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Demonstration of Specific High Affinity Receptors for Aldosterone in Cytosol of Rat Colon^*

HENRY J. BINDER, ALLAN WHITE, DIANE WHITING and JOHN HAYSLETT

Department of Internal Medicine, Yale University New Haven, Connecticut 06510;
The Department of Physiology and Biophysics, Faculty of Medicine, University of Chile Santiago, Chile

Address all correspondence and requests for reprints to: Henry J. Binder, M.D., Department of Internal Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06510.

Abstract

Since both aldosterone and glucocorticoids increase cation transport in rat distal colon, and a specific glucocorticoid high affinity cytosolic receptor has been indentified in this tissue, it was possible that the action of aldosterone was dependent on interaction with the glucocorticoid receptor. Studies were, therefore, performed to determine whether a specific high affinity receptor for aldosterone was present in rat distal colon.

At 4 C, aldosterone binding was saturable and exhibited a high affinity site with an apparent K_d of 6.2 ± 0.9 x 10^–10 M and a calculated number of binding sites of 57.2 ± 10.8 fmol/mg cytosol protein. Scatchard plot analysis also revealed a low affinity site with a K_d of 5.9 ± 1.1 x 10_–8 M and 961 ± 191 fmol/mg cytosol protein-binding sites. Competitive binding studies demonstrated that the high affinity binding protein was specific for aldosterone, compared to either dexamethasone or RU-28362.

Since a specific high affinity receptor protein for aldosterone is present in rat distal colon, these data are consistent with a direct action of aldosterone that is independent of the glucocorticoid receptor system. (Endocrinology 118: 628–631, 1986)

Footnotes

^* This work was supported by USPHS Research Grants AM-18061 and AM-18777 from the NIADDK.

Supported by a Pan American Health Organization Fellowship.

Received January 11, 1985.

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