Evidence map›Paper›PMID 28981090›Full record

ArticleCell death & disease2017

Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation.

Ye-Seul Yoon, Eun-Duk Cho, Woo Jung Ahn, Kyung Won Lee, Seung-Jae Lee, He-Jin Lee

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

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  16. Autophagy in the normal and diseased cornea.Experimental eye research · 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

6 authors at 2 institutions in 1 country.

Ye-Seul YoonDepartment of Anatomy, School of Medicine, Konkuk University, Seoul 05029, South Korea.
Eun-Duk ChoDepartment of Anatomy, School of Medicine, Konkuk University, Seoul 05029, South Korea.
Woo Jung AhnDepartment of Medicine, Seoul National University College of Medicine, Seoul, South Korea.
Kyung Won LeeIBST, Konkuk University, Seoul 05029, Korea.
Seung-Jae LeeDepartment of Medicine, Seoul National University College of Medicine, Seoul, South Korea.
He-Jin LeeDepartment of Anatomy, School of Medicine, Konkuk University, Seoul 05029, South Korea.
Konkuk University · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a pivotal intracellular process by which cellular macromolecules are degraded upon various stimuli. A failure in the degradation of autophagic substrates such as impaired organelles and protein aggregates leads to their accumulations, which are characteristics of many neurodegenerative diseases. Pharmacological activation of autophagy has thus been considered a prospective therapeutic approach for treating neurodegenerative diseases. Among a number of autophagy-inducing agents, trehalose has received attention for its beneficial effects in different disease models of neurodegeneration. However, how trehalose promotes autophagy has not been fully revealed. We investigated the influence of trehalose and other disaccharides upon autophagic flux and aggregation of α-synuclein, a protein linked to Parkinson's disease. In differentiated human neuroblastoma and primary rat cortical neuron culture models, treatment with trehalose and other disaccharides resulted in accumulation of lipidated LC3 (LC3-II), p62, and autophagosomes, whereas it decreased autolysosomes. On the other hand, addition of Bafilomycin A1 to trehalose treatments had relatively marginal effect, an indicative of autophagic flux blockage. In concordance with these results, the cells treated with trehalose exhibited an incremental tendency in α-synuclein aggregation. Secretion of α-synuclein was also elevated in the culture medium upon trehalose treatment, thereby significantly increasing intercellular transmission of this protein. Despite the substantial increase in α-synuclein aggregation, which normally leads to cell death, cell viability was not affected upon treatment with trehalose, suggesting an autophagy-independent protective function of trehalose against protein aggregates. This study demonstrates that, although trehalose has been widely considered an autophagic inducer, it may be actually a potent blocker of the autophagic flux.

Indexed as

alpha-SynucleinAnimalsAutophagosomesAutophagyCell SurvivalDisaccharidesHumansLysosomesMicrotubule-Associated ProteinsNeuronsParkinson DiseasePrimary Cell CultureProtein Aggregation, PathologicalRatsRNA-Binding ProteinsTrehalosealpha-SynucleinDisaccharidesMAP1LC3A protein, humanMicrotubule-Associated ProteinsP62 protein, humanRNA-Binding ProteinsTrehalose

Identifiers

PMID28981090
PMCPMC5682667
OpenAlexW2763542013

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Registered trials

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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.