Title: Palmitoylation of the three isoforms of human endothelin-converting enzyme-1
Authors : Schweizer, Anja
Löffler, Bernd-Michael
Rohrer, Jack
Published in : Biochemical Journal
Volume(Issue) : 340
Issue : 3
Pages : 649
Pages to: 656
Publisher / Ed. Institution : Portland Press
Issue Date: 15-Jun-1999
License (according to publishing contract) : Licence according to publishing contract
Type of review: Peer review (Publication)
Language : English
Subject (DDC) : 572: Biochemistry
Abstract: Endothelin-converting enzyme-1 (ECE-1) is a membrane-bound metalloprotease that catalyses the conversion of inactive big endothelins into active endothelins. Here we have examined whether the three isoforms of human ECE-1 (ECE-1a, ECE-1b and ECE-1c) are modified by the covalent attachment of the fatty acid palmitate and have evaluated a potential functional role of this modification. To do this, wild-type and mutant enzymes were expressed and analysed by metabolic labelling with [3H]palmitate, immunoprecipitation and SDS/PAGE. All three ECE-1 isoforms were found to be palmitoylated via hydroxylamine-sensitive thioester bonds. In addition, the isoforms showed similar levels of acylation. Cys46 in ECE-1a, Cys58 in ECE-1b and Cys42 in ECE-1c were identified as sites of palmitoylation and each of these cysteines accounted for all the palmitoylation that occurred in the corresponding isoform. Immunofluorescence analysis demonstrated further that palmitoylated and non-palmitoylated ECE-1 isoforms had the same subcellular localizations. Moreover, complete solubility of the three isoforms in Triton X-100 revealed that palmitoylation does not target ECE-1 to cholesterol and sphingolipid-rich membrane domains or caveolae. The enzymic activities of ECE-1a, ECE-1b and ECE-1c were also not significantly affected by the absence of palmitoylation.
Departement: Life Sciences und Facility Management
Publication type: Article in scientific Journal
DOI : 10.1042/bj3400649
ISSN: 0264-6021
URI: https://digitalcollection.zhaw.ch/handle/11475/6848
Appears in Collections:Publikationen Life Sciences und Facility Management

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