Please use this identifier to cite or link to this item: https://doi.org/10.1016/0006-2952(93)90054-Z
Title: Degradation of angiotensin I in the endothelium and smooth muscle of the rat aorta
Authors: Sim, M.K. 
Issue Date: 1993
Source: Sim, M.K. (1993). Degradation of angiotensin I in the endothelium and smooth muscle of the rat aorta. Biochemical Pharmacology 45 (7) : 1524-1527. ScholarBank@NUS Repository. https://doi.org/10.1016/0006-2952(93)90054-Z
Abstract: In homogenates of the endothelium and smooth muscle cum adventitia of the rat aorta, exogenous angiotensin (ANG) I was found to be degraded to des-aspartate-ANG I (des-Asp-ANG I) instead of ANG II. ANG II and ANG III were not detectable in either of the homogenates after 5, 10 and 30 min of incubation with the decapeptide. However, both the homogenates were able to catalyse hippuryl-L-histidyl-L-leucine (HHL) to hippuric acid and the catalysis was completely inhibited by 3 μM captopril. The data show that the angiotensin converting enzyme (ACE) present in the homogenates of rat aorta, prepared by normal laboratory procedures, is not able to hydrolyse ANG I to ANG II. This finding has important consequences in the study of vascular ACE as the assay of the enzyme is often carried out using crude homogenate and HHL or other artificial substrates. In addition, the aminopeptidase that degraded ANG I to des-Asp-ANG I was not inhibited by either amastatin or bestatin, indicating that it was not aminopeptidase A or B. Together with the recent findings of other investigators which show that the de novo production of ANG II in vascular tissues is stimulated and inhibited by β- and α-agonists, respectively, our present data may suggest that production of vascular ANG II occurs only in intact tissues and is probably under adrenergic regulation.
Source Title: Biochemical Pharmacology
URI: http://scholarbank.nus.edu.sg/handle/10635/32157
ISSN: 00062952
DOI: 10.1016/0006-2952(93)90054-Z
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

24
checked on Apr 2, 2018

WEB OF SCIENCETM
Citations

21
checked on Apr 2, 2018

Page view(s)

94
checked on Mar 11, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.