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J. Biol. Chem., Vol. 279, Issue 16, 15975-15983, April 16, 2004

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NH₃ Is Involved in the Transport Induced by the Functional Expression of the Human Rh C Glycoprotein^*

Naziha Bakouh, Fatine Benjelloun, Philippe Hulin, Franck Brouillard, Aleksander Edelman, Baya Chérif-Zahar, and Gabrielle Planelles

From the INSERM U 467, Université Paris V, Faculté de Médecine Necker-Enfants Malades, 75015 Paris, France

Renal ammonium (NH₃ + ) transport is a key process for body acid-base balance. It is well known that several ionic transport systems allow transmembrane translocation without high specificity , but it is still debated whether NH₃, and more generally, gas, may be transported by transmembrane proteins. The human Rh glycoproteins have been proposed to mediate ammonium transport. Transport of and/or NH₃ by the epithelial Rh C glycoprotein (RhCG) may be of physiological importance in renal ammonium excretion because RhCG is mainly expressed in the distal nephron. However, RhCG function is not yet established. In the present study, we search for ammonium transport by RhCG. RhCG function was investigated by electrophysiological approaches in RhCG-expressing Xenopus laevis oocytes. In the submillimolar concentration range, NH₄Cl exposure induced inward currents (I_AM) in voltage-clamped RhCG-expressing cells, but not in control cells. At physiological extracellular pH (pH_o) = 7.5, the amplitude of I_AM increased with NH₄Cl concentration and membrane hyperpolarization. The amplitude of I_AM was independent of external Na⁺ or K⁺ concentrations but was enhanced by alkaline pH_o and decreased by acid pH_o. The apparent affinity of RhCG for was affected by NH₃ concentration and by changing pH_o, whereas the apparent affinity for NH₃ was unchanged by pH_o, consistent with direct NH₃ involvement in RhCG function. The enhancement of methylammonium-induced current by NH₃ further supported this conclusion. Exposure to 500 µM NH₄Cl induced a biphasic intracellular pH change in RhCG-expressing oocytes, consistent with both NH₃ and enhanced influx. Our results support the hypothesis of a specific role for RhCG in NH₃ and transport.

Received for publication, August 4, 2003 , and in revised form, January 28, 2004.

^* This work was supported in part by INSERM and by Necker-Enfants Malades Faculty of Medicine. 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.

Supported by fellowships from Vaincre la Mucoviscidose and Association Mucoviscidose, ABCF Proteine.

To whom correspondence should be addressed: INSERM U 467, Université Paris V, Faculté de Médecine Necker-Enfants Malades, 156 rue de Vaugirard, 75015 Paris, France. Tel.: 33-1-40-61-56-20; Fax: 33-1-40-61-55-91; E-mail: planelle{at}necker.fr.

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