Evidence map›Paper›PMID 18599538›Full record

ArticleThe Journal of physiology2008

Human solute carrier SLC6A14 is the beta-alanine carrier.

Catriona M H Anderson, Vadivel Ganapathy, David T Thwaites

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Flux coupling, not specificity, shapes the transport and phylogeny of SLC6 glycine transporters.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. An emerging role of vitamin DAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Amino Acid Transporter SLC6A14 (ATBFrontiers in cell and developmental biology · 2020
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. The Concise Guide to PHARMACOLOGY 2013/14: transporters.British journal of pharmacology · 2013
    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

3 authors at 2 institutions in 2 countries.

Catriona M H AndersonInstitute for Cell & Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, UK.
Vadivel Ganapathy
David T Thwaites
Newcastle University · GBAugusta University · US

Funding

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

Abstract

The beta-alanine carrier was characterized functionally in the 1960s to 1980s at the luminal surface of the ileal mucosal wall and is a Na(+)- and Cl(-)-dependent transporter of a number of essential and non-essential cationic and dipolar amino acids including lysine, arginine and leucine. beta-Alanine carrier-like function has not been demonstrated by any solute carrier transport system identified at the molecular level. A series of experiments were designed to determine whether solute carrier SLC6A14 is the molecular correlate of the intestinal beta-alanine carrier, perhaps the last of the classical intestinal amino acid transport systems to be identified at the molecular level. Following expression of the human SLC6A14 transporter in Xenopus laevis oocytes, the key functional characteristics of the beta-alanine carrier, identified previously in situ in ileum, were demonstrated for the first time. The transport system is both Na(+) and Cl(-) dependent, can transport non-alpha-amino acids such as beta-alanine with low affinity, and has a higher affinity for dipolar and cationic amino acids such as leucine and lysine. N-methylation of its substrates reduces the affinity for transport. These observations confirm the hypothesis that the SLC6A14 gene encodes the transport protein known as the beta-alanine carrier which, due to its broad substrate specificity, is likely to play an important role in absorption of essential nutrients and drugs in the distal regions of the human gastrointestinal tract.

Indexed as

Amino Acid Transport SystemsAmino Acid Transport Systems, NeutralAnimalsbeta-AlanineGene Expression RegulationHumansOocytesXenopus laevisAmino Acid Transport SystemsAmino Acid Transport Systems, Neutralbeta-AlanineSLC6A14 protein, human

Identifiers

PMID18599538
PMCPMC2592472
OpenAlexW2149865901

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.