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Journal of Cell Science, Vol 109, Issue 5 919-928, Copyright © 1996 by Company of Biologists
JOURNAL ARTICLES |
K Barnes, K Shimada, M Takahashi, K Tanzawa and AJ Turner
Department of Biochemistry and Molecular Biology, University of Leeds, UK.
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.
This article has been cited by other articles:
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L. A. Dawson, N. J. Maitland, P. Berry, A. J. Turner, and B. A. Usmani Expression and localization of endothelin-converting enzyme-1 in human prostate cancer. Experimental Biology and Medicine, June 1, 2006; 231(6): 1106 - 1110. [Abstract] [Full Text] [PDF]
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K. J. MacLeod, R. D. Husain, D. A. Gage, and K. Ahn Constitutive Phosphorylation of Human Endothelin-converting Enzyme-1 Isoforms J. Biol. Chem., November 22, 2002; 277(48): 46355 - 46363. [Abstract] [Full Text] [PDF]
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 D. Russo, X. Wu, C. M. Redman, and S. Lee Expression of Kell blood group protein in nonerythroid tissues Blood, July 1, 2000; 96(1): 340 - 346. [Abstract] [Full Text] [PDF]
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N. Emoto, Y. Nurhantari, H. Alimsardjono, J. Xie, T. Yamada, M. Yanagisawa, and M. Matsuo Constitutive Lysosomal Targeting and Degradation of Bovine Endothelin-converting Enzyme-1a Mediated by Novel Signals in Its Alternatively Spliced Cytoplasmic Tail J. Biol. Chem., January 15, 1999; 274(3): 1509 - 1518. [Abstract] [Full Text] [PDF]
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 O Valdenaire, A Barret, A Schweizer, E Rohrbacher, F Mongiat, F Pinet, P Corvol, and C Tougard Two di-leucine-based motifs account for the different subcellular localizations of the human endothelin-converting enzyme (ECE-1) isoforms J. Cell Sci., January 9, 1999; 112(18): 3115 - 3125. [Abstract] [PDF]
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 F. D. Russell, J. N. Skepper, and A. P. Davenport Human Endothelial Cell Storage Granules : A Novel Intracellular Site for Isoforms of the Endothelin-Converting Enzyme Circ. Res., August 10, 1998; 83(3): 314 - 321. [Abstract] [Full Text] [PDF]
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 K. Barnes, C. Brown, and A. J. Turner Endothelin-Converting Enzyme: Ultrastructural Localization and Its Recycling From the Cell Surface Hypertension, January 1, 1998; 31(1): 3 - 9. [Abstract] [Full Text] [PDF]
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K. J. MacLeod, R. S. Fuller, J. D. Scholten, and K. Ahn Conserved Cysteine and Tryptophan Residues of the Endothelin-converting Enzyme-1 CXAW Motif Are Critical for Protein Maturation and Enzyme Activity J. Biol. Chem., August 10, 2001; 276(33): 30608 - 30614. [Abstract] [Full Text] [PDF]
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