Fibrinogen is comprised of two sets of three polypeptide chains termed alpha, beta and gamma that are joined by disulfide bridging within the N-terminal E domain (1). Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. Fibrinogen binds through its gamma chain to cell surface receptors, growth factors, and coagulation factors to perform key roles in fibrin clot formation, platelet aggregation, and wound healing (2). Fibrinogen gamma chain, a fibrinogen gamma-chain variant generated via alternative mRNA processing, binding to thrombin and factor VIII results in clots that are mechanically stiffer and resistant to fibrinolysis (2). Elevated plasma fibrinogen gamma concentration is associated with myocardial infarction (3). Fibrinogen-gamma C-terminal fragments can induce endothelial barrier dysfunction and microvascular leak (4).
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