Evidence map›Paper›PMID 15644866›Full record

ArticleBritish journal of pharmacology2005

Substrate specificity and functional characterisation of the H+/amino acid transporter rat PAT2 (Slc36a2).

David J Kennedy, Kelly M Gatfield, John P Winpenny, Vadivel Ganapathy, David T Thwaites

Open access · greenAbstract read
In one paragraph

Article in British journal of pharmacology, 2005. 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
1.1field-weighted citation impact, top 24% 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, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Trading amino acids at the aphid-Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. Article
  8. The Concise Guide to PHARMACOLOGY 2013/14: transporters.British journal of pharmacology · 2013
    Article
  9. Review
  10. Article
  11. Article
  12. Intracellular amino acid sensing and mTORC1-regulated growth: new ways to block an old target?Current opinion in investigational drugs (London, England : 2000) · 2010
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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 2 institutions in 1 country.

David J KennedyInstitute for Cell & Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
Kelly M Gatfield
John P Winpenny
Vadivel Ganapathy
David T Thwaites
Newcastle University · GBUniversity of East Anglia · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functional characteristics and substrate specificity of the rat proton-coupled amino acid transporter 2 (rat PAT2 (rPAT2)) were determined following expression in Xenopus laevis oocytes using radiolabelled uptake measurements, competition experiments and measurements of substrate-evoked current using the two-electrode voltage-clamp technique. The aim of the investigation was to determine the structural requirements and structural limitations of potential substrates for rPAT2. Amino (and imino) acid transport via rPAT2 was pH-dependent, Na(+)-independent and electrogenic. At extracellular pH 5.5 (in Na(+)-free conditions) proline uptake was saturable (Km 172+/-41 muM), demonstrating that rPAT2 is, relative to PAT1, a high-affinity transporter.PAT2 preferred substrates are L-alpha-amino acids with small aliphatic side chains (e.g. the methyl group in alanine) and 4- or 5-membered heterocyclic amino and imino acids such as 2-azetidine-carboxylate, proline and cycloserine, where both D- and L-enantiomers are transported. The major restrictions on transport are side chain size (the ethyl group of alpha-aminobutyric acid is too large) and backbone length, where the separation of the carboxyl and amino groups by only two CH(2) groups, as in beta-alanine, is enough to reduce transport. Methylation of the amino group is tolerated (e.g. sarcosine) but increasing methylation, as in betaine, decreases transport. A free carboxyl group is preferred as O-methyl esters show either reduced transport (alanine-O-methyl ester) or are excluded. The structural characteristics that determine the substrate specificity of rPAT2 have been identified. This information should prove valuable in the design of selective substrates/inhibitors for PAT1 and PAT2.

Indexed as

Amino AcidsAmino Acid Transport SystemsAmino Acid Transport Systems, NeutralAnimalsBetaineBiological TransportFemaleGlycineHydrogen-Ion ConcentrationMicroinjectionsOocytesPatch-Clamp TechniquesProlineProtonsRatsStereoisomerismAmino AcidsAmino Acid Transport SystemsAmino Acid Transport Systems, NeutralBetaineGlycineProlineProtonsSlc36a2 protein, ratSymporters

Identifiers

PMID15644866
PMCPMC1575977
OpenAlexW1773242321

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.