Insulin-like activity of Proteases. III. Effect of Insulin-like Activity-possessing Protease on Vascular Permeability

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The insulin-like activity-possessing protease (ILAPP), which was partially purified from Pronase, showed a high but short-lived increasing effect on the vascular permeability of mice, whereas only a low hemorrhagic activity was detected at the same dose. Soybean trypsin inhibitor and leupeptin both inhibited this increasing effect, whereas they exerted no influence on the hydrolytic activity of ILAPP towards casein or succinyl-L-alanyl-L-alanyl-L-alanine p-nitroanilide under the same conditions. The vasodilative activity assayed in a dog was very low, and no kinin-forming activity was detected. This enzyme showed a kinin-inactivating activity when preincubated with bradykinin. Its hydrolytic activity was higher towards acetyl-L-alanyl-L-alanyl-L-alanine methyl ester than towards derivatives of basic amino acid methyl esters. These results suggest that ILAPP differs from trypsin and trypsin-like enzymes in the specificity. The possibility that the insulin-like activity of ILAPP is attributable to kinins produced directly by ILAPP may therefore be excluded.
公益社団法人日本薬学会の論文
1980-06-25