Abstract
The thrombolytic mechanism of pro-urokinase (Pro-UK) was investigated. Pro-UK is of a single-chain form, and is converted to UK with plasmin-Sepharose. The [3H]DFP incorporation was strongly enhanced by plasmin treatment, which induces conformational changes as observed from the circular dichroism. A relatively higher affinity of Pro-UK for fibrin than that of UK was found by adsorption on fibrin-Sepharose and also by incorporation into fibrin during fibrinogen-fibrin conversion. Pro-UK produced effective thrombolysis without degrading fibrinogen. The presence of t-PA in the thrombus promoted thrombolysis effectively. Further, coexistence of t-PA and Pro-UK in the plasma markedly enhanced the thrombolysis. The adsorption of Pro-UK, plasminogen and t-PA on fibrin-Sepharose induced rapid activation of Pro-UK to UK as well as rapid production of plasmin on the fibrin surface. These results suggest that a trace amount of t-PA causes marked enhancement of Pro-UK induced thrombolysis.
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