Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18177
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dc.contributor.authorKouklis, P.en
dc.contributor.authorKonstantoulaki, M.en
dc.contributor.authorMalik, A. B.en
dc.date.accessioned2015-11-24T18:50:55Z-
dc.date.available2015-11-24T18:50:55Z-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18177-
dc.rightsDefault Licence-
dc.subjectAntigens, CDen
dc.subjectCadherins/*physiologyen
dc.subjectCateninsen
dc.subjectCell Adhesion Molecules/physiologyen
dc.subjectCell Membrane/*metabolismen
dc.subjectCells, Cultureden
dc.subjectCytoskeletal Proteins/physiologyen
dc.subjectEndothelium, Vascular/*cytology/ultrastructureen
dc.subjectHumansen
dc.subjectPhosphoproteins/physiologyen
dc.subjectTrans-Activators/physiologyen
dc.subjectbeta Cateninen
dc.subjectcdc42 GTP-Binding Protein/*physiologyen
dc.titleVE-cadherin-induced Cdc42 signaling regulates formation of membrane protrusions in endothelial cellsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1074/jbc.M212591200-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/12595527-
heal.identifier.secondaryhttp://www.jbc.org/content/278/18/16230.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2003-
heal.abstractThe cytoplasmic domain of cadherins and the associated catenins link the cytoskeleton with signal transduction pathways. To study the signaling function of non-junctional VE-cadherin, which can form during the loss VE-cadherin homotypic adhesion, wild type VE-cadherin or VE-cadherin cytoplasmic domain (DeltaEXD) was expressed in sub-confluent endothelial cells. We observed that Cdc42 was activated in transfected cells and that these cells also developed Cdc42-dependent >70-microm-long plasma membrane protrusions. The formation of these structures required actin polymerization, and they developed specifically in endothelial cells as compared with epithelial cells. Expression of the VE-cadherin cytoplasmic domain lacking the beta-catenin binding site also induced Cdc42 activation; thus, its activation cannot be ascribed to beta-catenin binding. However, these cells were not able to form the protrusions. These results suggest that the cytoplasmic domain of non-junctional VE-cadherin can serve as a scaffold involved in Cdc42 activation at the endothelial plasma membrane. beta-Catenin and the associated alpha-catenin may serve as support sites for actin polymerization, leading to formation of long plasma membrane protrusions. Thus, non-junctional VE-cadherin actively participates in inside-out signaling at the plasma membrane, leading to the development of endothelial membrane protrusions.en
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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