Evidence map›Paper›PMID 34074054›Full record

ArticleInternational journal of molecular sciences2021

Ganoderic Acid A Promotes Amyloid-β Clearance (In Vitro) and Ameliorates Cognitive Deficiency in Alzheimer's Disease (Mouse Model) through Autophagy Induced by Activating Axl.

Li-Feng-Rong Qi, Shuai Liu, Yu-Ci Liu, Ping Li, Xiaojun Xu

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

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.1field-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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. Article
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  7. Review
  8. Intranasal administration ofFrontiers in pharmacology · 2025
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  11. The Biological Activity ofMolecules (Basel, Switzerland) · 2024
    Review
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  13. Article
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  15. Article
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  17. Identification of potential neuroprotective compound fromAging medicine (Milton (N.S.W)) · 2023
    Article
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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

5 authors at 1 institution in 1 country.

Li-Feng-Rong QiState Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
Shuai LiuState Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
Yu-Ci LiuState Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
Ping LiState Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
Xiaojun XuState Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.ORCID 0000-0003-4379-8748
China Pharmaceutical University · CN

Funding

National Natural Science Foundation of China 81973500
6 · The paper itself

Abstract

Alzheimer's disease (AD) is thought to be caused by amyloid-β (Aβ) accumulation in the central nervous system due to deficient clearance. The aim of the present study was to investigate the effect of ganoderic acid A (GAA) on Aβ clearance in microglia and its anti-AD activity. Aβ degradation in BV2 microglial cells was determined using an intracellular Aβ clearance assay. GAA stimulated autophagosome formation via the Axl receptor tyrosine kinase (Axl)/RAC/CDC42-activated kinase 1 (Pak1) pathway was determined by Western blot analyses, and fluorescence-labeled Aβ42 was localized in lysosomes in confocal laser microscopy images. The in vivo anti-AD activity of GAA was evaluated by object recognition and Morris water maze (MWM) tests in an AD mouse model following intracerebroventricular injection of aggregated Aβ42. The autophagy level in the hippocampus was assayed by immunohistochemical assessment against microtubule-associated proteins 1A/1B light-chain 3B (LC3B). Intracellular Aβ42 levels were significantly reduced by GAA treatment in microglial cells. Additionally, GAA activated autophagy according to increased LC3B-II levels, with this increased autophagy stimulated by upregulating Axl and Pak1 phosphorylation. The effect of eliminating Aβ by GAA through autophagy was reversed by R428, an Axl inhibitor, or IPA-3, a Pak1 inhibitor. Consistent with the cell-based assay, GAA ameliorated cognitive deficiency and reduced Aβ42 levels in an AD mouse model. Furthermore, LC3B expression in the hippocampus was up-regulated by GAA treatment, with these GAA-specific effects abolished by R428. GAA promoted Aβ clearance by enhancing autophagy via the Axl/Pak1 signaling pathway in microglial cells and ameliorated cognitive deficiency in an AD mouse model.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAutophagosomesAutophagyAxl Receptor Tyrosine KinaseCell LineDisease Models, AnimalHeptanoic AcidsHippocampusImmunohistochemistryLanosterolLysosomesMaleMiceMice, Inbred C57BLAmyloid beta-PeptidesAxl Receptor Tyrosine KinaseAXL receptor tyrosine kinase, mouseganoderic acid AHeptanoic AcidsLanosterolp21-Activated KinasesPak1 protein, mouseProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesAlzheimer’s diseaseamyloid βautophagyAxlganoderic acid A

Identifiers

PMID34074054
PMCPMC8197357
OpenAlexW3165550821

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.