Inactivation of bradykinin and kallidin by cathepsin G and mast cell chymase.
Human neutrophil cathepsin G and human skin chymase can inactivate bradykinin by cleavage at the carboxy terminal phenylalanyl-arginyl peptide bond of this polypeptide. The mast cell enzyme is far more effective than cathepsin G, the rates of hydrolysis being comparable to that found for angiotensin I to angiotensin II conversion (C.F. Reilly, D. Tewksbury, N. Schechter, and J. Travis, J. Biological Chemistry 257:8619-8622). This ability to both inactivate bradykinin and accelerate the production of angiotensin II may be of significance in the development of biochemical events associated with inflammation.
D000595:Amino Acid Sequence; D001920:Bradykinin / Q000378:metabolism*; D056649:Cathepsin G; D002403:Cathepsins / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D053818:Chymases; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D007609:Kallidin / Q000378:metabolism*; D008407:Mast Cells / Q000201:enzymology; D009504:Neutrophils / Q000201:enzymology; D012697:Serine Endopeptidases; D012867:Skin / Q000201:enzymology
D007609:Kallidin; D002403:Cathepsins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D053818:Chymases; D001920:Bradykinin