ArticleAmerican journal of physiology. Cell physiology2010
Substrate specificity of Rhbg: ammonium and methyl ammonium transport.
Article in American journal of physiology. Cell physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Mutations in ammonia transporter RhBG that impair NHThe Journal of physiology · 2026Article
- Rhbg interaction with CA-IV and its effects on NHAmerican journal of physiology. Cell physiology · 2025Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Effects of chronic hypercapnia on ammonium transport in the mouse kidney.Physiological reports · 2019Article
- Ammonia Transporters and Their Role in Acid-Base Balance.Physiological reviews · 2017Review
- Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.American journal of physiology. Renal physiology · 2016Article
- Acid-Base Homeostasis.Clinical journal of the American Society of Nephrology : CJASN · 2015Review
- Mechanisms of ammonia and ammonium transport by rhesus-associated glycoproteins.American journal of physiology. Cell physiology · 2015Article
- Human SLC4A11 Is a Novel NH3/H+ Co-transporter.The Journal of biological chemistry · 2015Article
- Ammonia transport in the kidney by Rhesus glycoproteins.American journal of physiology. Renal physiology · 2014Review
- Intercalated cell-specific Rh B glycoprotein deletion diminishes renal ammonia excretion response to hypokalemia.American journal of physiology. Renal physiology · 2013Article
- Renal ammonia metabolism and transport.Comprehensive Physiology · 2013Review
- Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.American journal of physiology. Cell physiology · 2011Article
- Sodium-bicarbonate cotransporter NBCn1/Slc4a7 inhibits NH4Cl-mediated inward current in Xenopus oocytes.Experimental physiology · 2011Article
- pH sensitivity of ammonium transport by Rhbg.American journal of physiology. Cell physiology · 2010Article
- Characteristics of mammalian Rh glycoproteins (SLC42 transporters) and their role in acid-base transport.Molecular aspects of medicineReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Rhbg is a nonerythroid membrane glycoprotein belonging to the Rh antigen family. In the kidney, Rhbg is expressed at the basolateral membrane of intercalated cells of the distal nephron and is involved in NH4+ transport. We investigated the substrate specificity of Rhbg by comparing transport of NH3/NH4+ with that of methyl amine (hydrochloride) (MA/MA+), often used to replace NH3/NH4+, in oocytes expressing Rhbg. Methyl amine (HCl) in solution exists as neutral methyl amine (MA) in equilibrium with the protonated methyl ammonium (MA+). To assess transport, we used ion-selective microelectrodes and voltage-clamp experiments to measure NH3/NH4+- and MA/MA+-induced intracellular pH (pH(i)) changes and whole cell currents. Our data showed that in Rhbg oocytes, NH3/NH4+ caused an inward current and decrease in pH(i) consistent with electrogenic NH4+ transport. These changes were significantly larger than in H2O-injected oocytes. The NH3/NH4+-induced current was not inhibited in the presence of barium or in the absence of Na+. In Rhbg oocytes, MA/MA+ caused an inward current but an increase (rather than a decrease) in pH(i). MA/MA+ did not cause any changes in H2O-injected oocytes. The MA/MA+-induced current and pH(i) increase were saturated at higher concentrations of MA/MA+. Amiloride inhibited MA/MA+-induced current and the increase in pH(i) in oocytes expressing Rhbg but had no effect on control oocytes. These results indicate that MA/MA+ is transported by Rhbg but differently than NH3/NH4+. The protonated MA+ is likely a direct substrate whose transport resembles that of NH4+. Transport of electroneutral MA is also enhanced by expression of Rhbg.
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