Activation of human plasma prekallikrein by Pseudomonas aeruginosa elastase in vitro.
Human plasma prekallikrein, precursor of the bradykinin-generating enzyme, was activated in a purified system under a near physiological condition (pH 7.8, ionic strength I = 0.14, 37 degrees C) by Pseudomonas aeruginosa elastase which is a tissue-destructive metalloproteinase. Compared with that, Pseudomonas aeruginosa alkaline proteinase poorly activated it with a rate as low as less than one-twentieth of that of elastase. The activation by elastase was blocked with a specific inhibitor of elastase, HONHCOCH(CH2C6H5)CO-Ala-Gly-NH2 (10 microM). Generation of kallikrein-like amidolytic activity was also observed in plasma deficient in Hageman factor by treatment with elastase, but was not in plasma deficient in prekallikrein. The kallikrein-like activity generated in Hageman factor deficient plasma as well as the generation process itself was indeed inhibited by anti-human prekallikrein goat antibody. These results suggest that the pathological activation of the kallikrein-kinin system might occur under certain clinical conditions in pseudomonal infections.
Shibuya
Y
Y
Department of Allergy, Institute for Medical Immunology, Kumamoto University Medical School, Japan.
Tanaka
H
H
Nishino
N
N
Okabe
H
H
Kambara
T
T
Yamamoto
T
T
D000595:Amino Acid Sequence; D004789:Enzyme Activation; D005175:Factor XII Deficiency / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011288:Prekallikrein / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D011288:Prekallikrein; D010196:Pancreatic Elastase