Evidence map›Paper›PMID 27435677›Full record

ArticleThe Journal of biological chemistry2016

Aquaporin 4 as a NH3 Channel.

Mette Assentoft, Shreyas Kaptan, Hans-Peter Schneider, Joachim W Deitmer, Bert L de Groot, Nanna MacAulay

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  3. Mechanism of COThe Journal of physiology · 2026
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  11. Molecular mechanisms of brain water transport.Nature reviews. Neuroscience · 2021
    Review
  12. Review
  13. Longitudinal [NeuroImage. Clinical · 2021
    Article
  14. Article
  15. Article
  16. Acid-Base Basics.Seminars in nephrology · 2019
    Review
  17. Article
  18. Organ Distribution ofNeurochemical research · 2017
    Article
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

6 authors at 3 institutions in 2 countries.

Mette AssentoftFrom the Department of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen, Denmark.
Shreyas KaptanComputational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany, and.
Hans-Peter SchneiderDivision of General Zoology, Department of Biology, University of Kaiserslautern, 67653 Kaiserslautern, Germany.
Joachim W DeitmerDivision of General Zoology, Department of Biology, University of Kaiserslautern, 67653 Kaiserslautern, Germany.
Bert L de GrootComputational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany, and.
Nanna MacAulayFrom the Department of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen, Denmark, macaulay@sund.ku.dk.
Max Planck Institute for Biophysical Chemistry · DEUniversity of Copenhagen · DKUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ammonia is a biologically potent molecule, and the regulation of ammonia levels in the mammalian body is, therefore, strictly controlled. The molecular paths of ammonia permeation across plasma membranes remain ill-defined, but the structural similarity of water and NH3 has pointed to the aquaporins as putative NH3-permeable pores. Accordingly, a range of aquaporins from mammals, plants, fungi, and protozoans demonstrates ammonia permeability. Aquaporin 4 (AQP4) is highly expressed at perivascular glia end-feet in the mammalian brain and may, with this prominent localization at the blood-brain-interface, participate in the exchange of ammonia, which is required to sustain the glutamate-glutamine cycle. Here we observe that AQP4-expressing Xenopus oocytes display a reflection coefficient <1 for NH4Cl at pH 8.0, at which pH an increased amount of the ammonia occurs in the form of NH3 Taken together with an NH4Cl-mediated intracellular alkalization (or lesser acidification) of AQP4-expressing oocytes, these data suggest that NH3 is able to permeate the pore of AQP4. Exposure to NH4Cl increased the membrane currents to a similar extent in uninjected oocytes and in oocytes expressing AQP4, indicating that the ionic NH4 (+) did not permeate AQP4. Molecular dynamics simulations revealed partial pore permeation events of NH3 but not of NH4 (+) and a reduced energy barrier for NH3 permeation through AQP4 compared with that of a cholesterol-containing lipid bilayer, suggesting AQP4 as a favored transmembrane route for NH3 Our data propose that AQP4 belongs to the growing list of NH3-permeable water channels.

Indexed as

AmmoniaAmmonium ChlorideAnimalsAquaporin 4AquaporinsIon ChannelsIon TransportLipid BilayersMolecular Dynamics SimulationOocytesRatsXenopus laevisAmmoniaAmmonium ChlorideAqp4 protein, ratAquaporin 4aquaporin 8AquaporinsIon ChannelsLipid Bilayersammoniaaquaporin 4 (AQP4)membrane proteinmolecular dynamicspermeability

Identifiers

PMID27435677
PMCPMC5009286
OpenAlexW2475921848

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.