Transglutaminase in blood coagulation: Factor XIIIa (FXIIIa) Crosslinking of fibrin by Kevin Ahern 3

Kevin Ahern
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FXIIIa
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Fibrin stabilizing factor (factor XIII or FXIII) plays a critical role in the generation of a viable hemostatic plug. Following exposure to thrombin and calcium, the zymogen is activated to FXIIIa that, in turn, catalyzes the formation of N epsilon(gamma-glutamyl)lysine protein-to-protein side chain bridges within the clot network. Introduction of these covalent crosslinks greatly augments the viscoelastic storage modulus of the structure and its resistance to fibrinolytic enzymes (Lorand 2001).

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 (Wilmer 2002).

Coagulation factor XIII (FXIII) is a protein that promotes fibrin stabilization by forming multiple covalent cross-links between fibrin monomers (Franchini 2013).

FXIII (Factor XIII) is a Ca²+-dependent enzyme which forms covalent ϵ-(γ-glutamyl)lysine cross-links between the γ-carboxy-amine group of a glutamine residue and the ϵ-amino group of a lysine residue. FXIII was originally identified as a protein involved in fibrin clot stabilization (Richardson 2013).

Factor XIII (FXIII) is activated by thrombin to form a transglutaminase (FXIIIa) that stabilizes clot formation by the cross-linking of fibrin monomers and antifibrinolytic proteins (Levy 2013).

Coagulation factor XIII (FXIII) is converted by thrombin and Ca(2+) into an active transglutaminase (FXIIIa) in the final phase of coagulation cascade. Its main function is the mechanical stabilization of fibrin clot and its protection from fibrinolysis by cross-linking of fibrin chains and α(2)-plasmin inhibitor to fibrin (Katona 2012).

In the final phase of the coagulation cascade, FXIII is converted into an active transglutaminase (FXIIIa) by thrombin and Ca(2+). FXIIIa strengthens fibrin clot mechanically by cross-linking fibrin chains (Bereczky 2011)

The plasma circulating zymogenic coagulation factor XIII (FXIII) is a protransglutaminase, which upon activation by thrombin and calcium cross-links preformed fibrin clots/fibrinolytic inhibitors making them mechanically stable and less susceptible to fibrinolysis (Biswas 2014).

Factor XIII (FXIII) is a protransglutaminase that, after activation, cross-links fibrin chains and several plasma proteins, most importantly alpha plasmin inhibitor, to fibrin. FXIII strengthens the fibrin clot by covalent bonds and protects fibrin from the prompt elimination by the fibrinolytic system (Muszbek 2010).

Blood coagulation factor XIII (FXIII), which becomes transformed into an active transglutaminase (FXIIIa) in the final phase of coagulation cascade by thrombin and Ca(2+). FXIII is essential for hemostasis, its deficiency results in severe bleeding diathesis. FXIIIa mechanically stabilizes fibrin by cross-linking its α-, and γ-chains. It also protects newly formed fibrin from fibrinolysis, primarily by cross-linking α(2)-plasmin inhibitor to fibrin (Bagoly 2012).

Factor XIII (FXIII) is a tetrameric zymogen (FXIII-A (2)B (2)) that is converted into an active transglutaminase (FXIIIa) by thrombin and Ca (2+) in the terminal phase of the clotting cascade. By cross-linking fibrin chains and alpha (2) plasmin inhibitor to fibrin, FXIIIa mechanically stabilizes fibrin and protects it from fibrinolysis (Karimi 2009)

Blood coagulation factor XIII (FXIII) is a protransglutaminase that becomes activated by the concerted action of thrombin and Ca2+ in the final stage of the clotting cascade. In addition to plasma, FXIII also occurs in platelets, monocytes, and monocyte-derived macrophages. The main physiological function of plasmaFXIII is to cross-link fibrin and protect it from the fibrinolytic plasmin (Muszebk 1996).

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