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    Rhbg Rhesus blood group-associated B glycoprotein [ Mus musculus (house mouse) ]

    Gene ID: 58176, updated on 21-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Utilizing a structural homology analysis to AmtB, we have identified residues in Rhbg that are implicated in ion transport function. We introduced mutations into these residues and evaluated their function using measurements of intracellular pH (pHi), surface pH (pHs), and whole cell currents (I) that can distinguish between NH3 and NH4+ signals. Our results identified critical amino acids that affect transport.

    Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.
    Abdulnour-Nakhoul S, Le T, Rabon E, Hamm LL, Nakhoul NL., Free PMC Article

    03/22/2017
    We characterized ammonia and ammonium (NH3/NH4 (+)) transport by the rhesus-associated (Rh) glycoproteins RhAG, Rhbg, and Rhcg expressed in Xenopus oocytes. We used ion-selective microelectrodes and two-electrode voltage clamp to measure changes in intracellular pH, surface pH, and whole cell currents induced by NH3/NH4 (+) and methyl amine/ammonium (MA/MA(+)).

    Mechanisms of ammonia and ammonium transport by rhesus-associated glycoproteins.
    Caner T, Abdulnour-Nakhoul S, Brown K, Islam MT, Hamm LL, Nakhoul NL., Free PMC Article

    12/10/2015
    Rh B Glycoprotein (Rhbg) and Rh C Glycoprotein (Rhcg) are identified as ammonia transporters. They are expressed in specific cell populations and membrane domains in distal renal epithelial cells, where they facilitate ammonia secretion.

    Ammonia transport in the kidney by Rhesus glycoproteins.
    Weiner ID, Verlander JW., Free PMC Article

    07/19/2014
    Rhbg is critically important in the renal response to metabolic acidosis. in mice with intact Rhbg expression, metabolic acidosis does not induce maximal changes in PEPCK, NHE-3, and GS expression despite the presence of persistent metabolic acidosis.

    Effect of collecting duct-specific deletion of both Rh B Glycoprotein (Rhbg) and Rh C Glycoprotein (Rhcg) on renal response to metabolic acidosis.
    Lee HW, Verlander JW, Handlogten ME, Han KH, Weiner ID., Free PMC Article

    05/3/2014
    highly expressed in specific cells in the male reproductive tract

    Expression of the rhesus glycoproteins, ammonia transporter family members, RHCG and RHBG in male reproductive organs.
    Lee HW, Verlander JW, Handlogten ME, Han KH, Cooke PS, Weiner ID., Free PMC Article

    03/22/2014
    It was concluded that hypokalemia increases Rhbg expression in intercalated cells in the cortex and outer medulla and that intercalated cell Rhbg expression is necessary for the normal increase in renal ammonia excretion in response to hypokalemia.

    Intercalated cell-specific Rh B glycoprotein deletion diminishes renal ammonia excretion response to hypokalemia.
    Bishop JM, Lee HW, Handlogten ME, Han KH, Verlander JW, Weiner ID., Free PMC Article

    05/4/2013
    These data indicate that transport of NH(4)(+) and methyl ammonium (+) by Rhbg is pH sensitive.

    pH sensitivity of ammonium transport by Rhbg.
    Nakhoul NL, Abdulnour-Nakhoul SM, Schmidt E, Doetjes R, Rabon E, Hamm LL., Free PMC Article

    01/8/2011
    Rhbg in connecting segment and principal cells may contribute to renal ammonia excretion

    Role of the Rhesus glycoprotein, Rh B glycoprotein, in renal ammonia excretion.
    Bishop JM, Verlander JW, Lee HW, Nelson RD, Weiner AJ, Handlogten ME, Weiner ID., Free PMC Article

    12/4/2010
    Rhbg and Rhcg may contribute to bronchial epithelial cell ammonia metabolism and suggest that they do not contribute to pulmonary carbon dioxide transport.

    Expression of the gas-transporting proteins, Rh B glycoprotein and Rh C glycoprotein, in the murine lung.
    Han KH, Mekala K, Babida V, Kim HY, Handlogten ME, Verlander JW, Weiner ID., Free PMC Article

    01/21/2010
    Characterization of the role of Rhbg in ammonium ion transport using voltage clamp techniques.

