Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots |
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Institution: | 1. Institute for the Application of Nuclear Energy (INEP), Department for Metabolism, University of Belgrade, Banatska 31b, 11000 Belgrade, Serbia;2. Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia |
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Abstract: | 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 posttranslational 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 and the ability to form fibrin and how the resulting alterations affect fibrin architecture and viscoelastic and biochemical properties that may contribute to disease. |
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Keywords: | Fibrinogen Fibrin Coagulation Thrombosis Oxidation Nitrotyrosine Free radicals |
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