Evidence map›Paper›PMID 24077989›Full record

ArticleThe Journal of membrane biology2013

Relative CO₂/NH₃ permeabilities of human RhAG, RhBG and RhCG.

R Ryan Geyer, Mark D Parker, Ashley M Toye, Walter F Boron, Raif Musa-Aziz

Open access · greenAbstract read
In one paragraph

Article in The Journal of membrane biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Rhbg interaction with CA-IV and its effects on NHAmerican journal of physiology. Cell physiology · 2025
    Article
  5. Article
  6. Role of channels in thebioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Chloride Gradient Is Involved in Ammonium Influx in Human Erythrocytes.International journal of molecular sciences · 2024
    Article
  9. Review
  10. Expression and Functional Analysis ofAnimals : an open access journal from MDPI · 2023
    Article
  11. Review
  12. Architecture of the human erythrocyte ankyrin-1 complex.Nature structural & molecular biology · 2022
    Article
  13. Article
  14. Effects of butyratePflugers Archiv : European journal of physiology · 2022
    Article
  15. Beyond CaPflugers Archiv : European journal of physiology · 2021
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

R Ryan Geyer
Mark D Parker
Ashley M Toye
Walter F Boron
Raif Musa-Aziz
University School · USCase Western Reserve University · USUniversity of Bristol · GB

Funding

Regulation of Proximal Tubule TransportR01DK081567 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI BORON, WALTER F · 2009 to 2013
$2.6M
NIDDK NIH HHS DK81567NIDDK NIH HHS R01 DK081567
6 · The paper itself

Abstract

Mammalian glycosylated rhesus (Rh) proteins include the erythroid RhAG and the nonerythroid RhBG and RhCG. RhBG and RhCG are expressed in multiple tissues, including hepatocytes and the collecting duct (CD) of the kidney. Here, we expressed human RhAG, RhBG and RhCG in Xenopus oocytes (vs. H2O-injected control oocytes) and used microelectrodes to monitor the maximum transient change in surface pH (DpHS) caused by exposing the same oocyte to 5 % CO₂/33 mM HCO₃⁻ (an increase) or 0.5 mM NH₃/NH₄⁺ (a decrease). Subtracting the respective values for day-matched, H₂O-injected control oocytes yielded channel-specific values (*). (ΔpH*(S))(CO₂) and (-ΔpH*(S))(NH₃) were each significantly >0 for all channels, indicating that RhBG and RhCG--like RhAG--can carry CO₂ and NH₃. We also investigated the role of a conserved aspartate residue, which was reported to inhibit NH₃ transport. However, surface biotinylation experiments indicate the mutants RhBG(D178N) and RhCG(D177N) have at most a very low abundance in the oocyte plasma membrane. We demonstrate for the first time that RhBG and RhCG--like RhAG--have significant CO₂ permeability, and we confirm that RhAG, RhBG and RhCG all have significant NH₃ permeability. However, as evidenced by (ΔpH*(S))(CO₂)/ (-ΔpH*(S))(NH₃) values, we could not distinguish among the CO₂/ NH₃ permeability ratios for RhAG, RhBG and RhCG. Finally, we propose a mechanism whereby RhBG and RhCG contribute to acid secretion in the CD by enhancing the transport of not only NH₃ but also CO₂ across the membranes of CD cells.

Indexed as

Amino Acid SequenceAmmoniaAnimalsBiological TransportBlood ProteinsCarbon DioxideCation Transport ProteinsGene ExpressionGlycoproteinsHumansHydrogen-Ion ConcentrationMembrane GlycoproteinsMembrane PotentialsMembrane Transport ProteinsMicroinjectionsModels, BiologicalAmmoniaBlood ProteinsCarbon DioxideCation Transport ProteinsGlycoproteinsMembrane GlycoproteinsMembrane Transport ProteinsRHAG protein, humanRHBG protein, humanRHCG protein, human

Identifiers

PMID24077989
PMCPMC7684545
OpenAlexW2052798968

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.