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

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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

Document Type: Review Article


Affiliations: Proteolysis Research Group, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Publication date: October 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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