Abstract
Angiotensin-converting enzyme (ACE) is an example of a membrane-bound protein, which is shed from the cell surface in a soluble form by a post-translational proteolytic cleavage event involving a secretase. The secretase cleavage site in somatic ACE has been mapped to Arg-1203 / Ser-1204, 24 residues proximal to the membrane-anchoring domain and the ADAM (‘a d isintegrin a nd m etalloprotease’) family of proteins may be involved in ACE shedding.
Keywords: ace, angiotensin, disintegrin, hypertension, metalloproteinase, proteolysis, secretase, shedding
Protein & Peptide Letters
Title: Secretase-Mediated Cell Surface Shedding of the Angiotensin-Converting Enzyme
Volume: 11 Issue: 5
Author(s): Edward T. Parkin, Anthony J. Turner and Nigel M. Hooper
Affiliation:
Keywords: ace, angiotensin, disintegrin, hypertension, metalloproteinase, proteolysis, secretase, shedding
Abstract: Angiotensin-converting enzyme (ACE) is an example of a membrane-bound protein, which is shed from the cell surface in a soluble form by a post-translational proteolytic cleavage event involving a secretase. The secretase cleavage site in somatic ACE has been mapped to Arg-1203 / Ser-1204, 24 residues proximal to the membrane-anchoring domain and the ADAM (‘a d isintegrin a nd m etalloprotease’) family of proteins may be involved in ACE shedding.
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Cite this article as:
Parkin T. Edward, Turner J. Anthony and Hooper M. Nigel, Secretase-Mediated Cell Surface Shedding of the Angiotensin-Converting Enzyme, Protein & Peptide Letters 2004; 11 (5) . https://dx.doi.org/10.2174/0929866043406544
DOI https://dx.doi.org/10.2174/0929866043406544 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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