Evidence map›Paper›PMID 31165943›Full record

ArticleCellular and molecular neurobiology2019

Enhancing the Astrocytic Clearance of Extracellular α-Synuclein Aggregates by Ginkgolides Attenuates Neural Cell Injury.

Jun Hua, Nuo Yin, Shi Xu, Qiang Chen, Tingting Tao, Ji Zhang, Jianhua Ding, Yi Fan, Gang Hu

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular neurobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.4field-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

24 citing papers in PubMed, 32 citations in OpenAlex.

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  16. Neuroinflammation and Autophagy in Parkinson's Disease-Novel Perspectives.International journal of molecular sciences · 2022
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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

9 authors at 5 institutions in 1 country.

Jun HuaJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Nuo YinJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Shi XuJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Qiang ChenJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Tingting TaoJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Ji ZhangDivision of Clinical Pharmacy, Department of Pharmacy, The First Affiliated Hospital of Nanjing Medical University, Nanjing, 210029, Jiangsu, China.
Jianhua DingJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China.
Yi FanJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China. yfan@njmu.edu.cn.ORCID http://orcid.org/0000-0003-1783-3220
Gang HuJiangsu Key Laboratory of Neurodegeneration, Department of Pharmacology, Nanjing Medical University, 101 Longmian Road, Nanjing, 211166, Jiangsu, China. ghu@njmu.edu.cn.
Nanjing Medical University · CNChina Pharmaceutical University · CNGuangzhou University of Chinese Medicine · CNJiangsu Province Hospital · CNNanjing University of Chinese Medicine · CN

Funding

National Natural Science Foundation of China 81673408National Natural Science Foundation of China 81703485
6 · The paper itself

Abstract

The accumulation of aggregated forms of the α-Synuclein (α-Syn) is associated with the pathogenesis of Parkinson's disease (PD), and the efficient clearance of aggregated α-Syn represents a potential approach in PD therapy. Astrocytes are the most numerous glia cells in the brain and play an essential role in supporting brain functions in PD state. In the present study, we demonstrated that cultured primary astrocytes engulfed and degraded extracellular aggregated recombinant human α-Syn. Meanwhile, we observed that the clearance of α-Syn by astrocytes was abolished by proteasome inhibitor MG132 and autophagy inhibitor 3-methyladenine (3MA). We further showed that intracellular α-Syn was reduced after ginkgolide B (GB) and bilobalide (BB) treatment, and the decrease was reversed by MG132 and 3MA. More importantly, GB and BB reduced indirect neurotoxicity to neurons induced by α-Syn-stimulated astrocytic conditioned medium. Together, we firstly find that astrocytes can engulf and degrade α-Syn aggregates via the proteasome and autophagy pathways, and further show that GB and BB enhance astrocytic clearance of α-Syn, which gives us an insight into the novel therapy for PD in future.

Indexed as

Protein Aggregatesalpha-SynucleinAnimalsAstrocytesAutophagyCell Line, TumorCulture Media, ConditionedCyclopentanesEndocytosisExtracellular SpaceFuransGinkgolidesHumansLysosomesMice, Inbred C57BLNeuronsalpha-SynucleinbilobalideCulture Media, ConditionedCyclopentanesFuransGinkgolidesProteasome Endopeptidase ComplexProtein AggregatesRecombinant ProteinsUbiquitinAstrocytesAutophagyBilobalideGinkgolide Bα-Synuclein

Identifiers

PMID31165943
PMCPMC11457828
OpenAlexW2971120270

What OpenQuestion holds

Textmetadata
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.