Evidence map›Paper›PMID 29241092›Full record

ArticleRedox biology2018

Trehalose protects against oxidative stress by regulating the Keap1-Nrf2 and autophagy pathways.

Yuhei Mizunoe, Masaki Kobayashi, Yuka Sudo, Shukoh Watanabe, Hiromine Yasukawa, Daiki Natori, Ayana Hoshino, Arisa Negishi, Naoyuki Okita, Masaaki Komatsu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
12.8field-weighted citation impact, top 1% 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

109 citing papers in PubMed, 234 citations in OpenAlex.

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  11. Antioxidants (Basel, Switzerland) · 2025
    Article
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  18. Understanding the role of trehalose in interactions betweenFrontiers in cellular and infection microbiology · 2025
    Review
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  20. Article

49 more citing papers are in PubMed but not listed here.

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

11 authors at 3 institutions in 1 country.

Yuhei MizunoeLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan; Translational Research Center, Research Institute of Science and Technology, Tokyo University of Science, Noda 278-8510, Japan.
Masaki KobayashiLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan; Translational Research Center, Research Institute of Science and Technology, Tokyo University of Science, Noda 278-8510, Japan.
Yuka SudoLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan; Translational Research Center, Research Institute of Science and Technology, Tokyo University of Science, Noda 278-8510, Japan.
Shukoh WatanabeLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan.
Hiromine YasukawaLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan.
Daiki NatoriLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan.
Ayana HoshinoLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan.
Arisa NegishiLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan.
Naoyuki OkitaTranslational Research Center, Research Institute of Science and Technology, Tokyo University of Science, Noda 278-8510, Japan; Department of Internal Medicine Research, Sasaki Institute, Sasaki Foundation, Tokyo 101-0062, Japan.
Masaaki KomatsuDepartment of Biochemistry, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8510, Japan.
Yoshikazu HigamiLaboratory of Molecular Pathology and Metabolic Disease, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Noda, Chiba 278-8510, Japan; Translational Research Center, Research Institute of Science and Technology, Tokyo University of Science, Noda 278-8510, Japan. Electronic address: higami@rs.noda.tus.ac.jp.
Tokyo University of Science · JPNiigata University · JPSasaki Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysfunction of autophagy, which regulates cellular homeostasis by degrading organelles and proteins, is associated with pathogenesis of various diseases such as cancer, neurodegeneration and metabolic disease. Trehalose, a naturally occurring nontoxic disaccharide found in plants, insects, microorganisms and invertebrates, but not in mammals, was reported to function as a mechanistic target of the rapamycin (mTOR)-independent inducer of autophagy. In addition, trehalose functions as an antioxidant though its underlying molecular mechanisms remain unclear. In this study, we showed that trehalose not only promoted autophagy, but also increased p62 protein expression, in an autophagy-independent manner. In addition, trehalose increased nuclear translocation of nuclear factor (erythroid-derived 2)-like 2 (Nrf2) in a p62-dependent manner and enhance expression of its downstream antioxidant factors, heme oxygenase-1 (Ho-1) and nicotinamide adenine dinucleotide phosphate quinone dehydrogenase 1 (Nqo1). Moreover, treatment with trehalose significantly reduced amount of reactive oxygen species. Collectively, these results suggested that trehalose can function as a novel activator of the p62-Keap1/Nrf2 pathway, in addition to inducing autophagy. Therefore, trehalose may be useful to treat many chronic diseases involving oxidative stress and dysfunction of autophagy.

Indexed as

AnimalsAutophagyAutophagy-Related Protein 5Heme Oxygenase-1HumansKelch-Like ECH-Associated Protein 1Membrane ProteinsMiceMice, KnockoutNAD(P)H Dehydrogenase (Quinone)NF-E2-Related Factor 2Oxidative StressProto-Oncogene Proteins c-yesSignal TransductionTOR Serine-Threonine KinasesTrehaloseAtg5 protein, mouseAutophagy-Related Protein 5Heme Oxygenase-1Hmox1 protein, mouseKelch-Like ECH-Associated Protein 1Membrane ProteinsNAD(P)H Dehydrogenase (Quinone)Nfe2l2 protein, mouseNF-E2-Related Factor 2Nqo1 protein, mouseProto-Oncogene Proteins c-yesTOR Serine-Threonine KinasesTrehaloseYes1 protein, mouseAntioxidantAutophagyKeap1–Nrf2 systemOxidative stressp62Trehalose

Identifiers

PMID29241092
PMCPMC5730428
OpenAlexW2755718135

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.