Alternative pathways for the activation of factor XIII

British Journal of Haematology
J McDonagh, R P McDonagh

Abstract

Factor XIII is present in plasma as a proenzyme, which when activated catalyses the formation of epsilon(gamma-glutamyl)lysyl bonds in fibrin. In this study the activation of purified plasma factor XIII was examined quantitatively with the fluorescent amine incorporation assay. Activation products were examined by polyacrylamide gel electrophoresis. The serin proteases, thrombin, trypsin, chymotrypsin, and factor Xa, and also Reptilase were tested for their ability to activate factor XIII. Highly purified thrombins activated purified factor XIII; this reaction was not calcium dependent. Trypsin was also a potent activator, but no transglutaminase activity was found with chymotrypsin. The most highly purified preparations of Reptilase had no effect on factor XIII activity. Less purified Reptilase preparations activated factor XIII, which suggests the presence of another enzyme in these Reptilase preparations. Highly purified factor Xa was found to be an effective activator of purified factor XIII. In contrast to thrombin activation, this reaction required calcium. It may be that under certain circumstances factor XIIIa could be formed in vivo directly by the alternative pathway of factor Xa. Factor XIIIa could then crosslink fib...Continue Reading

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Citations

Jan 1, 1985·Pharmacology & Therapeutics·F Kornalík
Aug 1, 1988·British Journal of Haematology· Than-ThanD A Warrell
Mar 17, 2009·Blood Cells, Molecules & Diseases·Younan ChenJingqiu Cheng
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Jul 12, 2011·Physiological Reviews·László MuszbekÉva Katona
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