Evidence map›Paper›PMID 26504087›Full record

ArticleThe Journal of biological chemistry2015

Reactive Oxygen Species (ROS) Mediate p300-dependent STAT1 Protein Interaction with Peroxisome Proliferator-activated Receptor (PPAR)-γ in CD36 Protein Expression and Foam Cell Formation.

Sivareddy Kotla, Gadiparthi N Rao

RetractedOpen access · hybridAbstract readRetracted Publication
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Ozonated autohemotherapy elevates PPAR-γ expression in CD4American journal of translational research · 2021
    Article
  8. Article
  9. Review
  10. Review
  11. Responses to Cytokines and Interferons that Depend upon JAKs and STATs.Cold Spring Harbor perspectives in biology · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Sivareddy KotlaFrom the Department of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163.
Gadiparthi N RaoFrom the Department of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163 rgadipar@uthsc.edu.
University of Tennessee Health Science Center · US

Funding

Non-COX Arachidonic Acid Metabolites and AngiogenesisR01HL074860 · NHLBI · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI RAO, GADIPARTHI N · 2004 to 2020
$5.9M
PLA2, EICOSANOIDS AND VASCULAR REMODELINGR01HL064165 · NHLBI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI RAO, GADIPARTHI N · 2000 to 2016
$5.4M
NHLBI NIH HHS HL064165NHLBI NIH HHS HL074860NHLBI NIH HHS R01 HL064165NHLBI NIH HHS R01 HL074860
6 · The paper itself

Abstract

Previously, we have demonstrated that 15(S)-hydroxyeicosatetranoic acid (15(S)-HETE) induces CD36 expression involving STAT1. Many studies have shown that peroxisome proliferator-activated receptor (PPAR)-γ mediates CD36 expression. Therefore, we asked the question whether these transcriptional factors interact with each other in the regulation of CD36 expression by 15(S)-HETE. Here, we show that STAT1 interacts with PPARγ in the induction of CD36 expression and foam cell formation by 15(S)-HETE. In addition, using molecular biological approaches such as EMSA, supershift EMSA, ChIP, re-ChIP, and promoter-reporter gene assays, we demonstrate that the STAT1 and PPARγ complex binds to the STAT-binding site at -107 nucleotides in the CD36 promoter and enhances its activity. Furthermore, the interaction of STAT1 with PPARγ depends on STAT1 acetylation, which is mediated by p300. In addition, our findings show that reactive oxygen species-dependent Syk and Pyk2 stimulation is required for p300 tyrosine phosphorylation and activation. Together, these results demonstrate that an interaction between STAT1, p300, and peroxisome proliferator-activated receptor-γ is required for 15(S)-HETE-induced CD36 expression, oxidized low density lipoprotein uptake, and foam cell formation, critical events underlying the pathogenesis of atherosclerosis.

Indexed as

Gene Expression RegulationAtherosclerosisCD36 AntigensCell Line, TumorE1A-Associated p300 ProteinFoam CellsHumansHydroxyeicosatetraenoic AcidsPPAR gammaReactive Oxygen SpeciesResponse ElementsSTAT1 Transcription Factor15-hydroxy-5,8,11,13-eicosatetraenoic acidCD36 AntigensE1A-Associated p300 ProteinEP300 protein, humanHydroxyeicosatetraenoic AcidsPPAR gammaReactive Oxygen SpeciesSTAT1 protein, humanSTAT1 Transcription Factor15(S)-HETEcd36foam cellgene expressionlipidlipoxygenase pathwayperoxisome proliferator-activated receptor (PPAR)signal transducers and activators of transcription 1 (STAT1)

Identifiers

PMID26504087
PMCPMC4683256
OpenAlexW2301665554

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.