    Characteristics of renal Rhbg as an NH4(+) transporter.
    Nakhoul NL, Dejong H, Abdulnour-Nakhoul SM, Boulpaep EL, Hering-Smith K, Hamm LL.

    01/21/2010
    mIMCD-3 cells express a basolateral electroneutral NH4+/H+ exchange activity that may be mediated by RhBG.

    Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mIMCD-3).
    Handlogten ME, Hong SP, Westhoff CM, Weiner ID.

    01/21/2010
    These results strongly suggest that RhBG and RhCG transport ammonia by an electroneutral process that involves NH4(+)/H+ exchange resulting in net NH3 translocation.

    Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG.
    Mak DO, Dang B, Weiner ID, Foskett JK, Westhoff CM., Free PMC Article

    01/21/2010
    concluded that Rhbg is not a critical determinant of NH(4)(+) excretion by the kidney and of NH(4)(+) detoxification by the liver in vivo

    Genetic ablation of Rhbg in the mouse does not impair renal ammonium excretion.
    Chambrey R, Goossens D, Bourgeois S, Picard N, Bloch-Faure M, Leviel F, Geoffroy V, Cambillau M, Colin Y, Paillard M, Houillier P, Cartron JP, Eladari D.

    01/21/2010
    Review. Animal studies show Rhbg has a role in transmembrane NH3 or NH4+ transport in epithelial cells. The absence of distal tubular acidosis or hyperammonemia in Rhbg KO mice raises new questions about the physiological significance of this protein.

    Rh glycoproteins in epithelial cells: lessons from rat and mice studies.
    Chambrey R, Goossens D, Quentin F, Eladari D.

    01/21/2010
    RhBG-mediated transport is an electroneutral process that is driven by the NH4+ concentration and the transmembrane H+ gradient, effectively exchanging NH4+ for H+ in a process that results in transport of net NH3.

    Transport characteristics of mammalian Rh and Rh glycoproteins expressed in heterologous systems.
    Westhoff CM, Wylie DE.

    01/21/2010
    Basolateral RhBG is expressed by perivenous hepatocytes, where it may mediate ammonium uptake

    Localization of the ammonium transporters, Rh B glycoprotein and Rh C glycoprotein, in the mouse liver.
    Weiner ID, Miller RT, Verlander JW.

    01/21/2010
    RhBG and RhCG are present in a major site of ammonia secretion in the kidney, i.e., the CNT and CD, in agreement with their putative role in ammonium transport.

    RhBG and RhCG, the putative ammonia transporters, are expressed in the same cells in the distal nephron.
    Quentin F, Eladari D, Cheval L, Lopez C, Goossens D, Colin Y, Cartron JP, Paillard M, Chambrey R.

    01/21/2010
    Rhbg transport of NH4+ is electrogenic. Methylammonium is transported by Rhbg. NH4+ transport by Rhbg is saturated at high concentrations with Michaelis-Menten kinetics.

    Electrogenic ammonium transport by renal Rhbg.
    Nakhoul NL, Schmidt E, Abdulnour-Nakhoul SM, Hamm LL.

    01/21/2010
    The expression of the ammonia transporter family members Rh B glycoprotein (RhBG) and Rh C glycoprotein (RhCG) in the mouse gastrointestinal tract.

    Expression of the ammonia transporter proteins Rh B glycoprotein and Rh C glycoprotein in the intestinal tract.
    Handlogten ME, Hong SP, Zhang L, Vander AW, Steinbaum ML, Campbell-Thompson M, Weiner ID.

    01/21/2010
    Review. Rhbg is in distal nephron sites responsible for NH3 secretion and in perivenous hepatocyte basolateral plasma membrane. Cetabolic acidosis does not affect Rhbg, so it may be either an ammonia- sensor or mediate other roles.

    Expression of the non-erythroid Rh glycoproteins in mammalian tissues.
    Weiner ID., Free PMC Article

    01/21/2010
    Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney.

    Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney.
    Verlander JW, Miller RT, Frank AE, Royaux IE, Kim YH, Weiner ID.

    01/21/2010
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