AJP - Renal Physiology, Vol 253, Issue 1 21-F25, Copyright © 1987 by American Physiological Society

ARTICLES

Amiloride interacts with renal alpha- and beta-adrenergic receptors

M. J. Howard, M. D. Mullen and P. A. Insel

We have used radioligand binding techniques to assess whether amiloride and certain analogues of amiloride (ethylisopropyl amiloride and benzamil) can bind to adrenergic receptors in the kidney. We found that amiloride could compete for [3H]rauwolscine (alpha 2-adrenergic receptors), [3H]prazosin (alpha 1-adrenergic receptors), and [125I]iodocyanopindolol (beta-adrenergic receptors) binding in rat renal cortical membranes with inhibitor constants of 13.6 +/- 5.7, 24.4 +/- 7.4, and 83.6 +/- 13.5 microM, respectively. Ethylisopropyl amiloride and benzamil were from 2- to 25-fold more potent than amiloride in competing for radioligand binding sites in studies with these membranes. In addition, amiloride and the two analogues competed for [3H]prazosin sites on intact Madin-Darby canine kidney cells and amiloride blocked epinephrine-stimulated prostaglandin E2 production in these cells. We conclude that amiloride competes for binding to several classes of renal adrenergic receptors with a rank order of potency of alpha 2 greater than alpha 1 greater than beta. Binding to, and antagonism of, adrenergic receptors occurs at concentrations of amiloride that are lower than previously observed "nonspecific" interactions of this agent.

This article has been cited by other articles:

				J. L. Fisher Amiloride Inhibition of gamma -Aminobutyric AcidA Receptors Depends upon the alpha Subunit Subtype Mol. Pharmacol., June 1, 2002; 61(6): 1322 - 1328. [Abstract] [Full Text] [PDF]