Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1994-4-4
|
| pubmed:abstractText |
The integrin alpha v beta 6 has been shown to be a fibronectin-binding protein. To determine whether the cytoplasmic and transmembrane domains of alpha v beta 6 are necessary for binding to fibronectin, a truncated, secreted form of the integrin lacking these domains was engineered and expressed in Chinese hamster ovary cells. Fibronectin affinity chromatography demonstrated that the secreted integrin, like its full-length counterpart, was capable of binding fibronectin. Monoclonal antibodies were made to secreted alpha v beta 6 and to beta 6-transfected NIH 3T3 cells. In experiments designed to determine whether alpha v beta 6 can mediate cell attachment to fibronectin, full-length human beta 6 was expressed in Chinese hamster ovary cells and in the human colon carcinoma cell line SW480. beta 6-expressing cells were identified by alpha v beta 6-specific antibodies, and the beta 6-transfectants were used in cell-adhesion assays. In Chinese hamster ovary cells, human beta 6 associated with hamster alpha v but was incapable of mediating cell attachment to fibronectin. However, expression of beta 6 in these cells had the dominant negative effect of decreasing alpha v beta 5-dependent adhesion to vitronectin. In SW480 cells, beta 6 expression conferred the ability to bind to fibronectin even in the presence of inhibitory antibodies against beta 1 integrins. In such cells, fibronectin binding ability could be blocked by an antibody to alpha v integrins. These results constitute the first direct evidence that alpha v beta 6 mediates cell attachment to fibronectin.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/integrin alphavbeta6
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
4
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6940-8
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8120056-3T3 Cells,
pubmed-meshheading:8120056-Animals,
pubmed-meshheading:8120056-Antibodies, Monoclonal,
pubmed-meshheading:8120056-Antigens, Neoplasm,
pubmed-meshheading:8120056-CHO Cells,
pubmed-meshheading:8120056-Cell Adhesion,
pubmed-meshheading:8120056-Cell Line,
pubmed-meshheading:8120056-Chromatography, Affinity,
pubmed-meshheading:8120056-Cricetinae,
pubmed-meshheading:8120056-Fibronectins,
pubmed-meshheading:8120056-Flow Cytometry,
pubmed-meshheading:8120056-Gene Expression,
pubmed-meshheading:8120056-HeLa Cells,
pubmed-meshheading:8120056-Humans,
pubmed-meshheading:8120056-Integrins,
pubmed-meshheading:8120056-Mice,
pubmed-meshheading:8120056-Mice, Inbred BALB C,
pubmed-meshheading:8120056-Molecular Weight,
pubmed-meshheading:8120056-Plasmids,
pubmed-meshheading:8120056-Recombinant Proteins,
pubmed-meshheading:8120056-Transfection
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Role of the integrin alpha v beta 6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor.
|
| pubmed:affiliation |
Lung Biology Center, University of California, San Francisco 94143.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|