title: Localization and biochemical characterization of endothelin-converting enzyme.
abstract: We used a variety of biochemical and immunologic techniques to investigate the localization of endothelin-converting enzyme (ECE) in porcine lung, in human umbilical vein endothelial cells (HUVECs), and in the transformed endothelial cell line EA.hy926. Phosphoramidon-sensitive ECE activity was not enriched on immunomagnetically separated angiotensin-converting enzyme (ACE)-bearing luminal endothelial membranes from pig lung, whereas ACE showed a sevenfold enrichment. ECE activity did, however, co-localize with aminopeptidase-N (AP-N) activity on isolated EA.hy926 plasma membranes. Using a monoclonal antibody to rat lung ECE (AEC32-326) and immunofluorescence microscopy, we have demonstrated ECE on the cell surface of endothelial cell lines.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Leeds, England.
authors.forename: K
authors.initials: K
authors.lastname: Barnes
authors.forename: L J
authors.initials: LJ
authors.lastname: Murphy
authors.forename: M
authors.initials: M
authors.lastname: Takahashi
authors.forename: K
authors.initials: K
authors.lastname: Tanzawa
authors.forename: A J
authors.initials: AJ
authors.lastname: Turner
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000032:analysis / Q000276:immunology / Q000378:metabolism*; D002478:Cells, Cultured; D000072396:Endothelin-Converting Enzymes; D005455:Fluorescent Antibody Technique; D006801:Humans; D008168:Lung / Q000201:enzymology; D008666:Metalloendopeptidases; D051381:Rats; D013552:Swine
chemical_list: D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes