Evidence map›Paper›PMID 31289257›Full record

ArticleAging2019

Role of microtubule-associated protein 6 glycosylated with Gal-(β-1,3)-GalNAc in Parkinson's disease.

Li Ma, Jiaxin Song, Xueying Sun, Wenyong Ding, Kaiyang Fan, Minghua Qi, Yuefei Xu, Wenli Zhang

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Aging, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Glycosylation in aging and neurodegenerative diseases.Acta biochimica et biophysica Sinica · 2024
    Review
  6. Review
  7. TheJournal of proteome research · 2021
    Article
  8. Review
  9. Article
  10. Upregulation of Cellular Palmitoylation Mitigates α-Synuclein Accumulation and Neurotoxicity.Movement disorders : official journal of the Movement Disorder Society · 2021
    Article
  11. 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

8 authors at 2 institutions in 1 country.

Li Ma *Department of Epidemiology, Dalian Medical University, Dalian 116044, China.
Jiaxin Song *Department of Epidemiology, Dalian Medical University, Dalian 116044, China.
Xueying Sun *Department of Epidemiology, Dalian Medical University, Dalian 116044, China.
Wenyong DingBiochemistry and Molecular Biology Department of College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Kaiyang FanMedical Administration Department, Affiliated Hospital of Jining Medical University, Jining 272000, China.
Minghua QiBiochemistry and Molecular Biology Department of College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Yuefei XuBiochemistry and Molecular Biology Department of College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Wenli ZhangBiochemistry and Molecular Biology Department of College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Dalian Medical University · CNAffiliated Hospital of Jining Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aberrant glycosylation of proteins has major implications for human diseases. To determine whether protein glycosylation contributes to the pathogenesis of Parkinson's disease (PD), a mouse model of PD was established by injection of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Induction of PD-like features was verified by assessing motor impairment and confirming reductions in biological markers, including dopamine, 5-hydroxytryptamine and tyrosine hydroxylase, as well as the aggregation of α-synuclein. Altered glycosylation was detected using biotinylated agaracus bisporus lectin, which specifically binds exposed Gal-(β-1,3)-GalNAc linked to glycoproteins. Subsequent lectin affinity chromatography coupled with mass spectrometry revealed enhanced glycosylation of microtubule-associated protein 6 (MAP6) in PD mice as compared to healthy controls. In situ dual co-immunofluorescence analysis and immunoblotting confirmed that MAP6 is glycosylated with Gal-(β-1,3)-GalNAc oligosaccharides, which in turn alters the distribution and structure of MAP6 complexes within neurons. This is the first study to described MAP6 as a glycoprotein containing Gal-(β-1,3)-GalNAc oligosaccharides and to show that hyperglycosylation of MAP6 is strongly associated with the pathogenesis of PD. These findings provide potentially valuable information for developing new therapeutic targets for the treatment of PD as well as reliably prognostic biomarkers.

Indexed as

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineAnimalsChromatography, AffinityDisease Models, AnimalFluorescent Antibody TechniqueGalectinsGlycoproteinsGlycosylationImmunoblottingMaleMiceMice, Inbred C57BLMicrotubule-Associated ProteinsOligosaccharidesParkinson DiseaseSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineGalectinsGlycoproteinsMicrotubule-Associated ProteinsMtap6 protein, mouseOligosaccharidesglycosylationMAP6microtubule-associated protein 6MPTP-induced miceParkinson's disease

Identifiers

PMID31289257
PMCPMC6660046
OpenAlexW2961639430

What OpenQuestion holds

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LicenceCC BY
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.