| pubmed-article:1692034 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0032176 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0055023 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:1692034 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1692034 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1692034 | pubmed:dateCreated | 1990-6-6 | lld:pubmed |
| pubmed-article:1692034 | pubmed:abstractText | Vitronectin (Vn) is a multifunctional 75-kD glycoprotein that is present in plasma and the extracellular matrix. Vn functions as a complement regulatory protein in plasma, and promotes the growth and attachment of cells in tissue culture. Recent cDNA cloning reveals that like other adhesive proteins, Vn contains the sequence Arg-Gly-Asp and binds to some members of the integrin class of adhesive membrane receptors. In liposomes, the platelet membrane glycoprotein complex IIb/IIIa binds Vn, as well as fibrinogen, von Willebrand factor, and fibronectin. We examined the binding of purified Vn to resting and stimulated human platelets. Vn bound to thrombin-stimulated platelets in a calcium-dependent, specific, and saturable manner with a Kd of 320 nM and 8,000 sites per platelet. Epinephrine or ADP stimulation led to specific binding with KdS of 93 and 116 nM, respectively. Binding was inhibited by the tetrapeptide Arg-Gly-Asp-Ser and by monoclonal and polyclonal antibodies to GPIIb/IIIa. Endogenous platelet Vn stores were identified in immunoblots of gel-filtered platelets and the surface expression of endogenous platelet Vn was thrombin inducible. Monoclonal as well as polyclonal antibodies to Vn inhibited platelet aggregation, suggesting that Vn plays a role in the formation of stable platelet aggregates. | lld:pubmed |
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| pubmed-article:1692034 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1692034 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1692034 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:1692034 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1692034 | pubmed:month | May | lld:pubmed |
| pubmed-article:1692034 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:1692034 | pubmed:author | pubmed-author:PodackEE | lld:pubmed |
| pubmed-article:1692034 | pubmed:author | pubmed-author:AschEE | lld:pubmed |
| pubmed-article:1692034 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1692034 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:1692034 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1692034 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1692034 | pubmed:pagination | 1372-8 | lld:pubmed |
| pubmed-article:1692034 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1692034 | pubmed:meshHeading | pubmed-meshheading:1692034-... | lld:pubmed |
| pubmed-article:1692034 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1692034 | pubmed:articleTitle | Vitronectin binds to activated human platelets and plays a role in platelet aggregation. | lld:pubmed |
