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 α_2-macroglobulin, C_1-inactivator and α_1-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 α_2-plasmin inhibitor (α_2-antiplasmin, α_2-PI). These findings suggest that fibrin and α_2-PI play important roles in plasminogen activation by SAK but not by t-PA. Furthermore, protease inhibitors such as α_2-PI, α_2-macroglobulin, C_1-inactivator and α_1-antitrypsin inhibited plasminogen activation by SAK and the inhibitory actions of these protease inhibitors disappeared in the presence of fibrin. This shows that α_2-macroglobulin, C_1-inactivator and α_1-antitrypsin, other than α_2-PI, contribute to the fibrin-specificity of SAK.
社団法人日本薬学会の論文
1994-12-15