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J. Biol. Chem., Vol. 277, Issue 15, 12499-12502, April 12, 2002
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§,
From the Departments of The Rh blood group proteins are well known as the
erythrocyte targets of the potent antibody response that causes
hemolytic disease of the newborn. 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 mediates uptake of ammonium across cell membranes.
Rh-associated glycoprotein carrier-mediated uptake, characterized with
the radioactive analog of ammonium [14C]methylamine (MA),
had an apparent EC50 of 1.6 mM and a maximum uptake rate (Vmax) of 190 pmol/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- and tetraethylammonium 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.
Pathology and Laboratory
Medicine and ¶ Physiology, University of Pennsylvania, School of
Medicine, Philadelphia, Pennsylvania 19104
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