Activated factor XIII (FXIIIa) plays an important role in the final stage of the coagulation cascade by covalent crosslinking of fibrin strands. As a transglutaminase FXIIIa catalyses the generation of intermolecular amide bonds between lysine and glutamine residues resulting in a complex three-dimensional clot structure. Enhanced clot stability is supported by covalent binding of cyto-sceleton factors like actin and myosin. Moreover, the clot is protected against premature lysis by the incorporation of fibrinolysis inhibitors like ?2-antiplasmin and thrombin activatable fibrinolysis inhibitor (TAFI). A covalent crosslinking of the fibrin strands with extra-cellular matrix proteins like fibronectin, vitronectin, collagen and von Willebrand factor (vWF) immobilizes the clot at the site of injury. Moreover FXIII supports the healing process of damaged tissue. In this review assays for determination of FXIIIa activity, FXIII concentration and identification of the FXIIIVal34Leu polymorphism are shown.
Print ISSN: 0720-9355
Volume: 22
Pages: 32 - 42