Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1993-10-20
pubmed:abstractText
A 50-kDa integrin-associated protein (IAP), identified by its role in activation of neutrophils by extracellular matrix proteins, has recently been found to have a primary sequence that predicts five transmembrane domains, raising the possibility that the protein participates in ion transport. In endothelial cells, extracellular matrix proteins and anti-integrin antibodies have been shown to trigger an influx of [Ca2+]i via voltage-independent membrane channels. We now show that monoclonal antibodies to IAP that block neutrophil activation completely inhibited the fibronectin-stimulated rise in [Ca2+]i in endothelial cells. An antibody that binds IAP but does not block neutrophil function had no effect on endothelial cell [Ca2+]i. Inhibition of IAP function had no effect on endothelial cell adhesion, no effect on the integrin-mediated rise in intracellular pH, and no effect on the integrin-mediated increase in tyrosine phosphorylation. In addition, inhibition of IAP had no effect on the influx of Ca2+ triggered by histamine. These results demonstrate that IAP is specifically required for the integrin-regulated calcium influx and suggest that IAP itself might be an integrin-associated calcium channel.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19931-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells.
pubmed:affiliation
Committee on Vascular Biology, Scripps Research Institute, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.