title: Biochemical properties of endothelin converting enzyme in renal epithelial cell lines.
abstract: 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.
authors.affiliation: Central Research Laboratories, Banyu Pharmaceutical Co., Ltd., Tokyo, Japan.
authors.forename: J
authors.initials: J
authors.lastname: Takada
authors.forename: M
authors.initials: M
authors.lastname: Hata
authors.forename: K
authors.initials: K
authors.lastname: Okada
authors.forename: K
authors.initials: K
authors.lastname: Matsuyama
authors.forename: M
authors.initials: M
authors.lastname: Yano
mesh_terms: 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
chemical_list: D016232:Endothelins; D011480:Protease Inhibitors; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes