Expression of RhCG, a New Putative NH3/NH4 + Transporter, along the Rat Nephron

Eladari, Dominique; Cheval, Lydie; Quentin, Fabienne; Bertrand, Olivier; Mouro, I; Chérif-Zahar, Baya; Cartron, Jean‐Pierre; Paillard, Michel; Doucet, Alain; Chambrey, Régine

doi:10.1097/01.asn.0000025280.02386.9d

Cited by 124 publications

(118 citation statements)

References 29 publications

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“…These results, supported by crystallographic and functional studies demonstrating that AmtB, a bacterial member of the Amt/Mep/Rh superfamily, is a channel that conducts NH 3 [30,31], first identified Rh glycoproteins as members of an NH 3 channel family in mammals. In support of a physiological relevance for the capacity of RhBG and RhCG to transport NH 3 , it has been shown, at least in the kidney, that epithelial cells that exhibit the highest NH 3 permeability, namely intercalated cells of the collecting tubules [32], are those which express RhBG and RhCG [9][10][11]. Since ammonium transport may play different physiological roles in different organisms and in different tissues within the same organism, the findings that bacterial AmtB and mammalian Rh glycoproteins function as a gas channel for NH 3 should not rule out the possibility that other members of the Amt/Mep/Rh superfamily can function differently.…”

Section: Discussionmentioning

confidence: 98%

“…The pCEP4 vector was purchased from Invitrogen (Leek, The Netherlands). Rabbit polyclonal antisera raised against the cytoplasmic C-terminal of human RhBG (RhBG-Cter) and RhCG (RhCG-Cter) were described previously [9,11]. The LA18.18 anti-RhAG mouse monoclonal antibody was obtained from Dr A. E. Von dem Borne (Laboratory for Transfusion Science, Bloodbank Rotterdam, Rotterdam, the Netherlands).…”

Section: Methodsmentioning

confidence: 99%

“…HEK-293 cells, although of renal origin, were previously shown to lack endogenous expression of RhBG and RhCG [9,11]. These cells were stably transfected by the pCEP4-RhAG, pCEP4-RhBG and pCEP4-RhCG vectors.…”

Section: Stable Expression Of Recombinant Rhag Rhbg and Rhcg In Hek-mentioning

confidence: 99%

“…Interestingly, epithelial expression of RhBG and RhCG in the kidney is restricted to cells involved in ammonium secretion (connecting tubules and collecting ducts) and both proteins are expressed in the same cell types but with opposite polarity; RhBG is localized at the basolateral domain of the plasma membrane and RhCG at the apical domain [9][10][11]. In contrast, RhBG and RhCG are expressed in different cell types in the liver.…”

Section: Introductionmentioning

confidence: 99%

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Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells

Zidi-Yahiaoui

Mouro-Chanteloup

d'Ambrosio

et al. 2005

Biochemical Journal

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The mammalian Rh (Rhesus) protein family belongs to the Amt/ Mep (ammonia transporter/methylammonium permease)/Rh superfamily of ammonium transporters. Whereas RhCE, RhD and RhAG are erythroid specific, RhBG and RhCG are expressed in key organs associated with ammonium transport and metabolism. We have investigated the ammonium transport function of human RhBG and RhCG by comparing intracellular pH variation in wild-type and transfected HEK-293 (human embryonic kidney) cells and MDCK (Madin-Darby canine kidney) cells in the presence of ammonium (NH 4 + /NH 3 ) gradients. Stopped-flow spectrofluorimetry analysis, using BCECF [2 ,7 -bis-(2-carboxyethyl)-5(6)-carboxyfluorescein] as a pH-sensitive probe, revealed that all cells submitted to inwardly or outwardly directed ammonium gradients exhibited rapid alkalinization or acidification phases respectively, which account for ammonium movements in transfected and native cells. However, as compared with wildtype cells known to have high NH 3 lipid permeability, RhBGand RhCG-expressing cells exhibited ammonium transport characterized by: (i) a five to six times greater kinetic rateconstant; (ii) a weak temperature-dependence; and (iii) reversible inhibition by mercuric chloride (IC 50: 52 µM). Similarly, when subjected to a methylammonium gradient, RhBG-and RhCGexpressing cells exhibited kinetic rate constants greater than those of native cells. However, these constants were five times higher for RhBG as compared with RhCG, suggesting a difference in substrate accessibility. These results, indicating that RhBG and RhCG facilitate rapid and low-energy-dependent bi-directional ammonium movement across the plasma membrane, favour the hypothesis that these Rh glycoproteins, together with their erythroid homologue RhAG [Ripoche, Bertrand, Gane, Birkenmeier, Colin and Cartron (2005) Proc. Natl. Acad. Sci. U.S.A. 101, 17222-17227] constitute a family of NH 3 channels in mammalian cells.

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Section: Discussionmentioning

confidence: 98%

Section: Methodsmentioning

confidence: 99%

Section: Stable Expression Of Recombinant Rhag Rhbg and Rhcg In Hek-mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells

Zidi-Yahiaoui

Mouro-Chanteloup

d'Ambrosio

et al. 2005

Biochemical Journal

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“…The nonerythroid Rh glycoproteins, RhBG and RhCG, also transport ammonia (10 -16) and are expressed in a wide variety of tissues in which ammonia metabolism is important, including kidneys, liver, central nervous system, gastrointestinal tract, and skeletal muscles (17)(18)(19)(20)(21)(22)(23). In the kidney, RhCG is expressed in the distal convoluted tubule (DCT), connecting segment (CNT), initial collecting tubule (ICT), and collecting duct in both rat and mouse kidneys (19,21,24), and Rhcg expression in the outer medullary collecting duct (OMCD) and inner medullary collecting duct (IMCD) increases in response to chronic metabolic acidosis (24,25).…”

mentioning

confidence: 99%

Expression of the Ammonia Transporter, Rh C Glycoprotein, in Normal and Neoplastic Human Kidney

Han

Croker

Clapp

et al. 2006

Journal of the American Society of Nephrology

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Molecular Physiology of the Medullary Collecting Duct

Fenton

Prætorius

2011

Comprehensive Physiology

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The mammalian kidney is responsible for a multitude of homeostatic functions, which are mediated by both structural and functional diversity along the renal tubule. In this article, we focus on the major functions of the terminal portion of the renal tubule, the medullary collecting duct system. The role of the medullary collecting ducts in determining the composition of the final urine through controlled water, sodium, chloride, potassium and urea reabsorption, ammonia transport, and acid-base homeostasis is discussed. The molecular identity of the major channels and transporters that contribute to medullary collecting duct function are described in detail, including; aquaporins, urea transporters, the epithelial sodium channel (ENaC), the Na,K-ATPase, H-ATPase, Rh glycoproteins, and sodium bicarbonate transporters. Knowledge gained from studies in knockout mice is also discussed.

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Expression of RhCG, a New Putative NH3/NH4 + Transporter, along the Rat Nephron

Cited by 124 publications

References 29 publications

Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells

Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells

Expression of the Ammonia Transporter, Rh C Glycoprotein, in Normal and Neoplastic Human Kidney

Molecular Physiology of the Medullary Collecting Duct

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