Involvement of Protease Inhibitors in Staphylokinase-Induced Fibrin-Specific Fibrinolysis.

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We compared the fibrinolytic properties of recombinant staphylokinase (SAK), a fibrin-specific plasminogen activator, with those of streptokinase and tissue-type plasminogen activator (t-PA) by means of the amidolytic method. We also investigated the involvement of α2-macroglobulin, C1-inactivator and α1-antitrypsin in SAK-induced fibrin-specific fibrinolysis. Both SAK and t-PA activated plasminogen efficiently in the presence of fibrin in human plasma. Although t-PA activated plasminogen dependently on fibrin in the reconstituted plasma system, SAK activated plasminogen independently of fibrin without α2-plasmin inhibitor (α2-antiplasmin, α2-PI). These findings suggest that fibrin and α2-PI play important roles in plasminogen activation by SAK but not by t-PA. Furthermore, protease inhibitors such as α2-PI, α2-macroglobulin, C1-inactivator and α1-antitrypsin inhibited plasminogen activation by SAK and the inhibitory actions of these protease inhibitors disappeared in the presence of fibrin. This shows that α2-macroglobulin, C1-inactivator and α1-antitrypsin, other than α2-PI, contribute to the fibrin-specificity of SAK.

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