Source:http://linkedlifedata.com/resource/pubmed/id/15550395
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2005-2-7
|
| pubmed:abstractText |
Nectins are Ca2+-independent cell adhesion molecules found at cadherin-based adherens junctions. We used a dual pipette assay that measures the forces required to separate cell doublets to determine how nectins affect the formation and strength of cell-cell adhesion. Less force was required to separate doublets of L cells expressing nectin-1 or nectin-3 than to separate doublets of E-cadherin-expressing cells. Heterodimers formed between cells expressing nectin-1 or nectin-3 adhered more strongly than homodimers. Nectin-3 that does not trans-interact with nectin-1 inhibited E-cadherin-mediated adhesion. However, the extracellular fragment of nectin-1 did not have an agonistic effect on E-cadherin-dependent cell adhesion when it trans-interacted with nectin-3, expressed at high levels in cells. In contrast, the extracellular fragment of nectin-3 had a significant agonistic effect on cadherin-based adhesion when it interacted with endogenous nectin-1, expressed at low levels in cells. Our results indicate that E-cadherin is the key molecule involved in cell adhesion and that the regulation of E-cadherin-based adhesion involving cellular nectin-1 trans-interacting with nectin-3 is qualitatively different from that involving cellular nectin-3 trans-interacting with nectin-1 and depends on the nectin levels expressed by cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
11
|
| pubmed:volume |
280
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4753-60
|
| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15550395-Animals,
pubmed-meshheading:15550395-Blotting, Western,
pubmed-meshheading:15550395-Cadherins,
pubmed-meshheading:15550395-Calcium,
pubmed-meshheading:15550395-Cell Adhesion,
pubmed-meshheading:15550395-Cell Adhesion Molecules,
pubmed-meshheading:15550395-Cell Line,
pubmed-meshheading:15550395-Cytoplasm,
pubmed-meshheading:15550395-Dimerization,
pubmed-meshheading:15550395-Dose-Response Relationship, Drug,
pubmed-meshheading:15550395-Fibroblasts,
pubmed-meshheading:15550395-Humans,
pubmed-meshheading:15550395-Mice,
pubmed-meshheading:15550395-Models, Biological,
pubmed-meshheading:15550395-Protein Binding,
pubmed-meshheading:15550395-Protein Structure, Tertiary,
pubmed-meshheading:15550395-Rats,
pubmed-meshheading:15550395-Time Factors
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Separation force measurements reveal different types of modulation of E-cadherin-based adhesion by nectin-1 and -3.
|
| pubmed:affiliation |
UMR 144 CNRS-Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|