pubmed-article:15064358 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0007620 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0538161 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0333516 | lld:lifeskim |
pubmed-article:15064358 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:15064358 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:15064358 | pubmed:dateCreated | 2004-5-27 | lld:pubmed |
pubmed-article:15064358 | pubmed:abstractText | Endothelial cell survival and antiapoptotic pathways, including those stimulated by extracellular matrix, are critical regulators of vasculogenesis, angiogenesis, endothelial repair, and shear-stress-induced endothelial activation. One of these pathways is mediated by alpha(v)beta(3) integrin ligation, downstream activation of nuclear factor-kappaB, and subsequent up-regulation of osteoprotegerin (OPG). In this study, the mechanism by which OPG protects endothelial cells from death was examined. Serum-starved human microvascular endothelial cells (HMECs) plated on the alpha(v)beta(3) ligand osteopontin were protected from cell death. Immunoprecipitation experiments indicated that OPG formed a complex with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) in HMECs under these conditions. Furthermore, inhibitors of TRAIL, including recombinant soluble TRAIL receptors and a neutralizing antibody against TRAIL, blocked apoptosis of serum-starved HMECs plated on the nonintegrin attachment factor poly-d-lysine. Whereas TRAIL was unable to induce apoptosis in HMECs plated on osteopontin, the addition of recombinant TRAIL did increase the percentage of apoptotic HMECs plated on poly-d-lysine. This evidence indicates that OPG blocks endothelial cell apoptosis through binding TRAIL and preventing its interaction with death-inducing TRAIL-receptors | lld:pubmed |
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pubmed-article:15064358 | pubmed:language | eng | lld:pubmed |
pubmed-article:15064358 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15064358 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15064358 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15064358 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15064358 | pubmed:month | Jun | lld:pubmed |
pubmed-article:15064358 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:15064358 | pubmed:author | pubmed-author:ScatenaMM | lld:pubmed |
pubmed-article:15064358 | pubmed:author | pubmed-author:GiachelliC... | lld:pubmed |
pubmed-article:15064358 | pubmed:author | pubmed-author:PritzkerL BLB | lld:pubmed |
pubmed-article:15064358 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15064358 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:15064358 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15064358 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15064358 | pubmed:pagination | 2834-41 | lld:pubmed |