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Aprotinin inhibits urokinase but not tissue-type plasminogen activator
R Lottenberg1, N Sjak-Shie, A T Fazleabas
1Department of Medicine, University of Florida College of Medicine, Gainesville 32610.
Abstract:
The protease inhibitor, aprotinin, has been examined for its ability to inhibit urokinase and tissue-type plasminogen activators at pH 7.4 in assays utilizing pyroGlu-Gly-Arg-p-nitroanilide and H-D-Ile-Pro-Arg-p-nitroanilide as substrates, respectively. Aprotinin inhibited both two-chain low molecular weight urokinase and the high molecular weight form of the enzyme in a competitive manner with a similar Ki (27 microM). There was no observable inhibition of tissue-type plasminogen activators at aprotinin concentrations up to 500 microM. These findings suggest that sensitivity to inhibition by aprotinin could be used to distinguish tissue-type and urokinase-type plasminogen activators.