| pubmed-article:9585425 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9585425 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:9585425 | lifeskim:mentions | umls-concept:C0007620 | lld:lifeskim |
| pubmed-article:9585425 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:9585425 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:9585425 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9585425 | pubmed:dateCreated | 1998-6-17 | lld:pubmed |
| pubmed-article:9585425 | pubmed:abstractText | The alphavbeta3 integrin plays a fundamental role during the angiogenesis process by inhibiting endothelial cell apoptosis. However, the mechanism of inhibition is unknown. In this report, we show that integrin-mediated cell survival involves regulation of nuclear factor-kappa B (NF-kappaB) activity. Different extracellular matrix molecules were able to protect rat aorta- derived endothelial cells from apoptosis induced by serum withdrawal. Osteopontin and beta3 integrin ligation rapidly increased NF-kappaB activity as measured by gel shift and reporter activity. The p65 and p50 subunits were present in the shifted complex. In contrast, collagen type I (a beta1-integrin ligand) did not induce NF-kappaB activity. The alphavbeta3 integrin was most important for osteopontin-mediated NF-kappaB induction and survival, since adding a neutralizing anti-beta3 integrin antibody blocked NF-kappaB activity and induced endothelial cell death when cells were plated on osteopontin. NF-kappaB was required for osteopontin- and vitronectin-induced survival since inhibition of NF-kappaB activity with nonphosphorylatable IkappaB completely blocked the protective effect of osteopontin and vitronectin. In contrast, NF-kappaB was not required for fibronectin, laminin, and collagen type I-induced survival. Activation of NF-kappaB by osteopontin depended on the small GTP-binding protein Ras and the tyrosine kinase Src, since NF-kappaB reporter activity was inhibited by Ras and Src dominant-negative mutants. In contrast, inhibition of MEK and PI3-kinase did not affect osteopontin-induced NF-kappaB activation. These studies identify NF-kappaB as an important signaling molecule in alphavbeta3 integrin-mediated endothelial cell survival. | lld:pubmed |
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| pubmed-article:9585425 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9585425 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9585425 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9585425 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9585425 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9585425 | pubmed:month | May | lld:pubmed |
| pubmed-article:9585425 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:9585425 | pubmed:author | pubmed-author:FaustoNN | lld:pubmed |
| pubmed-article:9585425 | pubmed:author | pubmed-author:AlmeidaMM | lld:pubmed |
| pubmed-article:9585425 | pubmed:author | pubmed-author:ScatenaMM | lld:pubmed |
| pubmed-article:9585425 | pubmed:author | pubmed-author:NicosiaR FRF | lld:pubmed |
| pubmed-article:9585425 | pubmed:author | pubmed-author:GiachelliC... | lld:pubmed |
