Evidence map›Paper›PMID 30233076›Full record

ArticleNeural regeneration research2018

SIRT1 facilitates amyloid beta peptide degradation by upregulating lysosome number in primary astrocytes.

Min-Zhe Li, Liang-Jun Zheng, Jian Shen, Xin-Ya Li, Qi Zhang, Xue Bai, Qing-Song Wang, Jian-Guo Ji

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

Article in Neural regeneration research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.6field-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

45 citing papers in PubMed, 79 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Min-Zhe LiGeneral Surgery Department, Beijing Chao-Yang Hospital, Capital Medical University, Beijing, China.
Liang-Jun ZhengState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Jian ShenGeneral Surgery Department, Beijing Chao-Yang Hospital, Capital Medical University, Beijing, China.
Xin-Ya LiState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Qi ZhangState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Xue BaiState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Qing-Song WangState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Jian-Guo JiState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing, China.
Peking University · CNBeijing Chao-Yang Hospital · CNCapital Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies have shown that sirtuin 1 (SIRT1) reduces the production of neuronal amyloid beta (Aβ) and inhibits the inflammatory response of glial cells, thereby generating a neuroprotective effect against Aβ neurotoxicity in animal models of Alzheimer's disease. However, the protective effect of SIRT1 on astrocytes is still under investigation. This study established a time point model for the clearance of Aβ in primary astrocytes. Results showed that 12 hours of culture was sufficient for endocytosis of oligomeric Aβ, and 36 hours sufficient for effective degradation. Immunofluorescence demonstrated that Aβ degradation in primary astrocytes relies on lysosome function. Enzymatic agonists or SIRT1 inhibitors were used to stimulate cells over a concentration gradient. Aβ was co-cultured for 36 hours in medium. Western blot assay results under different conditions revealed that SIRT1 relies on its deacetylase activity to promote intracellular Aβ degradation. The experiment further screened SIRT1 using quantitative proteomics to investigate downstream, differentially expressed proteins in the Aβ degradation pathway and selected the ones related to enzyme activity of SIRT1. Most of the differentially expressed proteins detected are close to the primary astrocyte lysosomal pathway. Immunofluorescence staining demonstrated that SIRT1 relies on its deacetylase activity to upregulate lysosome number in primary astrocytes. Taken together, these findings confirm that SIRT1 relies on its deacetylase activity to upregulate lysosome number, thereby facilitating oligomeric Aβ degradation in primary astrocytes.

Indexed as

Alzheimer's diseaseamyloid beta peptideastrocytesgliocyteslysosomenerve regenerationneural regenerationneurodegenerationpeptide degradationquantitative proteomicssirtuin1time point model

Identifiers

PMID30233076
PMCPMC6183050
OpenAlexW2890246453

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.