Evidence map›Paper›PMID 32429337›Full record

ArticleCells2020

Lactulose and Melibiose Inhibit α-Synuclein Aggregation and Up-Regulate Autophagy to Reduce Neuronal Vulnerability.

Chiung Mei Chen, Chih-Hsin Lin, Yih-Ru Wu, Chien-Yu Yen, Yu-Ting Huang, Jia-Lan Lin, Chung-Yin Lin, Wan-Ling Chen, Chih-Ying Chao, Guey-Jen Lee-Chen and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  6. Article
  7. Article
  8. Article
  9. Review
  10. The Role of Oxidative Stress in Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2020
    Review
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

12 authors at 2 institutions in 1 country.

Chiung Mei ChenDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.ORCID 0000-0002-0769-0353
Chih-Hsin LinDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Yih-Ru WuDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Chien-Yu YenDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.
Yu-Ting HuangTaipei First Girls High School, Taipei 10045, Taiwan.
Jia-Lan LinTaipei First Girls High School, Taipei 10045, Taiwan.
Chung-Yin LinMedical Imaging Research Center, Institute for Radiological Research, Chang Gung University/Chang Gung Memorial Hospital, Taoyuan 33302, Taiwan.
Wan-Ling ChenDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Chih-Ying ChaoDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.
Guey-Jen Lee-ChenDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.
Ming-Tsan SuDepartment of Life Science, National Taiwan Normal University, Taipei 11677, Taiwan.
Kuo-Hsuan ChangDepartment of Neurology, Chang-Gung Memorial Hospital, Chang-Gung University College of Medicine, Taoyuan 33302, Taiwan.ORCID 0000-0003-4972-9823
Chang Gung University · TWNational Taiwan Normal University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkinson's disease (PD) is a neurodegenerative disease characterized by selective dopaminergic (DAergic) neuronal degeneration in the substantia nigra (SN) and proteinaceous α-synuclein-positive Lewy bodies and Lewy neuritis. As a chemical chaperone to promote protein stability and an autophagy inducer to clear aggregate-prone proteins, a disaccharide trehalose has been reported to alleviate neurodegeneration in PD cells and mouse models. Its trehalase-indigestible analogs, lactulose and melibiose, also demonstrated potentials to reduce abnormal protein aggregation in spinocerebellar ataxia cell models. In this study, we showed the potential of lactulose and melibiose to inhibit α-synuclein aggregation using biochemical thioflavin T fluorescence, cryogenic transmission electron microscopy (cryo-TEM) and prokaryotic split Venus complementation assays. Lactulose and melibiose further reduced α-synuclein aggregation and associated oxidative stress, as well as protected cells against α-synuclein-induced neurotoxicity by up-regulating autophagy and nuclear factor, erythroid 2 like 2 (NRF2) pathway in DAergic neurons derived from SH-SY5Y cells over-expressing α-synuclein. Our findings strongly indicate the potential of lactulose and melibiose for mitigating PD neurodegeneration, offering new drug candidates for PD treatment.

Indexed as

Protein AggregatesUp-Regulationalpha-SynucleinAmino Acid SequenceAntioxidantsAutophagyBenzothiazolesCell LineCell SurvivalDopaminergic NeuronsFluorescenceGreen Fluorescent ProteinsHumansLactuloseMelibioseNeuronal Outgrowthalpha-SynucleinAntioxidantsBenzothiazolesGreen Fluorescent ProteinsLactuloseMelibioseNeuroprotective AgentsProtein Aggregatesthioflavin TTrehaloseautophagy inducerlactulosemelibioseParkinson’s diseaseα-synuclein aggregation inhibition

Identifiers

PMID32429337
PMCPMC7290909
OpenAlexW3024737031

What OpenQuestion holds

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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.