Evidence map›Paper›PMID 33804171›Full record

ArticleMarine drugs2021

Dieckol Ameliorates Aβ Production via PI3K/Akt/GSK-3β Regulated APP Processing in SweAPP N2a Cell.

Jeong-Hyun Yoon, Nayoung Lee, Kumju Youn, Mi Ra Jo, Hyeung-Rak Kim, Dong-Seok Lee, Chi-Tang Ho, Mira Jun

Open access · goldAbstract readComparative Study
In one paragraph

Article in Marine drugs, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
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  8. Foods (Basel, Switzerland) · 2025
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  10. Antioxidants (Basel, Switzerland) · 2024
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  11. Review
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  14. Review
  15. Review
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  17. Review
  18. Aberrant Energy Metabolism in Alzheimer's Disease.Journal of translational internal medicine · 2022
    Article
  19. Article
  20. Article
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 5 institutions in 2 countries.

Jeong-Hyun YoonDepartment of Health Sciences, The graduate School of Dong-A University, Busan 49315, Korea.
Nayoung LeeDepartment of Health Sciences, The graduate School of Dong-A University, Busan 49315, Korea.
Kumju YounDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Korea.ORCID 0000-0002-3124-2665
Mi Ra JoDivision of Food Safety and Processing Research, National Institute of Fisheries Science, Busan 46083, Korea.
Hyeung-Rak KimDepartment of Food Science and Nutrition, Pukyong National University, Busan 48513, Korea.
Dong-Seok LeeSchool of Life Sciences & Biotechnology, College of Natural Sciences, Kyungpook National University, Daegu 41566, Korea.ORCID 0000-0002-7106-1615
Chi-Tang HoDepartment of Food Science, Rutgers University, New Brunswick, NJ 08901, USA.ORCID 0000-0001-8273-2085
Mira JunDepartment of Health Sciences, The graduate School of Dong-A University, Busan 49315, Korea.
Dong-A University · KRKyungpook National University · KRNational Institute of Fisheries Science · KRPukyong National University · KRRutgers, The State University of New Jersey · US

Funding

National Research Foundation of Korea NRF-2019R1A2C2006237
6 · The paper itself

Abstract

The proteolytic processing of amyloid precursor protein (APP) by β-secretase (BACE1) and γ-secretase releases amyloid-β peptide (Aβ), which deposits in amyloid plaques and contributes to the initial causative events of Alzheimer's disease (AD). In the present study, the regulatory mechanism of APP processing of three phlorotannins was elucidated in Swedish mutant APP overexpressed N2a (SweAPP N2a) cells. Among the tested compounds, dieckol exhibited the highest inhibitory effect on both intra- and extracellular Aβ accumulation. In addition, dieckol regulated the APP processing enzymes, such as α-secretase (ADAM10), β-secretase, and γ-secretase, presenilin-1 (PS1), and their proteolytic products, sAPPα and sAPPβ, implying that the compound acts on both the amyloidogenic and non-amyloidogenic pathways. In addition, dieckol increased the phosphorylation of protein kinase B (Akt) at Ser473 and GSK-3β at Ser9, suggesting dieckol induced the activation of Akt, which phosphorylated GSK-3β. The specific phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 triggered GSK-3β activation and Aβ expression. In addition, co-treatment with LY294002 noticeably blocked the effect of dieckol on Aβ production, demonstrating that dieckol promoted the PI3K/Akt signaling pathway, which in turn inactivated GSK-3β, resulting in the reduction in Aβ levels.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBenzofuransCell LineChromonesGlycogen Synthase Kinase 3 betaMiceMorpholinesPhosphatidylinositol 3-KinaseProto-Oncogene Proteins c-aktSignal TransductionTannins2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneAmyloid beta-PeptidesAmyloid beta-Protein PrecursorBenzofuransChromonesdieckolGlycogen Synthase Kinase 3 betaMorpholinesPhosphatidylinositol 3-KinaseProto-Oncogene Proteins c-aktTanninsAlzheimer’s diseaseamyloid-beta peptidedieckolGSK-3βSweAPP N2a

Identifiers

PMID33804171
PMCPMC8001366
OpenAlexW3138780785

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.