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- W2182180814 startingPage "919" @default.
- W2182180814 abstract "Endothelin-converting enzyme is a phosphoramidon-sensitive membrane metallopeptidase that catalyses the final step in biosynthesis of the potent vasoactive endothelin peptides. Immunomagnetic separation technology and immunohistochemistry have been used to demonstrate the co-localisation of endothelin-converting enzyme with the established ectoenzyme, aminopeptidase N, on the surface of endothelial cells. Unlike aminopeptidase N, however, endothelin-converting enzyme is seen to associate in clusters on the plasma membrane which can be distinguished from caveolae both biochemically and immunologically. Pre-treatment of endothelial cells with the metallopeptidase inhibitors phosphoramidon or thiorphan in the range 0.01-100 microM produced a dose-dependent increase in the levels of endothelin-converting enzyme protein and its accumulation in an intracellular compartment. No corresponding change in the levels of endothelin-converting enzyme-1 mRNA was detected under these conditions, nor in the levels of the closely related metalloenzyme, endopeptidase-24.11. The phosphoramidon and thiorphan-dependent increase is not due to direct inhibition of endothelin-converting enzyme not endopeptidase-24.11 but, rather, to an inhibition of the selective turnover of endothelin-converting enzyme protein." @default.
- W2182180814 created "2016-06-24" @default.
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- W2182180814 date "1996-05-01" @default.
- W2182180814 modified "2023-10-15" @default.
- W2182180814 title "Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme levels and its redistribution from the plasma membrane to an intracellular compartment" @default.
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- W2182180814 doi "https://doi.org/10.1242/jcs.109.5.919" @default.
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