Evidence map›Paper›PMID 12938672›Full record

ArticleThe Journal of physiology2003

Sugar transport by mammalian members of the SLC26 superfamily of anion-bicarbonate exchangers.

J-M Chambard, J F Ashmore

Abstract read
In one paragraph

Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Interaction between CFTR and prestin (SLC26A5).Biochimica et biophysica acta · 2010
    Article
  5. Article
  6. Article
  7. Article
  8. Distribution of pendrin in the organ of Corti of mice observed by electron immunomicroscopy.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2006
    Article
  9. Review
  10. 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

2 authors.

J-M ChambardDepartment of Physiology, University College London, UK.
J F Ashmore

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mammalian cochlea contains a population of outer hair cells (OHCs) whose electromotility depends on an assembly of 'motor' molecules in the basolateral membrane of the cell. Named 'prestin', the molecule is a member of the SLC26 anion transporter superfamily. We show both directly and indirectly that SLC26A5, rat prestin, takes up hexoses when expressed in several cell lines. Direct measurements of labelled fructose transport into COS-7 cells expressing prestin are reported here. Indirect measurements, using imaging techniques, show that transfected HEK-293 or CHO-Ki cells undergo reversible volume changes when exposed to isosmotic glucose-fructose exchange. The observations are consistent with the sugar transport. A similar transport was observed using a C-terminal green fluorescent protein (GFP)-tagged pendrin (SLC26A4) construct. Cells transfected with GFP alone did not respond to sugars. The data are consistent with fructose being transported by prestin with an apparent Km=24 nm. From the voltage-dependent capacitance of transfected cells, we estimate that 250,000 prestin molecules were present and hence that the single transport rate is not more than 3000 fructose molecules s(-1). Comparison of the transfected cell swelling rates induced by fructose and by osmotic steps indicates that water was co-transported with sugar. We suggest that the structure of SLC26 family members allows them to act as neutral substrate transporters and may explain observed properties of cochlear hair cells.

Indexed as

Carbohydrate MetabolismMembrane Transport ProteinsAlgorithmsAnimalsAnionsAnion Transport ProteinsAntiportersBicarbonatesCarrier ProteinsCell LineChlorocebus aethiopsCHO CellsCOS CellsCricetinaeElectrophysiologyFructoseAnionsAnion Transport ProteinsAntiportersBicarbonatesCarrier ProteinsFructoseMembrane Transport ProteinsProteinsSalicylatesSLC26A4 protein, humanSLC26A5 protein, humanSulfate TransportersWater

Identifiers

PMID12938672
PMCPMC2343088

What OpenQuestion holds

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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.