FGG

Fibrinogen gamma chain (FGG), a critical component of the fibrinogen hexamer, polymerizes with alpha (FGA) and beta (FGB) chains to form fibrin matrices essential for hemostasis. Also termed FGγ, this 48-kDa glycoprotein undergoes thrombin-mediated cleavage during coagulation, releasing fibrinopeptides to initiate clot formation. FGG interacts with integrins (αvβ3, αIIbβ3) and endothelial receptors, influencing thrombus stability and wound healing. Its genetic variants (e.g., FGG rs2066865) are linked to dysfibrinogenemias, predisposing to thrombosis, hemorrhage, or hypofibrinogenemia. Elevated FGG correlates with cardiovascular diseases, hepatic fibrosis, and cancer metastasis via extracellular matrix remodeling. Therapeutic strategies include recombinant fibrinogen for congenital deficiencies and antifibrinolytic agents (e.g., tranexamic acid) to mitigate bleeding. Novel FGG-targeted nanotherapies and monoclonal antibodies are under preclinical investigation for thrombotic disorders.