Evidence map›Paper›PMID 32843684›Full record

ArticleScientific reports2020

Atrogin1-induced loss of aquaporin 4 in myocytes leads to skeletal muscle atrophy.

Seok Won Chung, Ja-Yeon Kim, Jong Pil Yoon, Dong Won Suh, Woo Jin Yeo, Yong-Soo Lee

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  8. Review
  9. Assessing the Role of Aquaporin 4 in Skeletal Muscle Function.International journal of molecular sciences · 2023
    Review
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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 3 institutions in 1 country.

Seok Won ChungDepartment of Orthopedic Surgery, Research Institute of Medical Science, Konkuk University School of Medicine, Seoul, Republic of Korea.
Ja-Yeon KimDepartment of Orthopedic Surgery, Research Institute of Medical Science, Konkuk University School of Medicine, Seoul, Republic of Korea.
Jong Pil YoonDepartment of Orthopedic Surgery, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Dong Won SuhJoint Center, Barunsesang Hospital, #75-5, Yatap-ro, Seongnam-si, Gyeonggi-do, 13497, Republic of Korea.
Woo Jin YeoJoint Center, Barunsesang Hospital, #75-5, Yatap-ro, Seongnam-si, Gyeonggi-do, 13497, Republic of Korea.
Yong-Soo LeeDepartment of Orthopedic Surgery, Research Institute of Medical Science, Konkuk University School of Medicine, Seoul, Republic of Korea. hrcyslee@yahoo.co.kr.
Yang Hospital · KRKonkuk University · KRKyungpook National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The water channel aquaporin 4 (AQP4) regulates the flux of water across the cell membrane, maintaining cellular homeostasis. Since AQP4 is enriched in the sarcolemma of skeletal muscle, a functional defect in AQP4 may cause skeletal muscle dysfunction. To investigate a novel mechanism underlying skeletal muscle atrophy, we examined AQP4 expression and its regulation in muscle using the rotator cuff tear (RCT) model. Human and mouse AQP4 expression was significantly decreased in atrophied muscle resulting from RCT. The size and the number of myotubes were reduced following AQP4 knockdown. Atrogin 1-mediated ubiquitination of AQP4 was verified with an ubiquitination assay after immunoprecipitation of AQP4 with an anti-AQP4 antibody. In this study, we identified high mobility group box 1 (HMGB1) as a potent upstream regulator of atrogin 1 expression. Atrogin 1 expression was increased by recombinant mouse HMGB1 protein, and the HMGB1-induced atrogin 1 expression was mediated via NF-κB signaling. Our study suggests that loss of AQP4 appears to be involved in myocyte shrinkage after RCT, and its degradation is mediated by atrogin 1-dependent ubiquitination. HMGB1, in its function as a signaling molecule upstream of the ubiquitin ligase atrogin 1, was found to be a novel regulator of muscle atrophy.

Indexed as

AdultAnimalsAquaporin 4FemaleHMGB1 ProteinHumansMaleMiceMice, Inbred C57BLMuscle Fibers, SkeletalMuscle ProteinsMuscle, SkeletalMuscular AtrophyNF-kappa BSignal TransductionSKP Cullin F-Box Protein LigasesAquaporin 4Fbxo32 protein, mouseHMGB1 ProteinMuscle ProteinsNF-kappa BSKP Cullin F-Box Protein LigasesTripartite Motif ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID32843684
PMCPMC7447774
OpenAlexW3080124705

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.