Document Detail


Primary role of angiotensin-converting enzyme-2 in cardiac production of angiotensin-(1-7) in transgenic Ren-2 hypertensive rats.
MedLine Citation:
PMID:  17308000     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Angiotensin-converting enzyme-2 (ACE2) converts angiotensin II (ANG II) to angiotensin-(1-7) [ANG-(1-7)], and this enzyme may serve as a key regulatory juncture in various tissues. Although the heart expresses ACE2, the extent that the enzyme participates in the cardiac processing of ANG II and ANG-(1-7) is equivocal. Therefore, we utilized the Langendorff preparation to characterize the ACE2 pathway in isolated hearts from male normotensive Sprague-Dawley [Tg((-))] and hypertensive [mRen2]27 [Tg((+))] rats. During a 60-min recirculation period with 10 nM ANG II, the presence of ANG-(1-7) was assessed in the cardiac effluent. ANG-(1-7) generation from ANG II was similar in both the normal and hypertensive hearts [Tg((-)): 510 +/- 55 pM, n=20 vs. Tg((+)): 497 +/- 63 pM, n=14] with peak levels occurring at 30 min after administration of the peptide. ACE2 inhibition (MLN-4760, 1 microM) significantly reduced ANG-(1-7) production by 83% (57 +/- 19 pM, P<0.01, n=7) in the Tg((+)) rats, whereas the inhibitor had no significant effect in the Tg((-)) rats (285 +/- 53 pM, P>0.05, n=10). ACE2 activity was found in the effluent of perfused Tg((-)) and Tg((+)) hearts, and it was highly associated with ACE2 protein expression (r=0.78). This study is the first demonstration for a direct role of ACE2 in the metabolism of cardiac ANG II in the hypertrophic heart of hypertensive rats. We conclude that predominant expression of cardiac ACE2 activity in the Tg((+)) may be a compensatory response to the extensive cardiac remodeling in this strain.
Authors:
Aaron J Trask; David B Averill; Detlev Ganten; Mark C Chappell; Carlos M Ferrario
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-02-16
Journal Detail:
Title:  American journal of physiology. Heart and circulatory physiology     Volume:  292     ISSN:  0363-6135     ISO Abbreviation:  Am. J. Physiol. Heart Circ. Physiol.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-12     Completed Date:  2007-08-02     Revised Date:  2012-07-03    
Medline Journal Info:
Nlm Unique ID:  100901228     Medline TA:  Am J Physiol Heart Circ Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  H3019-24     Citation Subset:  IM    
Affiliation:
Hypertension and Vascular Research Center, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA. atrask@wfubmc.edu
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MeSH Terms
Descriptor/Qualifier:
Angiotensin II / metabolism*
Angiotensin-Converting Enzyme Inhibitors / pharmacology
Animals
Animals, Genetically Modified
Cardiomegaly / enzymology,  genetics,  metabolism*,  pathology
Disease Models, Animal
Half-Life
Hypertension / complications,  enzymology,  genetics,  metabolism*,  pathology
Imidazoles / pharmacology
Kinetics
Leucine / analogs & derivatives,  pharmacology
Male
Mice
Myocardium / enzymology,  metabolism*,  pathology
Peptide Fragments / metabolism*
Peptidyl-Dipeptidase A / metabolism*
Rats
Rats, Sprague-Dawley / genetics
Renin / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
HL51952/HL/NHLBI NIH HHS; HL56973/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/2-(1-carboxy-2-(3-(3,5-dichlorobenzyl)-3H-imidazol-4-yl)ethylamino)-4-methylpentanoic acid; 0/Angiotensin-Converting Enzyme Inhibitors; 0/Imidazoles; 0/Peptide Fragments; 0/Ren2 protein, mouse; 0/angiotensin I (1-7); 11128-99-7/Angiotensin II; 61-90-5/Leucine; EC 3.4.15.1/Peptidyl-Dipeptidase A; EC 3.4.17.-/angiotensin converting enzyme 2; EC 3.4.23.15/Renin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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