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Localization and biochemical characterization of endothelin-converting enzyme
K Barnes1, L J Murphy, M Takahashi
1Department of Biochemistry and Molecular Biology, University of Leeds, England.
Journal of Cardiovascular Pharmacology
|January 1, 1995
Summary
Endothelin-converting enzyme (ECE) is found on the cell surface of endothelial cells, not enriched in lung endothelial membranes. ECE activity co-localizes with aminopeptidase-N on plasma membranes.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- Endothelin-converting enzyme (ECE) plays a crucial role in the endothelin pathway.
- Understanding ECE localization is vital for endothelial cell function research.
Purpose of the Study:
- To investigate the cellular and subcellular localization of endothelin-converting enzyme (ECE).
- To compare ECE distribution with angiotensin-converting enzyme (ACE) and aminopeptidase-N (AP-N) in endothelial cells.
Main Methods:
- Biochemical assays to measure enzyme activity.
- Immunomagnetic separation of endothelial cell membranes.
- Immunofluorescence microscopy using a monoclonal antibody against ECE.
- Enzyme activity assays in cell lines and tissue samples.
Main Results:
- Phosphoramidon-sensitive ECE activity was not enriched in porcine lung luminal endothelial membranes, unlike ACE.
- ECE activity co-localized with aminopeptidase-N activity on EA.hy926 plasma membranes.
- Immunofluorescence confirmed ECE presence on the cell surface of endothelial cell lines.
Conclusions:
- ECE is primarily located on the cell surface of endothelial cells.
- ECE localization differs from ACE in porcine lung endothelium.
- ECE and AP-N share co-localization on the plasma membrane of endothelial cell lines.
