Wolberg Alisa S, Campbell Robert A
Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, 815 Brinkhous-Bullitt Building, CB #7525, Chapel Hill, NC 27599-7525, USA.
Transfus Apher Sci. 2008 Feb;38(1):15-23. doi: 10.1016/j.transci.2007.12.005. Epub 2008 Feb 20.
Hemostatic clot formation entails thrombin-mediated cleavage of fibrinogen to fibrin. Previous in vitro studies have shown that the thrombin concentration present during clot formation dictates the ultimate fibrin structure. In most prior studies of fibrin structure, clotting was initiated by adding thrombin to a solution of fibrinogen; however, clot formation in vivo occurs in an environment in which the concentration of free thrombin changes over the reaction course. These changes depend on local cellular properties and available concentrations of pro- and anti-coagulants. Recent studies suggest that abnormal thrombin generation patterns produce abnormally structured clots that are associated with an increased risk of bleeding or thrombosis. Further studies of fibrin formation during in situ thrombin generation are needed to understand fibrin clot formation in vivo.
止血凝块的形成需要凝血酶介导纤维蛋白原裂解为纤维蛋白。先前的体外研究表明，凝块形成过程中存在的凝血酶浓度决定了最终的纤维蛋白结构。在大多数先前关于纤维蛋白结构的研究中，通过向纤维蛋白原溶液中添加凝血酶来启动凝血；然而，体内凝块形成发生在一个环境中，其中游离凝血酶的浓度在反应过程中会发生变化。这些变化取决于局部细胞特性以及促凝剂和抗凝剂的可用浓度。最近的研究表明，异常的凝血酶生成模式会产生结构异常的凝块，这与出血或血栓形成风险增加有关。需要进一步研究原位凝血酶生成过程中的纤维蛋白形成，以了解体内纤维蛋白凝块的形成。
