Evidence map›Paper›PMID 15130092›Full record

ArticleThe Biochemical journal2004

Functional analysis of peroxisome-proliferator-responsive element motifs in genes of fatty acid-binding proteins.

Christian Schachtrup, Tanja Emmler, Bertram Bleck, Anton Sandqvist, Friedrich Spener

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 112 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Expression of fatty acid binding proteins in mesenteric adipose tissue.Biochemical and biophysical research communications · 2025
    Article
  5. Review
  6. Regulation of PPARγ2 Stability and Activity by SHP-1.Molecular and cellular biology · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Genome-Wide Analysis of theInternational journal of molecular sciences · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Fatty acid-binding protein 1 is preferentially lost in microsatellite instable colorectal carcinomas and is immune modulated via the interferon γ pathway.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2017
    Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Christian SchachtrupDepartment of Biochemistry, University of Münster, Wilhelm-Klemm-Str. 2, 48149 Münster, Germany.
Tanja Emmler
Bertram Bleck
Anton Sandqvist
Friedrich Spener
University of Münster · DEÅbo Akademi University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Retinoic acids and long-chain fatty acids are lipophilic agonists of nuclear receptors such as RXRs (retinoic X receptors) and PPARs (peroxisome-proliferator-activated receptors) respectively. These agonists are also ligands of intracellular lipid-binding proteins, which include FABPs (fatty acid-binding proteins). We reported previously that L (liver-type)-FABP targets fatty acids to the nucleus of hepatocytes and affects PPARalpha activation, which binds together with an RXR subtype to a PPRE (peroxisome-proliferator-responsive element). In the present study, we first determined the optimal combination of murine PPAR/RXR subtypes for binding to known murine FABP-PPREs and to those found by computer search and then tested their in vitro functionality. We show that all PPARs bind to L-FABP-PPRE, PPARalpha, PPARgamma1 and PPARgamma2 to A (adipocyte-type)-FABP-PPRE. All PPAR/RXR heterodimers transactivate L-FABP-PPRE, best are combinations of PPARalpha with RXRalpha or RXRgamma. In contrast, PPARalpha heterodimers do not transactivate A-FABP-PPRE, best combinations are of PPARgamma1 with RXRalpha and RXRgamma, and of PPARgamma2 with all RXR subtypes. We found that the predicted E (epidermal-type)- and H (heart-type)-FABP-PPREs are not activated by any PPAR/RXR combination without or with the PPAR pan-agonist bezafibrate. In the same way, C2C12 myoblasts transfected with promoter fragments of E-FABP and H-FABP genes containing putative PPREs are also not activated through stimulation of PPARs with bezafibrate applied to the cells. These results demonstrate that only PPREs of L- and A-FABP promoters are functional, and that binding of PPAR/RXR heterodimers to a PPRE in vitro does not necessarily predict transactivation.

Indexed as

AnimalsBase CompositionCarcinoma, HepatocellularCarrier ProteinsCell Line, TumorDimerizationDNAFatty Acid-Binding ProteinsGene Expression RegulationGenesGenes, ReporterHumansLiver NeoplasmsMiceMyoblastsPeroxisome Proliferator-Activated ReceptorsCarrier ProteinsDNAFABP1 protein, humanFabp1 protein, mouseFABP5 protein, humanFatty Acid-Binding ProteinsPeroxisome Proliferator-Activated ReceptorsPeroxisome ProliferatorsRetinoid X Receptors

Identifiers

PMID15130092
PMCPMC1133936
OpenAlexW2113682746

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.