Secretase-Mediated Cell Surface Shedding of the Angiotensin-Converting Enzyme

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.

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