VASCULAR-PERMEABILITY ENHANCING ACTIVITY OF PORPHYROMONAS-GINGIVALIS PROTEASE IN GUINEA-PIGS

Porphyromonas gingivalis protease, which had been isolated from a cult ure supernatant, caused vascular permeability enhancement in a dose-de pendent manner when injected into guinea pig skin. The permeability-en hancing reaction caused by the protease was not affected by treatment with antihistamine, but was greatly augmented by simultaneous injectio n of a kinin potentiator, carboxypeptidase N inhibitor. However, the r eaction was inhibited by soybean trypsin inhibitor or alpha(2)-antipla smin, although both of these inhibitors could not inhibit P. gingivali s protease at all by themselves. A bradykinin-degrading enzyme, carbox ypeptidase B, weakened this vascular reaction. Results described indic ate that the permeability-enhancing reaction induced by the protease i s caused by activation of the kallikrein-kinin cascade in the tissue.