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. 1995;16(6):1073-8.
doi: 10.1016/0196-9781(95)00082-u.

Angiotensin and bradykinin metabolism by peptidases identified in skeletal muscle

P E Ward  1 , J S Russell, P L Vaghy
Affiliations

Angiotensin and bradykinin metabolism by peptidases identified in skeletal muscle

P E Ward et al. Peptides. 1995.

Abstract

We have identified angiotensin-converting enzyme, neutral endopeptidase-24.11, and aminopeptidase M in a purified glycoprotein fraction of rabbit skeletal muscle membranes. The identification was based on substrate specificity and sensitivity to selective inhibitors. Angiotensin I metabolism was due to angiotensin-converting enzyme-mediated conversion to angiotensin II and neutral endopeptidase-24.11-mediated conversion to angiotensin(1-7). Bradykinin was degraded by angiotensin-converting enzyme and neutral endopeptidase-24.11; angiotensin II by neutral endopeptidase-24.11; and angiotensin III by neutral endopeptidase-24.11 and aminopeptidase M. Thus, the effects of angiotensins and kinins on skeletal muscle blood flow and metabolism may be regulated by local angiotensin-converting enzyme, neutral endopeptidase-24.11, and aminopeptidase M.

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