title: Endothelin-converting enzymes.
abstract: The putative endothelin-converting enzyme (ECE) has been the focus of intense research, both within academia and the pharmaceutical industry. Interest in ECE stems mainly from the hypothesis that development of inhibitors of ECE will provide an effective means of preventing production of endothelin in circumstances where it may play a pathogenic role. Both an aspartic and a metalloprotease have been identified that have characteristics of this putative enzyme. Evidence suggests that the metalloprotease, which is inhibited by phosphoramidon, may be the physiologically relevant converting enzyme. However, it remains to be demonstrated conclusively that any inhibitor of an ECE activity directly alters endogenous endothelin production and/or the pathogenesis of a disease condition in which endothelin is thought to play a primary role.
authors.affiliation: Pharmaceutical Products Division, Abbott Laboratories, Illinois 60064.
authors.forename: T J
authors.initials: TJ
authors.lastname: Opgenorth
authors.forename: J R
authors.initials: JR
authors.lastname: Wu-Wong
authors.forename: K
authors.initials: K
authors.lastname: Shiosaki
mesh_terms: D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000072396:Endothelin-Converting Enzymes; D016232:Endothelins / Q000378:metabolism*; D006801:Humans; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data
chemical_list: D016232:Endothelins; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes