Evidence map›Paper›PMID 26929182›Full record

ReviewJournal of cellular and molecular medicine2016

O-GlcNAcylation: a bridge between glucose and cell differentiation.

Chao Sun, Jin Shang, Yuan Yao, Xiaohong Yin, Minghan Liu, Huan Liu, Yue Zhou

Abstract readReview
In one paragraph

Review in Journal of cellular and molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. ProteinMetabolites · 2022
    Review
  9. Role of Diet in Stem and Cancer Stem Cells.International journal of molecular sciences · 2022
    Review
  10. Cancers · 2022
    Review
  11. Cells · 2022
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Metabolic rearrangements in primary liver cancers: cause and consequences.Nature reviews. Gastroenterology & hepatology · 2019
    Review
  18. Article
  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

7 authors.

Chao SunDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
Jin ShangDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
Yuan YaoDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
Xiaohong YinCenter for Evidence-based and Translational Medicine, Zhongnan Hospital, Wuhan University, Wuhan, China.
Minghan LiuDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
Huan LiuDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.
Yue ZhouDepartment of Orthopedics, Xinqiao Hospital, Third Military Medical University, Chongqing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucose is the major energy supply and a critical metabolite for most cells and is especially important when cell is differentiating. High or low concentrations of glucose enhances or inhibits the osteogenic, chondrogenic and adipogenic differentiation of cell via the insulin, transforming growth factor-β and peroxisome proliferator-activated receptor γ pathways, among others. New evidence implicates the hexosamine biosynthetic pathway as a mediator of crosstalk between glucose flux, cellular signalling and epigenetic regulation of cell differentiation. Extracellular glucose flux alters intracellular O-GlcNAcylation levels through the hexosamine biosynthetic pathway. Signalling molecules that are important for cell differentiation, including protein kinase C, extracellular signal-regulated kinase, Runx2, CCAAT/enhancer-binding proteins, are modified by O-GlcNAcylation. Thus, O-GlcNAcylation markedly alters cell fate during differentiation via the post-transcriptional modification of proteins. Furthermore, O-GlcNAcylation and phosphorylation show complex interactions during cell differentiation: they can either non-competitively occupy different sites on a substrate or competitively occupy a single site or proximal sites. Therefore, the influence of glucose on cell differentiation via O-GlcNAcylation offers a potential target for controlling tissue homoeostasis and regeneration in ageing and disease. Here, we review recent progress establishing an emerging relationship among glucose concentration, O-GlcNAcylation levels and cell differentiation.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylglucosamineAcylationAdipocytesCCAAT-Enhancer-Binding ProteinsCell DifferentiationChondrocytesCore Binding Factor Alpha 1 SubunitGlucoseHumansMesenchymal Stem CellsN-AcetylglucosaminyltransferasesOsteoblastsProtein Kinase CSignal TransductionAcetylglucosamineCCAAT-Enhancer-Binding ProteinsCEBPA protein, humanCore Binding Factor Alpha 1 SubunitGlucoseN-AcetylglucosaminyltransferasesProtein Kinase CRUNX2 protein, humanadipogenic differentiationcell differentiationchondrogenic differentiationglucoseO-GlcNAcylationosteogenic differentiation

Identifiers

PMID26929182
PMCPMC4831356

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Registered trials

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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.