Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 65, Issue -, Pages 411-418Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2013.06.039
Keywords
Fibrinogen; Fibrin; Coagulation; Thrombosis; Oxidation; Nitrotyrosine; Free radicals
Funding
- NHLBI NIH HHS [R01 HL103918] Funding Source: Medline
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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 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. (C) 2013 Elsevier Inc. All rights reserved.
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