Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
|
pubmed:dateCreated |
1990-5-10
|
pubmed:abstractText |
We describe a novel integrin heterodimer on the surface of the human embryonic kidney cell line 293. This receptor is comprised of alpha v and beta 1 subunits, each of which has been previously found in association with other integrin subunits. This alpha v.beta 1 complex was identified as the predominant vitronectin receptor (VnR) on the surface of 293 cells by immunoprecipitation with antibodies raised against the alpha v subunit. Polymerase chain reaction analysis detected mRNAs for alpha v and beta 1 subunits while no evidence was obtained for beta 2, beta 3, or alpha IIb integrin subunit mRNA. Immunoprecipitation of surface-iodinated proteins with antibodies to alpha v gave bands of 150 and 120 kDa. The 120-kDa band reacted with antibodies to beta 1 in immunoblotting experiments. 293 cells adhere to vitronectin, fibronectin, laminin, and collagen IV, while von Willebrand factor and fibrinogen, known ligands of the VnR (alpha v.beta 3), did not support adhesion. A polyclonal antibody directed against both subunits of the VnR (alpha v, beta 3) inhibits attachment of 293 cells to vitronectin but not to other adhesive proteins. A beta 1-specific monoclonal inhibited attachment to fibronectin, laminin, and collagen IV, known ligands of beta 1 integrins, as well as vitronectin. This novel (alpha v. beta 1) VnR thus appears to mediate cell adhesion exclusively to vitronectin, in contrast to previously described VnRs which have multiple ligands.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vitronectin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
265
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5938-41
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1690718-Antibodies,
pubmed-meshheading:1690718-Antigen-Antibody Complex,
pubmed-meshheading:1690718-Cell Adhesion,
pubmed-meshheading:1690718-Cell Line,
pubmed-meshheading:1690718-Embryo, Mammalian,
pubmed-meshheading:1690718-Extracellular Matrix,
pubmed-meshheading:1690718-Fibronectins,
pubmed-meshheading:1690718-Humans,
pubmed-meshheading:1690718-Integrins,
pubmed-meshheading:1690718-Kidney,
pubmed-meshheading:1690718-Macromolecular Substances,
pubmed-meshheading:1690718-Molecular Weight,
pubmed-meshheading:1690718-Polymerase Chain Reaction,
pubmed-meshheading:1690718-RNA, Messenger,
pubmed-meshheading:1690718-Receptors, Fibronectin,
pubmed-meshheading:1690718-Receptors, Immunologic,
pubmed-meshheading:1690718-Receptors, Vitronectin
|
pubmed:year |
1990
|
pubmed:articleTitle |
The integrin beta 1 subunit associates with the vitronectin receptor alpha v subunit to form a novel vitronectin receptor in a human embryonic kidney cell line.
|
pubmed:affiliation |
Department of Biomolecular Chemistry, Genentech, Inc., South San Francisco, California 94080.
|
pubmed:publicationType |
Journal Article
|