Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-6-6
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-1169259, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2409614, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2411420, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2414098, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2415521, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2420006, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2426279, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2433863, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2435757, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2437107, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2442758, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2449435, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2465293, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2478219, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2581612, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2582413, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2582428, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2833328, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-2848850, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-3004934, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-3028640, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-3754869, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-3875376, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-4008487, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-410885, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-4205973, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-447655, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-4936093, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-574143, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6191326, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6236859, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6266278, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6270087, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6282932, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6302680, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6308050, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6309863, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6325435, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-637870, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6384783, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6497883, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6501568, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6630199, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-6767512, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-7403340, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-7470616, http://linkedlifedata.com/resource/pubmed/commentcorrection/1692034-874364
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9738
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1372-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Vitronectin binds to activated human platelets and plays a role in platelet aggregation.
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