Vascular permeability enhancing activity of Porphyromonas gingivalis protease in guinea pigs.
Porphyromonas gingivalis protease, which had been isolated from a culture supernatant, caused vascular permeability enhancement in a dose-dependent manner when injected into guinea pig skin. The permeability-enhancing reaction caused by the protease was not affected by treatment with antihistamine, but was greatly augmented by simultaneous injection of a kinin potentiator, carboxypeptidase N inhibitor. However, the reaction was inhibited by soybean trypsin inhibitor or alpha 2-antiplasmin, although both of these inhibitors could not inhibit P. gingivalis protease at all by themselves. A bradykinin-degrading enzyme, carboxypeptidase B, weakened this vascular reaction. Results described indicate that the permeability-enhancing reaction induced by the protease is caused by activation, of the kallikrein-kinin cascade in the tissue.
Kaminishi
H
H
Department of Oral Microbiology, Fukuoka Dental College, Japan.
Cho
T
T
Itoh
T
T
Iwata
A
A
Kawasaki
K
K
Hagihara
Y
Y
Maeda
H
H
D000818:Animals; D002199:Capillary Permeability / Q000187:drug effects*; D002847:Chromatography, Agarose; D004789:Enzyme Activation / Q000187:drug effects; D005260:Female; D006168:Guinea Pigs; D016234:Kallikrein-Kinin System / Q000187:drug effects; D007610:Kallikreins / Q000378:metabolism; D008297:Male; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D012867:Skin / Q000098:blood supply; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D007610:Kallikreins