Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9475
Title: Characterization of renal angiotensin-converting enzyme 2 in diabetic nephropathy.
Authors: Tikellis, Christos;Johnston, Colin I;Forbes, Josephine M;Burns, Wendy C;Burrell, Louise M;Risvanis, John;Cooper, Mark E
Affiliation: Department of Medicine, University of Melbourne, Austin and Repatriation Medical Centre, Melbourne, Australia.
Issue Date: 24-Feb-2003
Citation: Hypertension 2003; 41(3): 392-7
Abstract: ACE2, initially cloned from a human heart, is a recently described homologue of angiotensin-converting enzyme (ACE) but contains only a single enzymatic site that catalyzes the cleavage of angiotensin I to angiotensin 1-9 [Ang(1-9)] and is not inhibited by classic ACE inhibitors. It also converts angiotensin II to Ang(1-7). Although the role of ACE2 in the regulation of the renin-angiotensin system is not known, the renin-angiotensin system has been implicated in the pathogenesis of diabetic complications and in particular in diabetic nephropathy. Therefore, the aim of this study was to assess the possible involvement of this new enzyme in the kidney from diabetic Sprague-Dawley rats to compare and contrast it to ACE. ACE2 and ACE gene and protein expression were measured in the kidney after 24 weeks of streptozocin diabetes. ACE2 and ACE mRNA levels were decreased in diabetic renal tubules by approximately 50% and were not influenced by ACE inhibitor treatment with ramipril. By immunostaining, both ACE2 and ACE protein were localized predominantly to renal tubules. In the diabetic kidney, there was reduced ACE2 protein expression that was prevented by ACE inhibitor therapy. The identification of ACE2 in the kidney, its modulation in diabetes, and the recent description that this enzyme plays a biological role in the generation and degradation of various angiotensin peptides provides a rationale to further explore the role of this enzyme in various pathophysiological states including diabetic complications.
Internal ID Number: 12623933
URI: http://ahro.austin.org.au/austinjspui/handle/1/9475
DOI: 10.1161/01.HYP.0000060689.38912.CB
URL: http://www.ncbi.nlm.nih.gov/pubmed/12623933
Type: Journal Article
Subjects: Angiotensin-Converting Enzyme Inhibitors.pharmacology
Animals
Carboxypeptidases.analysis.genetics.metabolism
Diabetes Mellitus, Experimental.enzymology.genetics
Diabetic Nephropathies.enzymology.genetics
Immunohistochemistry
In Situ Hybridization
Kidney.enzymology
Kidney Tubules.enzymology
Male
Peptidyl-Dipeptidase A.analysis.biosynthesis.genetics
RNA, Messenger.analysis.biosynthesis
Ramipril.pharmacology
Rats
Rats, Sprague-Dawley
Appears in Collections:Journal articles

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


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