Evidence map›Paper›PMID 32861245›Full record

ArticleJournal of neuroinflammation2020

Serum amyloid A inhibits astrocyte migration via activating p38 MAPK.

Aihua Lin, Jin Liu, Ping Gong, Yanqing Chen, Haibo Zhang, Yan Zhang, Yang Yu

Open access · goldAbstract read
In one paragraph

Article in Journal of neuroinflammation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 18% 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, 27 citations in OpenAlex.

  1. Article
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  4. Elevated Serum Amyloid A2 and A4 in Patients With Guillain-Barré Syndrome.Journal of clinical neurology (Seoul, Korea) · 2025
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  19. Pyroptosis in spinal cord injury.Frontiers in cellular neuroscience · 2022
    Review
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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

7 authors at 1 institution in 1 country.

Aihua LinEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Jin LiuEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Ping GongEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Yanqing ChenEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Haibo ZhangEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Yan ZhangEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.
Yang YuEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, and School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China. yuyang2011@sjtu.edu.cn.ORCID http://orcid.org/0000-0002-6256-6697
Shanghai Jiao Tong University · CN

Funding

National Natural Science Foundation of China 81571027National Natural Science Foundation of China 81870835
6 · The paper itself

Abstract

backgroundThe accumulation of astrocytes around senile plaques is one of the pathological characteristics in Alzheimer's disease (AD). Serum amyloid A (SAA), known as a major acute-phase protein, colocalizes with senile plaques in AD patients. Here, we demonstrate the role of SAA in astrocyte migration.

methodsThe effects of SAA on astrocyte activation and accumulation around amyloid β (Aβ) deposits were detected in APP/PS1 transgenic mice mated with Saa3

resultsSaa3 expression was significantly induced in aged APP/PS1 transgenic mouse brain. Saa3 deficiency exacerbated astrocyte activation and increased the number of astrocytes around Aβ deposits in APP/PS1 mice. In vitro studies demonstrated that SAA inhibited the migration of primary cultures of astrocytes and U251 cells. Mechanistic studies showed that SAA inhibited astrocyte polarization and protrusion formation via disrupting actin and microtubule reorganization and Golgi reorientation. Inhibition of the p38 MAPK pathway abolished the suppression of SAA on astrocyte migration and polarization.

conclusionsThese results suggest that increased SAA in the brain of APP/PS1 mice inhibits the migration of astrocytes to amyloid plaques by activating the p38 MAPK pathway.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsAstrocytesBrainCell Line, TumorCell MovementDisease Models, AnimalHumansMiceMice, Transgenicp38 Mitogen-Activated Protein KinasesPresenilin-1Serum Amyloid A ProteinAmyloid beta-Protein Precursorp38 Mitogen-Activated Protein KinasesPresenilin-1Serum Amyloid A ProteinAlzheimer’s diseaseAstrocytesMigrationp38 MAPKSerum amyloid A

Identifiers

PMID32861245
PMCPMC7456509
OpenAlexW3082489735

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.