Evidence map›Paper›PMID 28104914›Full record

ArticleExperimental & molecular medicine2017

Docosahexaenoic acid-mediated protein aggregates may reduce proteasome activity and delay myotube degradation during muscle atrophy in vitro.

Seung Kyun Shin, Ji Hyeon Kim, Jung Hoon Lee, Young Hoon Son, Min Wook Lee, Hak Joong Kim, Sue Ah Noh, Kwang Pyo Kim, In-Gyu Kim, Min Jae Lee

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  5. Review
  6. Potential Therapeutic Strategies for Skeletal Muscle Atrophy.Antioxidants (Basel, Switzerland) · 2022
    Review
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  11. Article
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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

10 authors at 3 institutions in 1 country.

Seung Kyun ShinDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin, Korea.
Ji Hyeon KimDepartment of Biomedical Sciences, Seoul National University Graduate School, Seoul, Korea.
Jung Hoon LeeDepartment of Biochemistry and Molecular Biology, Seoul National University College of Medicine, Seoul, Korea.
Young Hoon SonDepartment of Biomedical Sciences, Seoul National University Graduate School, Seoul, Korea.
Min Wook LeeDepartment of Chemistry, College of Science, Korea University, Seoul, Korea.
Hak Joong KimDepartment of Chemistry, College of Science, Korea University, Seoul, Korea.
Sue Ah NohDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin, Korea.
Kwang Pyo KimDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin, Korea.
In-Gyu KimDepartment of Biomedical Sciences, Seoul National University Graduate School, Seoul, Korea.
Min Jae LeeDepartment of Biomedical Sciences, Seoul National University Graduate School, Seoul, Korea.ORCID 0000-0002-3252-6467
Seoul National University · KRKyung Hee University · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasomes are the primary degradation machinery for oxidatively damaged proteins that compose a class of misfolded protein substrates. Cellular levels of reactive oxygen species increase with age and this cellular propensity is particularly harmful when combined with the age-associated development of various human disorders including cancer, neurodegenerative disease and muscle atrophy. Proteasome activity is reportedly downregulated in these disease conditions. Herein, we report that docosahexaenoic acid (DHA), a major dietary omega-3 polyunsaturated fatty acid, mediates intermolecular protein cross-linkages through oxidation, and the resulting protein aggregates potently reduce proteasomal activity both in vitro and in cultured cells. Cellular models overexpressing aggregation-prone proteins such as tau showed significantly elevated levels of tau aggregates and total ubiquitin conjugates in the presence of DHA, thereby reflecting suppressed proteasome activity. Strong synergetic cytotoxicity was observed when the cells overexpressing tau were simultaneously treated with DHA. Antioxidant N-acetyl cysteine significantly desensitized the cells to DHA-induced oxidative stress. DHA significantly delayed the proteasomal degradation of muscle proteins in a cellular atrophy model. Thus, the results of our study identified DHA as a potent inducer of cellular protein aggregates that inhibit proteasome activity and potentially delay systemic muscle protein degradation in certain pathologic conditions.

Indexed as

AnimalsAntioxidantsCell LineCell SurvivalDocosahexaenoic AcidsHumansMuscle Fibers, SkeletalMuscle ProteinsMuscular AtrophyProteasome Endopeptidase ComplexProtein AggregatesProtein Aggregation, PathologicalProteolysisProto-Oncogene Protein c-fli-1Reactive Oxygen SpeciesRecombinant ProteinsAntioxidantsDocosahexaenoic AcidsFLI1 protein, humanMuscle ProteinsProteasome Endopeptidase ComplexProtein AggregatesProto-Oncogene Protein c-fli-1Reactive Oxygen SpeciesRecombinant Proteinstau ProteinsUbiquitin

Identifiers

PMID28104914
PMCPMC5291838
OpenAlexW2578242919

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.