Evidence map›Paper›PMID 11533139›Full record

ArticleThe Journal of physiology2001

Multiple transport functions of a red blood cell anion exchanger, tAE1: its role in cell volume regulation.

H Guizouarn, N Gabillat, R Motais, F Borgese

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 53 citations in OpenAlex.

  1. KScience advances · 2020
    Article
  2. KNature · 2017
    Article
  3. Article
  4. Calcium in red blood cells-a perilous balance.International journal of molecular sciences · 2013
    Review
  5. Article
  6. Article
  7. Article
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  11. Review. Leaky Cl--HCO3- exchangers: cation fluxes via modified AE1.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009
    Review
  12. Article
  13. Article
  14. Article
  15. Article
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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

4 authors at 2 institutions in 1 country.

H GuizouarnLaboratoire de Physiologie des Membranes Cellulaires, UMR 6078, Université de Nice-Sophia Antipolis/CNRS, Bâtiment J. Maetz, 284 chemin Du Lazaret, 06230 Villefranche-sur-Mer, France.
N Gabillat
R Motais
F Borgese
Centre National de la Recherche Scientifique · FRUniversité Côte d'Azur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. It was previously shown that expressed in Xenopus oocyte the mouse (mAE1) and the trout (tAE1) anion exchanger behave differently: both elicit anion exchange activity but only tAE1 induces a transport of organic solutes correlated with a chloride channel activity. The present data, obtained by measurement of Xenopus oocyte membrane permeability and conductance, provide evidence that tAE1 also induces a large increase in Na(+) and K(+) permeability inhibited by several AE1 inhibitors. 2. This inhibition does not result from an effect on the driving force for electrodiffusion but represents a direct effect on the cation pathway. 3. As a control, expression of cystic fibrosis transmembrane conductance regulator (CFTR) having, once stimulated by 3-isobutyl-1-methylxanthine (IBMX), the same anion conductance magnitude as tAE1 did not induce any cation movement. 4. Chloride exchange, channel activity and cation transport induced by anion exchanger expression are inhibited by free or covalently bound H2DIDS as well. This covalent inhibition is reversed by the point mutation of Lys-522, the covalent binding site of H2DIDS to the protein. These data reveal that tAE1 itself acts both as an anion exchanger and as a channel of broad selectivity. 5. All results obtained by expression of AE1 isoforms in Xenopus oocytes and those obtained in erythrocytes are consistent with the proposal that, in nucleated erythrocytes, tAE1 functions as the swelling-activated osmolyte anion channel involved in cell volume regulation. In contrast AE1 from mammalian red cells, which do not regulate their volume, lacks swelling-activated osmolyte channel properties. 6. tAE1 illustrates the ability of a specific transport system to be a multifunctional protein exhibiting other transport functions when submitted to regulation.

Indexed as

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAngiogenesis InhibitorsAnimalsAnion Exchange Protein 1, ErythrocyteCationsChloridesCross-Linking ReagentsCyclooxygenase InhibitorsErythrocytesFemaleGene ExpressionLithiumMembrane PotentialsMutagenesis, Site-DirectedNiflumic AcidNitrobenzoates4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid5-nitro-2-(3-phenylpropylamino)benzoic acidAngiogenesis InhibitorsAnion Exchange Protein 1, ErythrocyteCationsChloridesCross-Linking ReagentsCyclooxygenase Inhibitorsdihydro-DIDSLithiumNiflumic AcidNitrobenzoatesPotassiumRubidiumSodium

Identifiers

PMID11533139
PMCPMC2278802
OpenAlexW1981130374

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.