ArticlePflugers Archiv : European journal of physiology2005
Expression of the human erythroid Rh glycoprotein (RhAG) enhances both NH3 and NH4+ transport in HeLa cells.
Article in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
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- Whole transcriptome analysis reveals T cell signaling activation in septic patients with thrombocytopenia.Scientific reports · 2025Article
- Comprehensive analysis of sialylation-related genes and construct the prognostic model in sepsis.Scientific reports · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Inhibition of NHE1 transport activity and gene transcription in DRG neurons in oxaliplatin-induced painful peripheral neurotoxicity.Scientific reports · 2023Article
- Ammonia as a Potential Neurotoxic Factor in Alzheimer's Disease.Frontiers in molecular neuroscience · 2016Review
- Mating induces the expression of immune- and pH-regulatory genes in the utero-vaginal junction containing mucosal sperm-storage tubuli of hens.Reproduction (Cambridge, England) · 2015Article
- Mechanisms of ammonia and ammonium transport by rhesus-associated glycoproteins.American journal of physiology. Cell physiology · 2015Article
- Overexpressing of OsAMT1-3, a High Affinity Ammonium Transporter Gene, Modifies Rice Growth and Carbon-Nitrogen Metabolic Status.International journal of molecular sciences · 2015Article
- Does aberrant membrane transport contribute to poor outcome in adult acute myeloid leukemia?Frontiers in pharmacology · 2015Article
- Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.American journal of physiology. Cell physiology · 2011Article
- The Rh protein family: gene evolution, membrane biology, and disease association.Cellular and molecular life sciences : CMLS · 2010Review
- Article
- Rhesus glycoprotein p2 (Rhp2) is a novel member of the Rh family of ammonia transporters highly expressed in shark kidney.The Journal of biological chemistry · 2010Article
- A model of Na+/H+ exchanger and its central role in regulation of pH and Na+ in cardiac myocytes.Biophysical journal · 2009Article
- Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH.Pflugers Archiv : European journal of physiology · 2009Article
- Expression of the gas-transporting proteins, Rh B glycoprotein and Rh C glycoprotein, in the murine lung.American journal of physiology. Lung cellular and molecular physiology · 2009Article
- Collecting duct-specific Rh C glycoprotein deletion alters basal and acidosis-stimulated renal ammonia excretion.American journal of physiology. Renal physiology · 2009Article
- Phosphorylation and ankyrin-G binding of the C-terminal domain regulate targeting and function of the ammonium transporter RhBG.The Journal of biological chemistry · 2008Article
- Molecular mechanisms of renal ammonia transport.Annual review of physiology · 2007Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The erythroid Rh-associated glycoprotein (RhAG) is strictly required for the expression of the Rh blood group antigens carried by Rh (D,CE) proteins. A biological function for RhAG in ammonium transport has been suggested by its ability to improve survival of an ammonium-uptake-deficient yeast. We investigated the function of RhAG by studying the entry of NH3/NH4+ in HeLa cells transiently expressing the green fluorescent protein (GFP)-RhAG fusion protein and using a fluorescent proton probe to measure intracellular pH (pHi). Under experimental conditions that reduce the intrinsic Na/H exchanger activity, exposure of control cells to a 10 mM NH4Cl- containing solution induces the classic pHi response profile of cells having a high permeability to NH3 (PNH3) but relatively low permeability to NH4+ (PNH4). In contrast, under the same conditions, the pHi profile of cells expressing RhAG clearly indicated an increased PNH4, as evidenced by secondary reacidification during NH4Cl exposure and a pHi undershoot below the initial resting value upon its removal. Measurements of pHi during methylammonium exposure showed that RhAG expression enhances the influx of both the unprotonated and ionic forms of methylammonium. Using a mathematical model to adjust passive permeabilities for a fit to the pHi profiles, we found that RhAG expression resulted in a threefold increase of PNH4 and a twofold increase of PNH3. Our results are the first evidence that the human erythroid RhAG increases the transport of both NH3 and NH4+.
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