheimer_s_disease","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/120542930/CSF_Presenilin_1_complexes_are_increased_in_Alzheimer_s_disease"><span 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2004</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Presenilin 1 and Cadherins: Stabilization of Cell-Cell Adhesion and Proteolysis-Dependent Regulation of Transcription","attachmentId":79754243,"attachmentType":"pdf","work_url":"https://www.academia.edu/69796053/Presenilin_1_and_Cadherins_Stabilization_of_Cell_Cell_Adhesion_and_Proteolysis_Dependent_Regulation_of_Transcription","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-related-work-grid-card-view-pdf" href="https://www.academia.edu/69796053/Presenilin_1_and_Cadherins_Stabilization_of_Cell_Cell_Adhesion_and_Proteolysis_Dependent_Regulation_of_Transcription"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="13" data-entity-id="84348977" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/84348977/Carboxyl_terminal_Fragments_of_Alzheimer_%CE%B2_Amyloid_Precursor_Protein_Accumulate_in_Restricted_and_Unpredicted_Intracellular_Compartments_in_Presenilin_1_deficient_Cells">Carboxyl-terminal Fragments of Alzheimer β-Amyloid Precursor Protein Accumulate in Restricted and Unpredicted Intracellular Compartments in Presenilin 1-deficient Cells</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="33473615" href="https://utoronto.academia.edu/HowardMount">Howard Mount</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 2000</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Carboxyl-terminal Fragments of Alzheimer β-Amyloid Precursor Protein Accumulate in Restricted and Unpredicted Intracellular Compartments in Presenilin 1-deficient Cells","attachmentId":89403159,"attachmentType":"pdf","work_url":"https://www.academia.edu/84348977/Carboxyl_terminal_Fragments_of_Alzheimer_%CE%B2_Amyloid_Precursor_Protein_Accumulate_in_Restricted_and_Unpredicted_Intracellular_Compartments_in_Presenilin_1_deficient_Cells","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline 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