| pubmed-article:2465293 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C1138427 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C0445223 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C1552599 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2465293 | lifeskim:mentions | umls-concept:C1704787 | lld:lifeskim |
| pubmed-article:2465293 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2465293 | pubmed:dateCreated | 1989-4-3 | lld:pubmed |
| pubmed-article:2465293 | pubmed:abstractText | Glycoprotein IIb-IIIa is the most prominent Arg-Gly-Asp (RGD)-binding adhesion receptor on platelets. By affinity chromatography on an immobilized RGD peptide, we have investigated the possible existence of other platelet-associated adhesion receptors that bind RGD peptides. When an octyl glucoside extract of surface-radioiodinated platelets was applied to an affinity matrix of KYGRGDS-coupled Sepharose 4B, a 160-kDa-labeled protein (P160) and GPIIb-IIIa bound and were specifically eluted by soluble GRGDSP peptide, but not by the variant GRGESP peptide. Furthermore, a dodecapeptide corresponding to fibrinogen gamma 400-411 eluted only GPIIb-IIIa but not P160 from the RGD affinity matrix. Characterization of P160 by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by the O'Farrell gel electrophoresis system indicated that P160 is a component of platelet GPIc. GoH3, a monoclonal antibody recognizing the alpha subunit of the very late antigen-6, failed to immunoprecipitate P160 from the RGD eluate, indicating that it did not contain the very late antigen-6 alpha subunit. In immunoblots, P160 reacted specifically with a polyclonal anti-peptide antibody recognizing the alpha subunit of the vitronectin receptor (VnR), but not with the monoclonal anti-GPIIb antibody PMI-1, suggesting that P160 is the alpha subunit of platelet VnR. This possibility was further substantiated by the complete identity between the determined amino-terminal sequence of P160 and the known sequence of the VnR alpha subunit. Moreover, direct association of P160 with a beta subunit having an apparent molecular weight similar to that of GPIIIa was demonstrated by immunoprecipitation with LM609, an anti-VnR complex monoclonal antibody. These results indicate that the VnR complex is present on platelets and may play a functional role in platelet adhesive reactions. | lld:pubmed |
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| pubmed-article:2465293 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2465293 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2465293 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2465293 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2465293 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2465293 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:PlowE FEF | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:GinsbergM HMH | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:MayT WTW | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:ChereshD ADA | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:FrelingerA... | lld:pubmed |
| pubmed-article:2465293 | pubmed:author | pubmed-author:D'SouzaS ESE | lld:pubmed |
| pubmed-article:2465293 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2465293 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2465293 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2465293 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2465293 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2465293 | pubmed:pagination | 3742-9 | lld:pubmed |
| pubmed-article:2465293 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2465293 | pubmed:meshHeading | pubmed-meshheading:2465293-... | lld:pubmed |
| pubmed-article:2465293 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2465293 | pubmed:articleTitle | Isolation and characterization of a platelet membrane protein related to the vitronectin receptor. | lld:pubmed |
| pubmed-article:2465293 | pubmed:affiliation | Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037. | lld:pubmed |
| pubmed-article:2465293 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2465293 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2465293 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2465293 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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