Evidence map›Paper›PMID 26869183›Full record

ArticleScientific reports2016

Prostaglandin I₂ Attenuates Prostaglandin E₂-Stimulated Expression of Interferon γ in a β-Amyloid Protein- and NF-κB-Dependent Mechanism.

Pu Wang, Pei-Pei Guan, Xin Yu, Li-Chao Zhang, Ya-Nan Su, Zhan-You Wang

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.3field-weighted citation impact, top 7% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Role of Eicosanoids in Alzheimer's Disease.International journal of environmental research and public health · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Prostaglandin IOncotarget · 2017
    Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Pu WangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Pei-Pei GuanCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Xin YuCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Li-Chao ZhangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Ya-Nan SuCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Zhan-You WangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, P. R. China.
Northeastern University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclooxygenase-2 (COX-2) has been recently identified as being involved in the pathogenesis of Alzheimer's disease (AD). However, the role of an important COX-2 metabolic product, prostaglandin (PG) I2, in AD development remains unknown. Using mouse-derived astrocytes as well as APP/PS1 transgenic mice as model systems, we firstly elucidated the mechanisms of interferon γ (IFNγ) regulation by PGE2 and PGI2. Specifically, PGE2 accumulation in astrocytes activated the ERK1/2 and NF-κB signaling pathways by phosphorylation, which resulted in IFNγ expression. In contrast, the administration of PGI2 attenuated the effects of PGE2 on stimulating the production of IFNγ via inhibiting the translocation of NF-κB from the cytosol to the nucleus. Due to these observations, we further studied these prostaglandins and found that both PGE2 and PGI2 increased Aβ1-42 levels. In detail, PGE2 induced IFNγ expression in an Aβ1-42-dependent manner, whereas PGI2-induced Aβ1-42 production did not alleviate cells from IFNγ inhibition by PGI2 treatment. More importantly, our data also revealed that not only Aβ1-42 oligomer but also fibrillar have the ability to induce the expression of IFNγ via stimulation of NF-κB nuclear translocation in astrocytes of APP/PS1 mice. The production of IFNγ finally accelerated the deposition of Aβ1-42 in β-amyloid plaques.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAstrocytesBrainCell NucleusDinoprostoneDisease ProgressionDown-RegulationEpoprostenolFemaleInterferon-gammaMice, Inbred C57BLMice, TransgenicModels, BiologicalNF-kappa BAmyloid beta-PeptidesDinoprostoneEpoprostenolInterferon-gammaN-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamideNF-kappa BNitrobenzenesPresenilin-1Sulfonamides

Identifiers

PMID26869183
PMCPMC4751455
OpenAlexW2259682063

What OpenQuestion holds

Textmetadata
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.