Biochemical properties of endothelin converting enzyme in renal epithelial cell lines.
This is the first report clearly demonstrating the presence of endothelin (ET) converting enzyme (ECE) in non-vascular cells (renal epithelial cell lines, MDCK and LLC-PK1). ECEs derived from these epithelial cells were very similar to the endothelial ECE in the following biochemical properties: 1) The optimum pH was 7.0; 2) the Km value for big ET-1 was approximately 30 microM; 3) the enzyme was potently inhibited by EDTA, o-phenanthroline and phosphoramidon; and 4) the enzyme did not convert big ET-2 or big ET-3. These data suggest that phosphoramidon-sensitive ECE is involved in the processing of big ET-1 to ET-1 in the renal tubule.
Takada
J
J
Central Research Laboratories, Banyu Pharmaceutical Co., Ltd., Tokyo, Japan.
Hata
M
M
Okada
K
K
Matsuyama
K
K
Yano
M
M
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D000072396:Endothelin-Converting Enzymes; D016232:Endothelins / Q000378:metabolism*; D004848:Epithelium / Q000201:enzymology; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008666:Metalloendopeptidases; D008861:Microsomes / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology
D016232:Endothelins; D011480:Protease Inhibitors; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes