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J. Biol. Chem., Vol. 278, Issue 31, 28719-28726, August 1, 2003

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Intracellular Na⁺ Regulates Dopamine and Angiotensin II Receptors Availability at the Plasma Membrane and Their Cellular Responses in Renal Epithelia^*

Riad Efendiev  , Claudia E. Budu  , Angel R. Cinelli ¶, Alejandro M. Bertorello || and Carlos H. Pedemonte  **

From the College of Pharmacy, University of Houston, Houston, Texas 77204, ^¶Department of Anatomy and Cell Biology, State University of New York, Brooklyn, New York 11203, and ^||Department of Medicine, Atherosclerosis Research Unit, Karolinska Institutet, Karolinska Hospital, Stockholm S-17176, Sweden

The balance and cross-talk between natruretic and antinatruretic hormone receptors plays a critical role in the regulation of renal Na⁺ homeostasis, which is a major determinant of blood pressure. Dopamine and angiotensin II have antagonistic effects on renal Na⁺ and water excretion, which involves regulation of the Na⁺,K⁺-ATPase activity. Herein we demonstrate that angiotensin II (Ang II) stimulation of AT1 receptors in proximal tubule cells induces the recruitment of Na⁺,K⁺-ATPase molecules to the plasmalemma, in a process mediated by protein kinase C and interaction of the Na⁺,K⁺-ATPase with adaptor protein 1. Ang II stimulation led to phosphorylation of the subunit Ser-11 and Ser-18 residues, and substitution of these amino acids with alanine residues completely abolished the Ang II-induced stimulation of Na⁺,K⁺-ATPase-mediated Rb⁺ transport. Thus, for Ang II-dependent stimulation of Na⁺,K⁺-ATPase activity, phosphorylation of these serine residues is essential and may constitute a triggering signal for recruitment of Na⁺,K⁺-ATPase molecules to the plasma membrane. When cells were treated simultaneously with saturating concentrations of dopamine and Ang II, either activation or inhibition of the Na⁺,K⁺-ATPase activity was produced dependent on the intracellular Na⁺ concentration, which was varied in a very narrow physiological range (9–19 mM). A small increase in intracellular Na⁺ concentrations induces the recruitment of D1 receptors to the plasma membrane and a reduction in plasma membrane AT1 receptors. Thus, one or more proteins may act as an intracellular Na⁺ concentration sensor and play a major regulatory role on the effect of hormones that regulate proximal tubule Na⁺ reabsorption.

Received for publication, April 10, 2003 , and in revised form, May 16, 2003.

^* This work was supported in part by National Institutes of Health Grant DK53460, American Heart Association Grant 0050801Y, and Swedish Research Council Grant 10860. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Contributed equally to this publication.

^** To whom correspondence should be addressed: University of Houston, College of Pharmacy, 4800 Calhoun Rd., Bldg. SR2, Rm. 555, Houston, TX 77204. Tel.: 713-743-1211; Fax: 713-743-1229; E-mail: cpedemonte{at}uh.edu.

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