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J. Biol. Chem., Vol. 268, Issue 24, 17711-17715, 08, 1993
K Maruo, T Akaike, Y Inada, I Ohkubo, T Ono and H Maeda
Kinin release from guinea pig plasma high molecular weight kininogen (HMWK)
induced by various microbial and mite proteases has been demonstrated
previously (Molla, A., Yamamoto, T., Akaike, T., Miyoshi, S., and Maeda, H.
(1989) J. Biol. Chem. 264, 10589-10594; Maruo, K., Akaike, T., Matsumura,
Y., Kohmoto, S., Inada, Y., Ono, T., Arao, T., and Maeda, H. (1991)
Biochim. Biophys. Acta 1074, 62-68). In this paper, we describe the effects
of various microbial and mite proteases on low molecular weight kininogen
(LMWK) and HMWK from human plasma. A protease from the house dust mite
Dermatophagoides farinae (Df- protease) directly liberated kinin from both
LMWK and HMWK to a significant degree. The Km, kcat, and kcat/Km values for
kinin generation from LMWK were 3.24 microM, 0.61 s-1, and 1.9 x 10(5) M-1
x s-1, respectively, and those for kinin generation from HMWK were 0.56
microM, 0.12 s-1, and 2.1 x 10(5) M-1 x s-1, respectively; kcat/Km values
for Df-protease were comparable with that for glandular kallikrein. In
contrast, microbial proteases showed only weak kinin- releasing activity
from both human plasma kininogens. Four of ten different microbial
proteases liberated kinin from LMWK, and only serratial 56-kDa protease
released kinin from HMWK. Furthermore, Df- protease markedly inactivated
the thiol protease inhibitory activity of LMWK and HMWK, whereas all
microbial proteases (as well as the endogenous protease trypsin) did not
affect this inhibitory activity of both kininogens from human plasma.
Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity
Department of Microbiology, Kumamoto University School of Medicine, Japan.
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