Angiotensin converting enzyme activity is present in the endothelium-denuded aorta.
Angiotensin converting enzyme activity was measured in intact aortic rings utilizing the synthetic tripeptide [3H]-benzoyl-Phe-Ala-Pro as the substrate. Intact aortic rings possessed angiotensin converting enzyme activity which was blocked by captopril. Enzyme activity was reduced by approximately 30% after removal of the endothelium by chemical or mechanical methods. The remaining activity was also captopril-sensitive. These results suggest that in addition to endothelium, angiotensin converting enzyme activity is present in other vascular cells and may contribute to the metabolism of angiotensin I generated within the vessel wall.
Pipili
E
E
University of Patras, School of Medicine, Department of Pharmacology, Greece.
Manolopoulos
V G
VG
Catravas
J D
JD
Maragoudakis
M E
ME
D000109:Acetylcholine / Q000494:pharmacology; D000803:Angiotensin I / Q000096:biosynthesis; D000818:Animals; D001013:Aorta, Thoracic / Q000201:enzymology*; D004730:Endothelium, Vascular / Q000201:enzymology; D066298:In Vitro Techniques; D008297:Male; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D051381:Rats; D011921:Rats, Inbred WKY
D000803:Angiotensin I; D007703:Peptidyl-Dipeptidase A; D000109:Acetylcholine