Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots.

Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots.
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DOI:
10.1016/j.freeradbiomed.2013.06.039
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发表时间:
2013-12
影响因子:
7.4
通讯作者:
Ischiropoulos, Harry
Ischiropoulos, Harry
中科院分区:
医学1区
文献类型:
--
作者:
Martinez, Marissa;Weisel, John W.;Ischiropoulos, Harry

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Fibrinogen is a circulating multifunctional plasma protein vital for hemostasis. Activation of the coagulation cascade converts soluble fibrinogen to insoluble polymerized fibrin, which, along with platelets, forms the hemostatic clot. However, inappropriate formation of fibrin clots may result in arterial and venous thrombotic disorders that may progress to life-threatening adverse events. Often thrombotic disorders are associated with inflammation and the production of oxidants. Fibrinogen represents a potential target for oxidants and several oxidative post-translational modifications that influence fibrinogen structure and function have been associated with disease pathogenesis. Here, we review various oxidative modifications of fibrinogen and the consequences of these modifications on protein structure, ability to form fibrin and the resulting alterations on fibrin architecture, viscoelastic and biochemical properties that may contribute to disease.
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