| pubmed-article:9239397 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C0041455 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9239397 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9239397 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9239397 | pubmed:dateCreated | 1997-9-4 | lld:pubmed |
| pubmed-article:9239397 | pubmed:abstractText | A cDNA (1.6 kb) encoding a platelet protein receptor that binds type I collagen has been isolated from a human bone marrow cDNA library by using a degenerate oligonucleotide probe derived from the amino acid sequence of a CNBr fragment of the purified receptor. Computer search revealed that this cDNA represents the coding sequence of a unique protein. Using the prokaryotic expression system pKK 223-3-65 cDNA, a 54-kD recombinant protein was obtained and purified to apparent homogeneity. In an eukaryotic expression vector (pcDNA3-65 cDNA), a 65-kD protein was identified that was recognized by monoclonal anti-65 kD antibody (anti-65m). The recombinant protein binds to type I, but not to type III collagen by affinity column chromatography. The binding of the recombinant protein to type I collagen-coated Petri dishes is inhibited by anti-65m in a dose-dependent manner. The pcDNA3-65 cDNA-transfected nonadherent T cells express the protein, allowing them to attach to a type I collagen matrix, and are inhibited by anti-65m in a dose-dependent manner. Like the receptor protein purified from platelet membranes, the recombinant protein inhibits type I collagen-induced platelet aggregation and the adhesion of [14C]serotonin-labeled platelets to type I collagen in a dose-dependent manner. The recombinant protein neither binds to type III collagen-coated Petri dishes nor inhibits type III collagen and ADP-induced platelet aggregation, indicating specificity for type I collagen. | lld:pubmed |
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| pubmed-article:9239397 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9239397 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9239397 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:9239397 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9239397 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9239397 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:9239397 | pubmed:author | pubmed-author:KangA HAH | lld:pubmed |
| pubmed-article:9239397 | pubmed:author | pubmed-author:ChiangT MTM | lld:pubmed |
| pubmed-article:9239397 | pubmed:author | pubmed-author:RinaldyAA | lld:pubmed |
| pubmed-article:9239397 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9239397 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9239397 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:9239397 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9239397 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9239397 | pubmed:pagination | 514-21 | lld:pubmed |
| pubmed-article:9239397 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9239397 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9239397 | pubmed:articleTitle | Cloning, characterization, and functional studies of a nonintegrin platelet receptor for type I collagen. | lld:pubmed |
| pubmed-article:9239397 | pubmed:affiliation | Department of Medicine, University of Tennessee at Memphis, Memphis, Tennessee 38104, USA. tchiang@utmem2.utmen.edu | lld:pubmed |
| pubmed-article:9239397 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9239397 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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