Evidence map›Paper›PMID 24379411›Full record

ArticleThe Journal of biological chemistry2014

Molecular identification and functional characterization of the human colonic thiamine pyrophosphate transporter.

Svetlana M Nabokina, Katsuhisa Inoue, Veedamali S Subramanian, Judith E Valle, Hiroaki Yuasa, Hamid M Said

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. A new combined prognostic model involvingTranslational cancer research · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Effect of knocking out mouseAmerican journal of physiology. Gastrointestinal and liver physiology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Frontiers in pharmacology · 2023
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Svetlana M NabokinaFrom the Departments of Medicine and Physiology/Biophysics, University of California, Irvine, California 92697.
Katsuhisa Inoue
Veedamali S Subramanian
Judith E Valle
Hiroaki Yuasa
Hamid M Said
Tokyo University of Pharmacy and Life Sciences · JPUniversity of California, Irvine · USLong Beach Medical Center · USNagoya City University · JP

Funding

Vitamin B1 (thiamin) transport in Alzheimer’s Disease: Role of microRNAs in regulating level of expression of its transporters (SLC19A2 & SLC19A3) in human brain cells and effect of hypoxiaR01DK056061 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI SAID, HAMID M · 1999 to 2024
$5.0M
Mechanism/Regulation of Intestinal Thiamin UptakeR37DK056061 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI SAID, HAMID M · 2009 to 2018
$3.6M
NIDDK NIH HHS DK 56061-15NIDDK NIH HHS R01 DK056061NIDDK NIH HHS R37 DK056061
6 · The paper itself

Abstract

Colonic microbiota synthesize a considerable amount of thiamine in the form of thiamine pyrophosphate (TPP). Recent functional studies from our laboratory have shown the existence of a specific, high-affinity, and regulated carrier-mediated uptake system for TPP in human colonocytes. Nothing, however, is known about the molecular identity of this system. Here we report on the molecular identification of the colonic TPP uptake system as the product of the SLC44A4 gene. We cloned the cDNA of SLC44A4 from human colonic epithelial NCM460 cells, which, upon expression in ARPE19 cells, led to a significant (p < 0.01, >5-fold) induction in [(3)H]TPP uptake. Uptake by the induced system was also found to be temperature- and energy-dependent; Na(+)-independent, slightly higher at acidic buffer pH, and highly sensitive to protonophores; saturable as a function of TPP concentration, with an apparent Km of 0.17 ± 0.064 μM; and highly specific for TPP and not affected by free thiamine, thiamine monophosphate, or choline. Expression of the human TPP transporter was found to be high in the colon and negligible in the small intestine. A cell surface biotinylation assay and live cell confocal imaging studies showed the human TPP transporter protein to be expressed at the apical membrane domain of polarized epithelia. These results show, for the first time, the molecular identification and characterization of a specific and high-affinity TPP uptake system in human colonocytes. The findings further support the hypothesis that the microbiota-generated TPP is absorbable and could contribute toward host thiamine homeostasis, especially toward cellular nutrition of colonocytes.

Indexed as

AnimalsBiological Transport, ActiveCloning, MolecularColonDNA, ComplementaryDogsGene Expression RegulationHumansHydrogen-Ion ConcentrationIntestine, SmallMadin Darby Canine Kidney CellsMembrane Transport ProteinsOrgan SpecificityThiamine PyrophosphateDNA, ComplementaryMembrane Transport ProteinsSLC44A4 protein, humanThiamine PyrophosphateIntestinal EpitheliumMembrane TransportThiamineTransfectionTransporters

Identifiers

PMID24379411
PMCPMC3924303
OpenAlexW2122918648

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.