NDLI: Human Rhesus-associated glycoprotein mediates facilitated transport of NH3 into red blood cells

Content Provider	PubMed Central
Author	Pierre, Ripoche Bertrand, Olivier Gane, Pierre Birkenmeier, Connie Colin, Yves Cartron, Jean-pierre
Copyright Year	2004
Abstract	Rhesus (Rh) antigens are carried by a membrane complex that includes Rh proteins (D and CcEe), Rh-associated glycoproteins (RhAG), and accessory chains (LW and CD47) associated by noncovalent bonds. In heterologous expression systems, RhAG and its kidney orthologs function as ammonium transporters. In red blood cells (RBCs), it is generally accepted that NH3 permeates by membrane lipid diffusion. We have revisited these issues by studying RBC and ghosts from human and mouse genetic variants with defects of proteins that comprise the Rh complex. In both normal and mutant cells, stopped-flow analyses of intracellular pH changes in the presence of inwardly directed methylammonium (CH3NH+ 3+CH3NH2) or ammonium (NH+ 4+NH3) gradients showed a rapid alkalinization phase. Cells from human and mouse variants exhibited a decrease in their kinetic rate constants that was strictly correlated to the degree of reduction of their RhAG/Rhag expression level. Rate constants were not affected by a reduction of Rh, CD47, or LW. CH3NH2/NH3 transport was characterized by (i) a sensitivity to mercurials that is reversible by 2-mercaptoethanol and (ii) a reduction of alkalinization rate constants after bromelain digestion, which cleaves RhAG. The results show that RhAG facilitates CH3NH2/NH3 movement across the RBC membrane and represents a potential example of a gas channel in mammalian cells. In RBCs, RhAG may transport NH3 to detoxifying organs, like kidney and liver, and together with nonerythroid tissue orthologs may contribute to the regulation of the systemic acid–base balance.
Related Links	http://dx.doi.org/10.1073/pnas.0403704101
Starting Page	17222
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	49
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-12-07
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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