Evidence map›Paper›PMID 29149631›Full record

ArticleNeurobiology of aging2018

Prostaglandin J2 promotes O-GlcNAcylation raising APP processing by α- and β-secretases: relevance to Alzheimer's disease.

Teneka Jean-Louis, Patricia Rockwell, Maria E Figueiredo-Pereira

Abstract read
In one paragraph

Article in Neurobiology of aging, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Trial
  2. Nutritional Mushroom Treatment in Meniere's Disease withInternational journal of molecular sciences · 2019
    Trial
  3. Review
  4. Article
  5. Review
  6. Review
  7. 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

3 authors at 1 institution in 1 country.

Teneka Jean-LouisDepartment of Biological Sciences, Hunter College, Biology and Biochemistry Programs, Graduate Center, The City University of New York, New York, NY, USA.
Patricia RockwellDepartment of Biological Sciences, Hunter College, Biology and Biochemistry Programs, Graduate Center, The City University of New York, New York, NY, USA.
Maria E Figueiredo-PereiraDepartment of Biological Sciences, Hunter College, Biology and Biochemistry Programs, Graduate Center, The City University of New York, New York, NY, USA. Electronic address: pereira@genectr.hunter.cuny.edu.
The Graduate Center, CUNY · US

Funding

RISE Program Hunter College Option IIIR25GM060665 · NIGMS · HUNTER COLLEGE · PI ORTIZ, BENJAMIN D.,, SERRANO, PETER A · 2000 to 2022
$22.8M
Basic and Translational Research Center for Reducing Health DisparitiesG12MD007599 · NIMHD · HUNTER COLLEGE · PI ANGULO, JESUS A · 2012 to 2017
$14.6M
NIGMS NIH HHS R25 GM060665NIMHD NIH HHS G12 MD007599
6 · The paper itself

Abstract

Regulation of the amyloid precursor protein (APP) processing by α- and β-secretases is of special interest to Alzheimer's disease (AD), as these proteases prevent or mediate amyloid beta formation, respectively. Neuroinflammation is also implicated in AD. Our data demonstrate that the endogenous mediator of inflammation prostaglandin J2 (PGJ2) promotes full-length APP (FL-APP) processing by α- and β-secretases. The decrease in FL-APP was independent of proteasomal, lysosomal, calpain, caspase, and γ-secretase activities. Moreover, PGJ2-treatment promoted cleavage of secreted APP, specifically sAPPα and sAPPβ, generated by α and β-secretase, respectively. Notably, PGJ2-treatment induced caspase-dependent cleavage of sAPPβ. Mechanistically, PGJ2-treatment selectively diminished mature (O- and N-glycosylated) but not immature (N-glycosylated only) FL-APP. PGJ2-treatment also increased the overall levels of protein O-GlcNAcylation, which occurs within the nucleocytoplasmic compartment. It is known that APP undergoes O-GlcNAcylation and that the latter protects proteins from proteasomal degradation. Our results suggest that by increasing protein O-GlcNAcylation levels, PGJ2 renders mature APP less prone to proteasomal degradation, thus shunting APP toward processing by α- and β-secretases.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsCaspasesCells, CulturedCytoplasmFemaleGlycosylationHumansInflammationMaleProstaglandin D2Proteasome Endopeptidase ComplexProteolysisRats, Sprague-Dawley9-deoxy-delta-9-prostaglandin D2Amyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesCaspasesProstaglandin D2Proteasome Endopeptidase ComplexApoptosisAPPO-GlcNAcylationProstaglandin J2Secretases

Identifiers

PMID29149631
PMCPMC5743611
OpenAlexW2769980514

What OpenQuestion holds

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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.