title: Expression of ECE and related membrane peptidases in the EA.hy926 cell line.
abstract: The membrane anchorage of endothelin-converting enzyme (ECE) and endopeptidase E-24.11 (E-24.11) was investigated using the human endothelial cell line EA.hy926 as a model system. Detergent solubilization and temperature-induced phase separation data were consistent with recently published ECE sequences in characterizing ECE as an integral membrane protein. With GK4A9, a monoclonal antibody raised to E-24.11, more than 75% of total ECE activity could be precipitated from a membrane fraction, indicating a common epitope between ECE and E-24.11.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Leeds, England.
authors.forename: B J
authors.initials: BJ
authors.lastname: Walkden
authors.forename: A J
authors.initials: AJ
authors.lastname: Turner
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000032:analysis* / Q000276:immunology; D002460:Cell Line; D000072396:Endothelin-Converting Enzymes; D004730:Endothelium, Vascular / Q000201:enzymology*; D006801:Humans; D008666:Metalloendopeptidases; D015260:Neprilysin / Q000032:analysis* / Q000276:immunology
chemical_list: D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D015260:Neprilysin; D000072396:Endothelin-Converting Enzymes