Inhibition of mite protease (Df-protease) with protease inhibitors.
A protease from house dust mite(Dermatophagoides farinae) having high specificity towards a substrate of blood coagulation factor XIIa catalyzes the activation of kallikrein-kinin system in plasma (Takahashi et al., 1990). To prevent the formation of kinin by the mite-protease, inhibition of the protease with its inhibitors was tested in vitro and in vivo. Its kinetic studies revealed that Ki values are 3.9 x 10(-10) M for aprotinin, 3.0 x 10(-9) M for soybean trypsin inhibitor (Kunitz) and 2.5 x 10(-8) M for gabexate mesylate. Enhancement of blood permeability in guinea pigs caused by the protease was markedly suppressed by these inhibitors.
D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D001667:Binding, Competitive; D002199:Capillary Permeability / Q000187:drug effects; D010450:Endopeptidases / Q000378:metabolism* / Q000494:pharmacology; D015956:Factor XIIa / Q000378:metabolism; D016670:Gabexate / Q000494:pharmacology; D006168:Guinea Pigs; D016234:Kallikrein-Kinin System / Q000187:drug effects; D007610:Kallikreins / Q000378:metabolism; D007700:Kinetics; D008925:Mites / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology*; D012867:Skin / Q000098:blood supply; D013379:Substrate Specificity; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000494:pharmacology
D011480:Protease Inhibitors; D016670:Gabexate; D007611:Aprotinin; D014360:Trypsin Inhibitor, Kunitz Soybean; D010450:Endopeptidases; D007610:Kallikreins; D015956:Factor XIIa