Independent variation of β-adrenergic receptor binding and catecholamine-stimulated adenylate cyclase activity in rat erythrocytes

Michael E. Charness, David B. Bylund, Barbara S. Beckman, Morley D. Hollenberg, Solomon H. Snyder

Research output: Contribution to journalArticle

Abstract

Isoproterenol-stimulated adenylate cyclase activity in membrane preparations of reticulocyte-rich (90%) erythrocytes from phenylhydrazine-treated rats is 9 times greater than in untreated animals (1% reticulocytes); basal and fluoride-stimulated activities are also enhanced 2 and 4-fold respectively. In contrast, the number of β-adrenergic receptor sites detected by the binding of 125I-hydroxybenzylpindolol (125I-HYP) is increased only 40% in these same preparations. The dissociation constant (KD) of 125I-HYP and the IC50 of (-)-isoproterenol for receptor binding sites are unchanged, as is the EC50 of (-)-isoproterenol for activation of adenylate cyclase. The disproportionately large increase in the activity of the isoproterenol-sensitive adenylate cyclase, compared with the small increase in the number of 125I-HYP binding sites indicates that the functions of catecholamine recognition and consequent adenylate cyclase response can vary independently and suggest that the receptor and the cyclase may be autonomous molecular entities.

Original languageEnglish (US)
Pages (from-to)243-250
Number of pages8
JournalLife Sciences
Volume19
Issue number2
DOIs
StatePublished - Jul 15 1976

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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