Coagulation factor XIII A chain (F13A1) (F13A1)

Coagulation factor XIII A chain (F13A1) is the catalytic subunit of the heterotetrameric Factor XIII complex, which serves as the final enzyme in the blood coagulation cascade (UniProt P00488). Activated by thrombin and calcium, the A chain functions as a transglutaminase that catalyzes the formation of covalent gamma-glutamyl-epsilon-lysyl cross-links between fibrin molecules, thereby stabilizing the blood clot and protecting it from premature fibrinolysis (PubMed: 25154332). Beyond hemostasis, F13A1 plays critical roles in wound healing, angiogenesis, and the maintenance of pregnancy by supporting tissue remodeling and placental attachment (StatPearls: NBK542241). Genetic mutations in the F13A1 gene result in congenital Factor XIII deficiency, a rare but severe bleeding disorder characterized by umbilical cord bleeding, intracranial hemorrhage, and soft tissue hematomas. Therapeutic management involves replacement therapy using recombinant Factor XIII-A (e.g., Catridecacog) or plasma-derived concentrates to restore enzymatic activity and prevent bleeding episodes (DrugBank: DB09035). Additionally, the A chain is a target of interest for novel antithrombotic agents designed to modulate clot stability without significantly increasing systemic bleeding risk.

Other names

Factor XIII subunit AFibrin-stabilizing factor A subunitTransglutaminase A chainF13AProtein-glutamine gamma-glutamyltransferase A chain

Replacement of the catalytic subunit to restore transglutaminase activity for fibrin cross-linking and clot stabilization.