Evidence map›Paper›PMID 21214566›Full record

ArticleJournal of neurochemistry2011

Histone acetylation-mediated glycosyltransferase gene regulation in mouse brain during development.

Yusuke Suzuki, Makoto Yanagisawa, Toshio Ariga, Robert K Yu

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.9field-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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Epigenetic Regulation of Glycosylation in Cancer and Other Diseases.International journal of molecular sciences · 2021
    Review
  12. Epigenetic Regulation of Glycosylation.Advances in experimental medicine and biology · 2021
    Article
  13. Review
  14. EZH2 Inhibition in Ewing Sarcoma Upregulates GMolecular therapy : the journal of the American Society of Gene Therapy · 2019
    Article
  15. Article
  16. Article
  17. Epigenetics and Sphingolipid Metabolism in Health and Disease.International journal of biopharmaceutical sciences · 2018
    Article
  18. Gangliosides in Nerve Cell Specification.Progress in molecular biology and translational science · 2018
    Review
  19. Review
  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

4 authors at 1 institution in 1 country.

Yusuke SuzukiInstitute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, Georgia 30912, USA.
Makoto Yanagisawa
Toshio Ariga
Robert K Yu
Augusta University · US

Funding

Spingoglycolipids of normal and pathological brainsR01NS011853 · NINDS · YALE UNIVERSITY · PI YU, ROBERT K. · 1985 to 2010
$3.5M
ROLE OF GLYCOLIPIDS IN EXPERIMENTAL NEUROPATHYR01NS026994 · NINDS · VIRGINIA COMMONWEALTH UNIVERSITY · PI YU, ROBERT K. · 1988 to 2012
$3.3M
NINDS NIH HHS NS11853NINDS NIH HHS NS26994NINDS NIH HHS R01 NS011853NINDS NIH HHS R01 NS026994
6 · The paper itself

Abstract

Gangliosides are sialic acid-containing glycosphingolipids abundant in the central nervous tissues. The quantity and expression pattern of gangliosides in brain change drastically during early development and are mainly regulated through stage-specific expression of glycosyltransferase (ganglioside synthase) genes. It is still unclear, however, how the transcriptional activation of glycosyltransferase genes is regulated during development. In this study, we investigated the epigenetic regulation of two key glycosyltransferases, N-acetylgalactosaminyltransferase I (GA2/GM2/GD2/GT2-synthase) and sialyltransferase II (GD3-synthase), in embryonic, postnatal, and adult mouse brains. Combined bisulfite restriction analysis assay showed that DNA methylation in the 5' regions of these glycosyltransferase genes was not associated with their expression patterns. On the other hand, chromatin immunoprecipitation assay of both glycosyltransferase genes showed that their histone H3 acetylation was highly correlated to their mRNA expression levels during development. In fact, we confirmed that the expression patterns of gangliosides and glycosyltransferases in neuroepithelial cells were changed after treatment with a histone deacetylase inhibitor, sodium butyrate. Our studies provide the first evidence that efficient histone acetylation of the glycosyltransferase genes in mouse brain contributes to the developmental alteration of ganglioside expression.

Indexed as

AcetylationAnimalsAnimals, NewbornBrainButyratesCells, CulturedChromatin ImmunoprecipitationChromatography, Thin LayerDNA MethylationEmbryo, MammalianEnzyme InhibitorsGene Expression Regulation, DevelopmentalHistonesMiceMice, Inbred ICRN-Acetylgalactosaminyltransferasesalpha-N-acetylneuraminate alpha-2,8-sialyltransferaseButyratesEnzyme InhibitorsHistonesN-AcetylgalactosaminyltransferasesSialyltransferases

Identifiers

PMID21214566
PMCPMC3706450
OpenAlexW1585646325

What OpenQuestion holds

Textmetadata
LicenceTDM
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.