| pubmed-article:18343874 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18343874 | lifeskim:mentions | umls-concept:C0300423 | lld:lifeskim |
| pubmed-article:18343874 | lifeskim:mentions | umls-concept:C0021721 | lld:lifeskim |
| pubmed-article:18343874 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:18343874 | lifeskim:mentions | umls-concept:C1332729 | lld:lifeskim |
| pubmed-article:18343874 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:18343874 | pubmed:dateCreated | 2008-6-27 | lld:pubmed |
| pubmed-article:18343874 | pubmed:abstractText | Specifically expressed at intercellular adherens junctions of endothelial cells, VE-cadherin is a receptor that exhibits particular self-association properties. Indeed, in vitro studies demonstrated that the extracellular part of VE-cadherin elaborates Ca(++)-dependent hexameric structures. We hypothesized that this assembly could be at the basis of a new cadherin-mediated cell-cell adhesion mechanism. To verify this assumption, we first demonstrated that VE-cadherin can elaborate hexamers at the cell surface of confluent endothelial cells. Second, mutations were introduced within the extracellular part of VE-cadherin to destabilize the hexamer. Following an in vitro screening, three mutants were selected, among which, one is able to elaborate only dimers. The selected mutations were expressed as C-terminal green fluorescent protein fusions in CHO cells. Despite their capacity to elaborate nascent cell-cell contacts, the mutants seem to be rapidly degraded and/or internalized. Altogether, our results suggest that the formation of VE-cadherin hexamers protects this receptor and might allow the elaboration of mature endothelial cell-cell junctions. | lld:pubmed |
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| pubmed-article:18343874 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18343874 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18343874 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18343874 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18343874 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:18343874 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:VernetThierry... | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:BibertStéphan... | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:ConcordEvelyn... | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:HermantBastie... | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:RivelineDanie... | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:AyariHélèneH | lld:pubmed |
| pubmed-article:18343874 | pubmed:author | pubmed-author:Gulino-Debrac... | lld:pubmed |
| pubmed-article:18343874 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18343874 | pubmed:volume | 143 | lld:pubmed |
| pubmed-article:18343874 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18343874 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18343874 | pubmed:pagination | 821-32 | lld:pubmed |
| pubmed-article:18343874 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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| pubmed-article:18343874 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18343874 | pubmed:articleTitle | Establishment of cell-cell junctions depends on the oligomeric states of VE-cadherin. | lld:pubmed |
| pubmed-article:18343874 | pubmed:affiliation | Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, (CEA/CNRS, UJF), 41 rue Jules Horowitz, 38027 Grenoble Cedex, France. Stephanie.Bibert@unil.ch | lld:pubmed |
| pubmed-article:18343874 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18343874 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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