pubmed-article:2948968 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C0072393 | lld:lifeskim |
pubmed-article:2948968 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:2948968 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2948968 | pubmed:dateCreated | 1987-3-12 | lld:pubmed |
pubmed-article:2948968 | pubmed:abstractText | Protein S is a vitamin K-dependent glycoprotein cofactor to the serine protease, activated protein C. In this study we demonstrate that 125I-protein S bound to unstimulated platelets in a time- and calcium-dependent saturable reaction. Half-maximal binding occurred at a protein S concentration of 10 nM, with approximately 1,100 binding sites per platelet. The binding of protein S to platelets was followed by rapid cleavage of the protein mediated by a protease confined to the platelet membrane. The membrane protease was Ca++-dependent, inhibited by high concentrations of diisopropyl fluorophosphate, but was resistant to a variety of other protease inhibitors. Functional studies demonstrated that the cleavage of protein S was associated with complete loss of cofactor anticoagulant activity. We conclude that protein S binds to platelets and is inactivated by a novel Ca++-dependent membrane protease. This may represent a physiological reaction that regulates the activity of protein S. | lld:pubmed |
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pubmed-article:2948968 | pubmed:language | eng | lld:pubmed |
pubmed-article:2948968 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2948968 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:2948968 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2948968 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2948968 | pubmed:issn | 0021-9738 | lld:pubmed |
pubmed-article:2948968 | pubmed:author | pubmed-author:MitchellC ACA | lld:pubmed |
pubmed-article:2948968 | pubmed:author | pubmed-author:SalemH HHH | lld:pubmed |
pubmed-article:2948968 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2948968 | pubmed:volume | 79 | lld:pubmed |
pubmed-article:2948968 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2948968 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2948968 | pubmed:pagination | 374-9 | lld:pubmed |
pubmed-article:2948968 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2948968 | pubmed:meshHeading | pubmed-meshheading:2948968-... | lld:pubmed |
pubmed-article:2948968 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2948968 | pubmed:articleTitle | Cleavage of protein S by a platelet membrane protease. | lld:pubmed |
pubmed-article:2948968 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2948968 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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