High affinity aldosterone binding sites (type I receptors) in rat heart

Clin Exp Pharmacol Physiol. 1987 Nov-Dec;14(11-12):859-66. doi: 10.1111/j.1440-1681.1987.tb02422.x.

Abstract

1. The use of the receptor stabilizing agent sodium molybdate, and of RU26988 to exclude [3H]-aldosterone binding from Type II glucocorticoid receptors, has enabled the characterization of high affinity Type I aldosterone binding sites in rat atrial and ventricular cytosols. 2. In adult male and female rats the affinity of binding (Kd 4 degrees C) is approximately 1-2 nmol/l for both atria and ventricles; specificity of binding is similar to that for Type I sites in classical aldosterone target tissues (aldosterone = corticosterone much greater than dexamethasone). 3. Levels of atrial Type I sites are higher than the corresponding levels in ventricle in both males and females, whereas for Type II (classical glucocorticoid) receptors the reverse is the case; levels of both Type I and Type II sites fall over the age range examined (40 days-6 months). 4. The physiological function(s) of cardiac Type I sites, and their in vivo mineralocorticoid or glucocorticoid selectivity, remain to be explored.

MeSH terms

  • Adrenalectomy
  • Aging / metabolism
  • Androstanols / pharmacology
  • Animals
  • Female
  • Male
  • Myocardium / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Receptors, Glucocorticoid / metabolism*
  • Receptors, Mineralocorticoid
  • Sex Factors

Substances

  • Androstanols
  • Receptors, Glucocorticoid
  • Receptors, Mineralocorticoid
  • RU 26988