Evidence map›Paper›PMID 25651436›Full record

ArticleThe journal of nutrition, health & aging2015

Folic acid inhibits tau phosphorylation through regulation of PP2A methylation in SH-SY5Y cells.

W Li, M Jiang, Y Xiao, X Zhang, S Cui, G Huang

Open access · greenAbstract read
In one paragraph

Article in The journal of nutrition, health & aging, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Role of Tau protein in long COVID and potential therapeutic targets.Frontiers in cellular and infection microbiology · 2023
    Review
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  5. Article
  6. Article
  7. Article
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  9. New Insights Into Drug Discovery Targeting Tau Protein.Frontiers in molecular neuroscience · 2020
    Review
  10. Review
  11. Homocysteine Increases Tau Phosphorylation, Truncation and Oligomerization.International journal of molecular sciences · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Epigenetic modulation of DNA methylation by nutrition and its mechanisms in animals.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2015
    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 1 institution in 1 country.

W LiGuowei Huang, Department of Nutrition and Food Science, School of Public Health, Tianjin Medical University, 22 Qixiangtai Road, Heping District, Tianjin 300070, P. R. China. Tel: +86-22-83336606. Fax: +86-22-83336603. E-mail: huangguowei@tmu.edu.cn.
M Jiang
Y Xiao
X Zhang
S Cui
G Huang
Tianjin Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesNeurofibrillary tangles (NFTs), which are composed of intracellular filamentous aggregates of hyperphosphorylated tau protein, are one of the pathological hallmarks of Alzheimer's disease (AD). Because tau phosphorylation is regulated by phosphatases, abnormal metabolism of protein phosphatase 2A (PP2A) has been proposed to be a contributing factor to the disease process.

resultsTo determine the function of folic acid on tau phosphorylation, an in vitro model of human neuroblastoma cells (SH-SY5Y) were exposed to folic acid (0-40 μmol/L) for 96 h, in the presence or absence of the phosphoesterase inhibitor okadaic acid (OA) (10 nmol/L) for 9 h. The data of western blot showed tau phosphorylation at the Ser396 site in OA-incubated SH-SY5Y cells was inhibited by folic acid in a concentration-dependent manner, with the folic acid concentration of 40 μmol/L providing maximal inhibition. Folic acid can downregulate tau protein phosphorylation by inhibiting the demethylation reactions of PP2A. High folic acid concentrations (20 and 40 μmol/L) increased SAM:SAH ratios and cell viability.

conclusionTherefore, we can speculate that folate deficiency may be a cause of PP2A deregulation, which can in turn lead to expression of the abnormal hyperphosphorylated form of tau.

Indexed as

Alzheimer DiseaseCell Line, TumorCell SurvivalFolic AcidFolic Acid DeficiencyHumansMethylationNeuroblastomaOkadaic AcidPhosphorylationProtein Phosphatase 2tau ProteinsFolic AcidOkadaic AcidProtein Phosphatase 2tau Proteins

Identifiers

PMID25651436
PMCPMC12877531
OpenAlexW2060210281

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.