Evidence map›Paper›PMID 26537798›Full record

ArticleMolecular & cellular proteomics : MCP2016

Terminal Galactosylation and Sialylation Switching on Membrane Glycoproteins upon TNF-Alpha-Induced Insulin Resistance in Adipocytes.

Benjamin L Parker, Morten Thaysen-Andersen, Daniel J Fazakerley, Mira Holliday, Nicolle H Packer, David E James

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
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  7. Article
  8. Article
  9. Analytical and bioanalytical chemistry · 2024
    Article
  10. Article
  11. Glycoproteome remodeling and organelle-specificProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
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  14. Review
  15. Article
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  17. Review
  18. Article
  19. The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021
    Review
  20. 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

6 authors at 2 institutions in 1 country.

Benjamin L ParkerFrom the ‡Charles Perkins Centre, School of Molecular Bioscience and.
Morten Thaysen-Andersen¶Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia.
Daniel J FazakerleyFrom the ‡Charles Perkins Centre, School of Molecular Bioscience and.
Mira HollidayFrom the ‡Charles Perkins Centre, School of Molecular Bioscience and.
Nicolle H Packer¶Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia.
David E JamesFrom the ‡Charles Perkins Centre, School of Molecular Bioscience and §School of MedicineUniversity of Sydney, Sydney, Australia; david.james@sydney.edu.au.
University of Sydney · AUMacquarie University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin resistance (IR) is a complex pathophysiological state that arises from both environmental and genetic perturbations and leads to a variety of diseases, including type-2 diabetes (T2D). Obesity is associated with enhanced adipose tissue inflammation, which may play a role in disease progression. Inflammation modulates protein glycosylation in a variety of cell types, and this has been associated with biological dysregulation. Here, we have examined the effects of an inflammatory insult on protein glycosylation in adipocytes. We performed quantitative N-glycome profiling of membrane proteins derived from mouse 3T3-L1 adipocytes that had been incubated with or without the proinflammatory cytokine TNF-alpha to induce IR. We identified the regulation of specific terminal N-glycan epitopes, including an increase in terminal di-galactose- and a decrease in biantennary alpha-2,3-sialoglycans. The altered N-glycosylation of TNF-alpha-treated adipocytes correlated with the regulation of specific glycosyltransferases, including the up-regulation of B4GalT5 and Ggta1 galactosyltransferases and down-regulation of ST3Gal6 sialyltransferase. Knockdown of B4GalT5 down-regulated the terminal di-galactose N-glycans, confirming the involvement of this enzyme in the TNF-alpha-regulated N-glycome. SILAC-based quantitative glycoproteomics of enriched N-glycopeptides with and without deglycosylation were used to identify the protein and glycosylation sites modified with these regulated N-glycans. The combined proteome and glycoproteome workflow provided a relative quantification of changes in protein abundance versus N-glycosylation occupancy versus site-specific N-glycans on a proteome-wide level. This revealed the modulation of N-glycosylation on specific proteins in IR, including those previously associated with insulin-stimulated GLUT4 trafficking to the plasma membrane.

Indexed as

3T3-L1 CellsAdipocytesAnimalsGalactoseGlycomicsGlycopeptidesGlycosylationInsulin ResistanceMass SpectrometryMembrane GlycoproteinsMiceN-Acetylneuraminic AcidPolysaccharidesProteomeProteomicsTumor Necrosis Factor-alphaGalactoseGlycopeptidesMembrane GlycoproteinsN-Acetylneuraminic AcidPolysaccharidesProteomeTumor Necrosis Factor-alpha

Identifiers

PMID26537798
PMCPMC4762517
OpenAlexW2202024625

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.