Evidence map›Paper›PMID 19074966›Full record

ArticleThe Journal of physiology2009

Taurine uptake across the human intestinal brush-border membrane is via two transporters: H+-coupled PAT1 (SLC36A1) and Na+- and Cl(-)-dependent TauT (SLC6A6).

Catriona M H Anderson, Alison Howard, Julian R F Walters, Vadivel Ganapathy, David T Thwaites

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

62 citing papers in PubMed, 134 citations in OpenAlex.

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2 more citing papers are in PubMed but not listed here.

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 2 countries.

Catriona M H AndersonEpithelial Research Group, Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, UK. catriona.anderson@ncl.ac.uk
Alison Howard
Julian R F Walters
Vadivel Ganapathy
David T Thwaites
Newcastle University · GBAugusta University · USHammersmith Hospital · GB

Funding

Wellcome TrustWellcome Trust 078640/Z/05/Z
6 · The paper itself

Abstract

Taurine is an essential amino acid in some mammals and is conditionally essential in humans. Taurine is an abundant component of meat and fish-based foods and has been used as an oral supplement in the treatment of disorders such as cystic fibrosis and hypertension. The purpose of this investigation was to identity the relative contributions of the solute transporters involved in taurine uptake across the luminal membrane of human enterocytes. Distinct transport characteristics were revealed following expression of the candidate solute transporters in Xenopus laevis oocytes: PAT1 (SLC36A1) is a H(+)-coupled, pH-dependent, Na(+)- and Cl(-)-independent, low-affinity, high-capacity transporter for taurine and beta-alanine; TauT (SLC6A6) is a Na(+)- and Cl(-)-dependent, high-affinity, low-capacity transporter of taurine and beta-alanine; ATB(0,+) (SLC6A14) is a Na(+)- and Cl(-)-dependent, high-affinity, low-capacity transporter which accepts beta-alanine but not taurine. Taurine uptake across the brush-border membrane of human intestinal Caco-2 cell monolayers showed characteristics of both PAT1- and TauT-mediated transport. Under physiological conditions, Cl(-)-dependent TauT-mediated uptake predominates at low taurine concentrations, whereas at higher concentrations typical of diet, Cl(-)-independent PAT1-mediated uptake is the major absorptive mechanism. Real-time PCR analysis of human duodenal and ileal biopsy samples demonstrates that PAT1, TauT and ATB(0,+) mRNA are expressed in each tissue but to varying degrees. In conclusion, this study is the first to demonstrate both taurine uptake via PAT1 and functional coexpression of PAT1 and TauT at the apical membrane of the human intestinal epithelium. PAT1 may be responsible for bulk taurine uptake during a meal whereas TauT may be important for taurine supply to the intestinal epithelium and for taurine capture between meals.

Indexed as

Amino Acid Transport SystemsAnimalsCaco-2 CellsFemaleHumansHydrogenIntestinal MucosaIntestine, SmallMembrane GlycoproteinsMembrane Transport ProteinsMicrovilliSymportersTaurineTaurine TransportersXenopus laevisAmino Acid Transport SystemsHydrogenMembrane GlycoproteinsMembrane Transport ProteinsSLC36A1 protein, humanSymportersTaurineTaurine Transporters

Identifiers

PMID19074966
PMCPMC2669967
OpenAlexW2138018209

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.