Abstract:
:Human fibrinogen 1 is homodimeric with respect to its gamma chains (gammaA-gammaA'), whereas fibrinogen 2 molecules each contain one gammaA (gammaA1-411V) and one gamma' chain, which differ by containing a unique C-terminal sequence from gamma'408 to 427L that binds thrombin and factor XIII. We investigated the structural and functional features of these fibrins and made several observations. First, thrombin-treated fibrinogen 2 produced finer, more branched clot networks than did fibrin 1. These known differences in network structure were attributable to delayed release of fibrinopeptide (FP) A from fibrinogen 2 by thrombin, which in turn was likely caused by allosteric changes at the thrombin catalytic site induced by thrombin exosite 2 binding to the gamma' chains. Second, cross-linking of fibrin gamma chains was virtually the same for both types of fibrin. Third, the acceleratory effect of fibrin on thrombin-mediated XIII activation was more prominent with fibrin 1 than with fibrin 2, and this was also attributable to allosteric changes at the catalytic site induced by thrombin binding to gamma' chains. Fourth, fibrinolysis of fibrin 2 was delayed compared with fibrin 1. Altogether, differences between the structure and function of fibrins 1 and 2 are attributable to the effects of thrombin binding to gamma' chains.
journal_name
Bloodjournal_title
Bloodauthors
Siebenlist KR,Mosesson MW,Hernandez I,Bush LA,Di Cera E,Shainoff JR,Di Orio JP,Stojanovic Ldoi
10.1182/blood-2005-01-0240subject
Has Abstractpub_date
2005-10-15 00:00:00pages
2730-6issue
8eissn
0006-4971issn
1528-0020pii
2005-01-0240journal_volume
106pub_type
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