Evidence map›Paper›PMID 22025646›Full record

ArticleThe Journal of pharmacology and experimental therapeutics2012

Histone H3 phosphorylation (Ser10, Ser28) and phosphoacetylation (K9S10) are differentially associated with gene expression in liver of rats treated in vivo with acute ethanol.

Taryn T James, Annayya R Aroor, Robert W Lim, Shivendra D Shukla

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of pharmacology and experimental therapeutics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Chemical Components and Hepatoprotective Mechanism of Xwak Granule in Mice Treated with Acute Alcohol.Evidence-based complementary and alternative medicine : eCAM · 2020
    Article
  6. Article
  7. Article
  8. Epigenetics and Liver Fibrosis.Cellular and molecular gastroenterology and hepatology · 2017
    Review
  9. International journal of biological sciences · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Binge ethanol and liver: new molecular developments.Alcoholism, clinical and experimental research · 2013
    Review
  16. Article
  17. 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

4 authors at 1 institution in 1 country.

Taryn T JamesDepartment of Medical Pharmacology and Physiology, University of Missouri School of Medicine, Columbia, MO 65203, USA.
Annayya R Aroor
Robert W Lim
Shivendra D Shukla
University of Missouri · US

Funding

Histone Modifications by Ethanol: Mechanism & ConsequenceR01AA016347 · NIAAA · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHUKLA, SHIVENDRA D · 2007 to 2011
$1.6M
NIAAA NIH HHS AA16347NIAAA NIH HHS R01 AA016347
6 · The paper itself

Abstract

The epigenetic histone modification by ethanol is emerging as one of the mechanisms for its deleterious effects in the liver. In this context, we have investigated the role of histone H3 phosphorylation at Ser10 (P-H3-Ser10), and Ser28 (P-H3-Ser28) in liver after acute ethanol treatment in vivo. Ethanol was administered intraperitoneally in male Sprague-Dawley rats. Ethanol dose-response (1-5 g/kg body weight) and time-course (1-4 h) experiments were conducted, and various parameters were monitored. Steatosis and necrosis (serum alanine aminotransferase) of the liver increased in 4 h, suggesting liver injury. There were differences between P-H3-Ser10 and P-H3-Ser28 at 1 h, with the latter being more sensitive to lower ethanol doses. It was noteworthy that phosphorylation of both serines disappeared at the highest dose used (5 g/kg). We also examined phosphoacetylation of histone H3 at K9S10 and observed a dramatic increase. The changes in histone H3 phosphorylation and phosphoacetylation were also accompanied with expression of early response genes (c-fos, c-jun, mitogen-activated protein kinase phosphatase-1). Chromatin immunoprecipitation assays in samples from 1.5 and 4 h of ethanol administration indicated that increased histone H3 phosphorylation at Ser28 was associated with the promoters of c-jun and plasminogen activator inhibitor-1. In conclusion, this study demonstrates for the first time that in vivo exposure of liver to acute ethanol induced phosphorylation and phosphoacetylation of histone H3, and these modifications are differentially involved in the mRNA expression of genes.

Indexed as

AcetylationAlanine TransaminaseAnimalsCaspase 3Chromatin ImmunoprecipitationDose-Response Relationship, DrugDual Specificity Phosphatase 1EthanolFatty Liver, AlcoholicGene ExpressionHistonesKineticsLiverMaleMucoproteinsPhosphorylationAlanine TransaminaseCaspase 3Dual Specificity Phosphatase 1Dusp1 protein, ratEthanolHistoneslysin, gastropodaMucoproteinsPlasminogen Activator Inhibitor 1Proto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junReceptors, LDLSerineTumor Necrosis Factor-alpha

Identifiers

PMID22025646
PMCPMC3263962
OpenAlexW2099327775

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.