Factor XIII transamidase is an enzyme that plays a crucial role in the final step of blood clot formation, known as clot stabilization. It is also referred to as fibrin stabilizing factor or coagulation factor XIII (FXIII). The enzyme is a heterotetramer consisting of two A subunits and two B subunits.
Factor XIII transamidase acts on the clotting protein fibrinogen, which is converted into fibrin during the coagulation process. Once fibrin is formed, the transamidase catalyzes the formation of covalent bonds between adjacent fibrin molecules, resulting in the cross-linking of fibrin polymers. This cross-linking provides structural strength and stability to the clot, making it resistant to breakdown and dissolution.
The activity of factor XIII transamidase is essential for the proper functioning of blood coagulation and wound healing. Deficiency or dysfunction of this enzyme can lead to various bleeding disorders, such as congenital factor XIII deficiency, in which patients experience abnormal bleeding and delayed wound healing.
Factor XIII transamidase is also involved in non-hemostatic functions, including tissue repair, angiogenesis, and immune regulation. It participates in scar formation during tissue healing by stabilizing newly formed fibrin meshwork. Additionally, it plays a role in the clearance of immune complexes through interactions with immune cells and complement system.
In summary, factor XIII transamidase is an enzyme responsible for stabilizing blood clots by cross-linking fibrin polymers, and its deficiency or malfunction can result in bleeding disorders. Furthermore, it has non-hemostatic functions related to tissue repair and immune regulation.
