| pubmed-article:10373475 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0015498 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0015501 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C1552302 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C1552291 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10373475 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:10373475 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:10373475 | pubmed:dateCreated | 1999-7-15 | lld:pubmed |
| pubmed-article:10373475 | pubmed:abstractText | The blood coagulation proteinase, thrombin, converts factor V into factor Va through a multistep activation pathway that is regulated by interactions with thrombin exosites. Thrombin exosite interactions with human factor V and its activation products were quantitatively characterized in equilibrium binding studies based on fluorescence changes of thrombin covalently labeled with 2-anilinonaphthalene-6-sulfonic acid (ANS) linked to the catalytic site histidine residue by Nalpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2Cl ([ANS]FPR-thrombin). Exosite I was shown to play a predominant role in the binding of factor V and factor Va from the effect of the exosite I-specific ligand, hirudin54-65, on the interactions. Factor V and factor Va bound to exosite I of [ANS]FPR-thrombin with similar dissociation constants of 3.4 +/- 1.3 and 1.1 +/- 0.4 microM and fluorescence enhancements of 182 +/- 41 and 127 +/- 17%, respectively. Native thrombin and labeled thrombin bound with similar affinity to factor Va. Among factor V activation products, the factor Va heavy chain was shown to contain the site of exosite I binding, whereas exosite I-independent, lower affinity interactions were observed for activation fragments E and C1, and no detectable binding was observed for the factor Va light chain. The results support the conclusion that the factor V activation pathway is initiated by exosite I-mediated binding of thrombin to a site in the heavy chain region of factor V that facilitates the initial cleavage at Arg709 to generate the heavy chain of factor Va. The results further suggest that binding of thrombin through exosite I to factor V activation intermediates may regulate their conversion to factor Va and that similar binding of thrombin to the factor Va produced may reflect a mode of interaction involved in the regulation of prothrombin activation. | lld:pubmed |
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| pubmed-article:10373475 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10373475 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10373475 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10373475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10373475 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10373475 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10373475 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10373475 | pubmed:author | pubmed-author:BockP EPE | lld:pubmed |
| pubmed-article:10373475 | pubmed:author | pubmed-author:OlsonS TST | lld:pubmed |
| pubmed-article:10373475 | pubmed:author | pubmed-author:Dharmawardana... | lld:pubmed |
| pubmed-article:10373475 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10373475 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10373475 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10373475 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10373475 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10373475 | pubmed:pagination | 18635-43 | lld:pubmed |
| pubmed-article:10373475 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10373475 | pubmed:meshHeading | pubmed-meshheading:10373475... | lld:pubmed |
| pubmed-article:10373475 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10373475 | pubmed:articleTitle | Role of regulatory exosite I in binding of thrombin to human factor V, factor Va, factor Va subunits, and activation fragments. | lld:pubmed |
| pubmed-article:10373475 | pubmed:affiliation | Department of Pathology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. | lld:pubmed |
| pubmed-article:10373475 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10373475 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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