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Papers In Press, published online ahead of print February 22, 2002
J. Biol. Chem, 10.1074/jbc.C200060200
Submitted on January 29, 2002
Revised on February 21, 2002
Accepted on February 22, 2002

Identification of the erythrocyte Rh-blood group glycoprotein as a mammalian ammonium transporter

Connie M. Westhoff, Michelle Ferreri-Jacobia, Don-On Daniel Mak, and J. Kevin Foskett

Physiology and Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104

Corresponding Author: westhoff{at}mail.med.upenn.edu

The Rh blood group proteins are well known as the erythrocyte targets of the potent antibody response that causes hemolytic disease of the newborn (HDN). These proteins have been described in molecular detail, however, little is known about their function. A transport function is suggested by their predicted structure and from phylogenetic analysis. To obtain evidence for a role in solute transport, we expressed Rh proteins in Xenopus oocytes, and now demonstrate that the erythroid Rh-associated glycoprotein (RhAG) mediates uptake of ammonium across cell membranes. RhAG carrier-mediated uptake, characterized with the radioactive analogue of ammonium [14C] methylamine (MA), had an apparent EC50 of 1.6 mM and a maximum uptake rate (Vmax) of 190 pmole/oocyte/min. Uptake was independent of the membrane potential and the Na+ gradient. MA transport was stimulated by raising extracellular pH or by lowering intracellular pH, suggesting that uptake was coupled to an outwardly-directed H+ gradient. MA uptake was insensitive to additions of amiloride, amine-containing compounds tetramethyl- (TMA) and tetraethyl- (TEA) ammonium chloride, glutamine, and urea. However, MA uptake was significantly antagonized by ammonium chloride with inhibition kinetics (IC50=1.14 mM) consistent with the hypothesis that the uptake of MA and ammonium involves a similar H+-coupled counter-transport mechanism.


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