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Factor XIIIa formation promoted by complexing of alpha-thrombin, fibrin,
and plasma factor XIII
CS Greenberg, KE Achyuthan and JW Fenton
Fibrin polymers (des A,B fibrinogen) reduced the concentration of alpha-
thrombin required for 50% activation of plasma factor XIII (a2b2 tetramer)
by approximately 100-fold. In the presence of fibrin, the amount of
gamma-thrombin required for activation was not affected. Catalytically
inactive i-Pr2P- and D-Phe-Pro-Arg-CH2-alpha-thrombin were found to inhibit
over 95% of the activation by alpha-thrombin in the presence of fibrin.
Unlike plasma factor XIII, the concentration of alpha-thrombin required for
50% activation of platelet factor XIII (a2 dimer) was lower, and the
activation was not enhanced by fibrin. However, when the a2 platelet factor
XIII was incubated with purified b- chains, the alpha- and gamma-thrombin
concentrations required for activation increased tenfold and reached levels
similar to those required for activation of the plasma factor XIII. When
fibrin was present, the alpha-thrombin concentrations needed for activation
of the a2b2 complexes were reduced, and the presence of fibrin had no
effect on gamma-thrombin cleavage of the a2b2 complexes. Therefore, the b-
chains must inhibit a-chain cleavage by alpha-thrombin in the absence of
fibrin. These results imply that the formation of a cocomplex involving
alpha-thrombin, fibrin, and plasma factor XIII causes some conformational
change in plasma factor XIII such that the b-chains no longer inhibit
cleavage of the a-chains.
Volume 69,
Issue 3,
pp. 867-871,
03/01/1987
Copyright © 1987 by The American Society of Hematology
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