Dissecting the role of chymase in angiotensin II formation and heart and blood vessel diseases.
Inhibition of angiotensin II action or its formation by angiotensin-converting enzyme has been highly successful in the treatment of cardiovascular diseases. Since the identification of chymase as a major angiotensin II-forming enzyme in the human heart and its vessels more than a decade ago, numerous studies have sought to understand the importance of this enzyme in tissue angiotensin II formation and in the pathogenesis of hypertension, congestive heart failure, and vascular disease. Recent studies show that chymase and angiotensin-converting enzyme regulate angiotensin II production in distinct tissue compartments and that, in the pathogenesis of cardiovascular diseases, chymase-dependent effects extend beyond its ability to regulate tissue angiotensin II levels.
Dell'Italia
Louis J
LJ
Department of Medicine, Division of Cardiovascular Disease, Birmingham Veteran Affairs Medical Center, University of Alabama at Birmingham, University Station, Birmingham, Alabama 35295-007, USA. Dell'Italia@physiology.uab.edu
Husain
Ahsan
A
D000803:Angiotensin I / Q000502:physiology; D000804:Angiotensin II / Q000097:blood*; D001161:Arteriosclerosis / Q000201:enzymology; D006332:Cardiomegaly / Q000209:etiology; D002318:Cardiovascular Diseases / Q000188:drug therapy / Q000201:enzymology* / Q000209:etiology*; D053818:Chymases; D006331:Heart Diseases / Q000188:drug therapy / Q000201:enzymology*; D006333:Heart Failure / Q000209:etiology; D006801:Humans; D006973:Hypertension / Q000209:etiology; D007703:Peptidyl-Dipeptidase A / Q000502:physiology*; D012697:Serine Endopeptidases / Q000502:physiology*
D000804:Angiotensin II; D000803:Angiotensin I; D007703:Peptidyl-Dipeptidase A; D012697:Serine Endopeptidases; D053818:Chymases