The effect of blood coagulation factor XIII on fibrin clot structure and fibrinolysis
The effect of blood coagulation factor XIII on fibrin clot structure and fibrinolysis
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DOI:
10.1111/jth.12455
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发表时间:
2014-02-01
影响因子:
10.4
通讯作者:
Philippou, H.
中科院分区:
文献类型:
--
作者:
Hethershaw, E. L.;La Corte, A. L. Cilia;Philippou, H.
BackgroundFactor XIII is a 320kDa tetramer, comprising two enzymatic A-subunits and two carrier B-subunits (FXIII A(2)B(2)). Activated FXIII (FXIIIa) catalyses the formation of epsilon-(-glutamyl)lysyl covalent bonds between -, - and - chains of adjacent fibrin molecules and also cross-links the major plasmin inhibitor, 2-antiplasmin, to fibrin.ObjectivesWe investigated the role of FXIII cross-linking of fibrin directly in clot morphology and its functional effect on clot formation and lysis, in the absence of 2-antiplasmin.Results and ConclusionsOur data show that the presence of FXIII during clot formation results in fibrin clots that have a significant 2.1-fold reduction in pore size, as determined by the Darcy constant, Ks, and formed thinner fibers (74.7 +/- 1.5nm) and higher density of fibers compared with those without FXIII (86.0 +/- 1.7nm, P