| pubmed-article:8376355 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C0220248 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1332713 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:8376355 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:8376355 | pubmed:issue | 27 | lld:pubmed |
| pubmed-article:8376355 | pubmed:dateCreated | 1993-10-20 | lld:pubmed |
| pubmed-article:8376355 | 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. | lld:pubmed |
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| pubmed-article:8376355 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8376355 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8376355 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8376355 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8376355 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8376355 | pubmed:author | pubmed-author:SchwartzM AMA | lld:pubmed |
| pubmed-article:8376355 | pubmed:author | pubmed-author:BrownE JEJ | lld:pubmed |
| pubmed-article:8376355 | pubmed:author | pubmed-author:FazeliBB | lld:pubmed |
| pubmed-article:8376355 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8376355 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8376355 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8376355 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8376355 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8376355 | pubmed:pagination | 19931-4 | lld:pubmed |
| pubmed-article:8376355 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8376355 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8376355 | pubmed:articleTitle | A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. | lld:pubmed |
| pubmed-article:8376355 | pubmed:affiliation | Committee on Vascular Biology, Scripps Research Institute, La Jolla, California 92037. | lld:pubmed |
| pubmed-article:8376355 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8376355 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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