Differential binding of plasminogen to crosslinked and noncrosslinked
fibrins: its significance in hemostatic defect in factor XIII deficiency
Y Sakata, J Mimuro and N Aoki
In spontaneous fibrinolysis of an alpha 2-plasmin inhibitor-deficient
plasma clot or tissue-type plasminogen activator-induced fibrinolysis in a
purified system without alpha 2-plasmin inhibitor, the lysis was faster
when factor XIII-mediated crosslinking of fibrin to fibrin did not occur.
During the initial period, the binding of plasminogen to fibrin steadily
increased with incubation time. The initial level and subsequent increase
of the binding, which may be critical for the subsequent development of
fibrinolysis, were more remarkable when fibrin was not crosslinked. The
amount of glu- or lys-plasminogen bound to noncrosslinked fibrin was around
4 or 1.5 times larger than the amount of the respective plasminogen bound
to crosslinked fibrin. Plasmin was also found to be bound to noncrosslinked
fibrin twice as much as the amount bound to crosslinked fibrin. Structural
changes induced by crosslinking of fibrin alpha-chain may reduce either the
affinity or the number of available complementary sites to lysine binding
sites of plasmin(ogen), thereby decreasing the binding of plasmin(ogen) to
fibrin. These results suggest that an increased affinity of noncrosslinked
fibrin for plasmin(ogen) is contributory to the accelerated fibrinolysis
observed in factor XIII deficiency, in addition to an absence of
crosslinking of alpha 2-plasmin inhibitor to fibrin.
Volume 63,
Issue 6,
pp. 1393-1401,
06/01/1984
Copyright © 1984 by The American Society of Hematology
