(Circulation. 1995;91:1461-1471.)
© 1995 American Heart Association, Inc.
Articles |
Regulation, Chamber Localization, and Subtype Distribution of Angiotensin II Receptors in Human Hearts
From the Department of Internal Medicine/Cardiology and Angiology (V.R.-Z., A. Heymann, P.B., M.N., E.F.) and the Department of Cardiovascular Surgery (N.F., R.H.), Free University of Berlin, Klinikum Rudolf Virchow and German Heart Institute Berlin; the Molecular Neurobiology Working Group (A.R.), Institute of Neuropsychopharmacology, Free University of Berlin; and the Federal Institute for Drugs and Medical Devices (C.S., A. Hildebrandt), Berlin.
Correspondence to PD Dr Vera Regitz-Zagrosek, Department of Internal Medicine/Cardiology, German Heart Institute Berlin, Augustenburger Platz 1, 13353 Berlin, FRG.
Background To assess the chamber localization, subtype distribution, and regulation of human myocardial angiotensin II receptors in heart failure, we determined the binding of angiotensin II, Sar1Ile8–angiotensin II, and the subtype-specific antagonists Dup 753 (AT1-specific) and PD 123319 (AT2-specific) in atria from patients with normal (left ventricular ejection fraction >55%) or moderately impaired (left ventricular ejection fraction 30% to 55%) cardiac function and in atria and ventricles from explanted end-stage failing hearts. Sarcolemmal and combined fractions, the latter including internalized receptors, were studied. In addition, AT1 mRNA content was analyzed by polymerase chain reaction after reverse transcription.
Methods and Results The number of angiotensin II binding sites (Bmax) in sarcolemmal fractions was significantly reduced in explanted end-stage failing hearts in comparison with control subjects and moderate heart failure (Bmax 3.9±0.8 versus 11.2±1.7 and 9.6±0.8 fmol/mg protein, respectively). A comparable 65% reduction in receptor numbers was found in combined fractions from end-stage failing hearts, indicating that the loss of binding sites was not due to their internalization. The dissociation constants were comparable in sarcolemmal and combined fractions and in nonfailing and failing hearts, ranging from 0.5±0.2 to 1.2±0.5 nmol/L. In nonfailing hearts, 69±4% of binding sites were blocked by the subtype-2–specific inhibitor PD 123319 and were therefore classified as AT2; 33±5% were blocked by the subtype-1–specific inhibitor DUP 753 and thus classified as subtype 1. In explanted hearts, comparable ratios of 66±5% AT2 sites and 34±5% AT1 sites were found. AT1 cDNA amplification signals by polymerase chain reaction were reduced to about one third of the level in control subjects in end-stage failing hearts.
Conclusions Angiotensin II receptors in human myocardium are present in relatively low numbers, and AT2 is the predominant subtype. A significant loss of angiotensin II receptors occurs in end stage but not in moderate heart failure. The loss of receptors affects both subtypes to a comparable degree. The data suggest that the decrease in receptor density is due to a decrease in steady-state mRNA abundance.
Key Words: angiotensin • RNA • heart failure • binding sites
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