Evidence map›Paper›PMID 26598517›Full record

ArticleThe Journal of biological chemistry2016

O-Linked β-N-acetylglucosamine (O-GlcNAc) Acts as a Glucose Sensor to Epigenetically Regulate the Insulin Gene in Pancreatic Beta Cells.

Sean P Durning, Heather Flanagan-Steet, Nripesh Prasad, Lance Wells

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Regulation of insulin secretion by the post-translational modifications.Frontiers in cell and developmental biology · 2023
    Review
  10. ProteinMetabolites · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. O-GlcNAcylation, a sweet link to the pathology of diseases.Journal of Zhejiang University. Science. B · 2019
    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 2 institutions in 1 country.

Sean P DurningFrom the Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602-1516 and.
Heather Flanagan-SteetFrom the Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602-1516 and.
Nripesh PrasadHudsonAlpha Institute of Biotechnology, Genomic Services Laboratory, Huntsville, Alabama 35806.
Lance WellsFrom the Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602-1516 and lwells@ccrc.uga.edu.
University of Georgia · USHudsonAlpha Institute for Biotechnology · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Tumor Glycomics Laboratory for Discovery of Pancreatic Cancer MarkersU01CA128454 · NCI · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2007 to 2017
$5.7M
NCI NIH HHS U01 CA128454NCI NIH HHS U01CA128454NIGMS NIH HHS P41 GM103490NIGMS NIH HHS P41GM103490
6 · The paper itself

Abstract

The post-translational protein modification O-linked β-N-acetylglucosamine (O-GlcNAc) is a proposed nutrient sensor that has been shown to regulate multiple biological pathways. This dynamic and inducible enzymatic modification to intracellular proteins utilizes the end product of the nutrient sensing hexosamine biosynthetic pathway, UDP-GlcNAc, as its substrate donor. Type II diabetic patients have elevated O-GlcNAc-modified proteins within pancreatic beta cells due to chronic hyperglycemia-induced glucose overload, but a molecular role for O-GlcNAc within beta cells remains unclear. Using directed pharmacological approaches in the mouse insulinoma-6 (Min6) cell line, we demonstrate that elevating nuclear O-GlcNAc increases intracellular insulin levels and preserves glucose-stimulated insulin secretion during chronic hyperglycemia. The molecular mechanism for these observed changes appears to be, at least in part, due to elevated O-GlcNAc-dependent increases in Ins1 and Ins2 mRNA levels via elevations in histone H3 transcriptional activation marks. Furthermore, RNA deep sequencing reveals that this mechanism of altered gene transcription is restricted and that the majority of genes regulated by elevated O-GlcNAc levels are similarly regulated by a shift from euglycemic to hyperglycemic conditions. These findings implicate the O-GlcNAc modification as a potential mechanism for hyperglycemic-regulated gene expression in the beta cell.

Indexed as

Epigenesis, GeneticAcetylglucosamineAnimalsCell LineComputational BiologyGene Expression RegulationGenomeGlucoseHigh-Throughput Nucleotide SequencingInsulinInsulinomaInsulin-Secreting CellsMiceMicroscopy, ConfocalProtein Processing, Post-TranslationalRNA, MessengerAcetylglucosamineGlucoseInsulinRNA, Messengerbeta cell (B-cell)diabetesepigeneticsinsulinO-linked N-acetylglucosamine (O-GlcNAc)post-translational modification (PTM)RNASeq

Identifiers

PMID26598517
PMCPMC4732198
OpenAlexW2172715200

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.