| pubmed-article:12939270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0033706 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:12939270 | lifeskim:mentions | umls-concept:C0072435 | lld:lifeskim |
| pubmed-article:12939270 | pubmed:issue | 45 | lld:pubmed |
| pubmed-article:12939270 | pubmed:dateCreated | 2003-11-3 | lld:pubmed |
| pubmed-article:12939270 | pubmed:abstractText | Prothrombin (Pro) activation by factor Xa generates the thrombin catalytic site and exosites I and II. The role of fragment 1 (F1) in the pathway of exosite I expression during Pro activation was characterized in equilibrium binding studies using hirudin(54-65) labeled with 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate ([NBD]Hir(54-65)(SO3-)) or 5-(carboxy)fluorescein ([5F]Hir(54-65)(SO3-)). [NBD]Hir(54-65)(SO3-) distinguished exosite I environments on Pro, prethrombin 1 (Pre 1), and prethrombin 2 (Pre 2) but bound with the same affinities as [5F]Hir(54-65)(SO3-). Conversion of Pro to Pre 1 caused a 7-fold increase in affinity for the peptides. Conversely, fragment 1.2 (F1.2) decreased the affinity of Pre 2 for [5F]Hir(54-65)(SO3-) by 3-fold. This was correlated with a 16-fold increased affinity of F1.2 for Pre 2 in comparison to thrombin, demonstrating an enhancing effect of F1 on F1.2 binding. The active intermediate, meizothrombin, demonstrated a 50- to 220-fold increase in exosite affinity. Free thrombin and thrombin.F1.2 complex bound [5F]Hir(54-65)(SO3-) with indistinguishable affinity, indicating that the effect of F1 on peptide binding was eliminated upon expression of catalytic activity and exosite I. The results demonstrate a new zymogen-specific role for F1 in modulating the affinity of ligands for exosite I. This may reflect a direct interaction between the F1 and Pre 2 domains in Pro that is lost upon folding of the zymogen activation domain. The effect of F1 on (pro)exosite I and the role of (pro)exosite I in factor Va-dependent substrate recognition suggest that the Pro activation pathway may be regulated by (pro)exosite I interactions with factor Va. | lld:pubmed |
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| pubmed-article:12939270 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12939270 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12939270 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12939270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12939270 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:12939270 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12939270 | pubmed:author | pubmed-author:BockPaul EPE | lld:pubmed |
| pubmed-article:12939270 | pubmed:author | pubmed-author:AndersonPatri... | lld:pubmed |
| pubmed-article:12939270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12939270 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:12939270 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12939270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12939270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12939270 | pubmed:pagination | 44489-95 | lld:pubmed |
| pubmed-article:12939270 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12939270 | pubmed:meshHeading | pubmed-meshheading:12939270... | lld:pubmed |
| pubmed-article:12939270 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12939270 | pubmed:articleTitle | Role of prothrombin fragment 1 in the pathway of regulatory exosite I formation during conversion of human prothrombin to thrombin. | lld:pubmed |
| pubmed-article:12939270 | pubmed:affiliation | Department of Pathology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. | lld:pubmed |
| pubmed-article:12939270 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12939270 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12939270 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12939270 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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