Evidence map›Paper›PMID 30262782›Full record

ArticleInternational journal of molecular sciences2018

AMPK Mediates Muscle Mass Change But Not the Transition of Myosin Heavy Chain Isoforms during Unloading and Reloading of Skeletal Muscles in Mice.

Tatsuro Egawa, Yoshitaka Ohno, Ayumi Goto, Shingo Yokoyama, Tatsuya Hayashi, Katsumasa Goto

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
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  9. Article
  10. AMP-Activated Protein Kinase Signalling.International journal of molecular sciences · 2019
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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.

Tatsuro EgawaDepartment of Physiology, Graduate School of Health Sciences, Toyohashi SOZO University, Toyohashi, Aichi 440-8511, Japan. egawa.tatsuro.4u@kyoto-u.ac.jp.ORCID 0000-0001-9363-1589
Yoshitaka OhnoLaboratory of Physiology, School of Health Sciences, Toyohashi SOZO University, Toyohashi, Aichi 440-8511, Japan. yohno@sozo.ac.jp.
Ayumi GotoDepartment of Physiology, Graduate School of Health Sciences, Toyohashi SOZO University, Toyohashi, Aichi 440-8511, Japan. ayumi.goto8@gmail.com.
Shingo YokoyamaLaboratory of Physiology, School of Health Sciences, Toyohashi SOZO University, Toyohashi, Aichi 440-8511, Japan. s-yokoyama@sozo.ac.jp.
Tatsuya HayashiLaboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, Japan. tatsuya@kuhp.kyoto-u.ac.jp.ORCID 0000-0001-7600-4735
Katsumasa GotoDepartment of Physiology, Graduate School of Health Sciences, Toyohashi SOZO University, Toyohashi, Aichi 440-8511, Japan. gotok@sepia.ocn.ne.jp.
Kyoto University · JPToyohashi Sozo College · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

5'AMP-activated protein kinase (AMPK) plays an important role in the regulation of skeletal muscle mass and fiber-type distribution. However, it is unclear whether AMPK is involved in muscle mass change or transition of myosin heavy chain (MyHC) isoforms in response to unloading or increased loading. Here, we checked whether AMPK controls muscle mass change and transition of MyHC isoforms during unloading and reloading using mice expressing a skeletal-muscle-specific dominant-negative AMPKα1 (AMPK-DN). Fourteen days of hindlimb unloading reduced the soleus muscle weight in wild-type and AMPK-DN mice, but reduction in the muscle mass was partly attenuated in AMPK-DN mice. There was no difference in the regrown muscle weight between the mice after 7 days of reloading, and there was concomitantly reduced AMPKα2 activity, however it was higher in AMPK-DN mice after 14 days reloading. No difference was observed between the mice in relation to the levels of slow-type MyHC I, fast-type MyHC IIa/x, and MyHC IIb isoforms following unloading and reloading. The levels of 72-kDa heat-shock protein, which preserves muscle mass, increased in AMPK-DN-mice. Our results indicate that AMPK mediates the progress of atrophy during unloading and regrowth of atrophied muscles following reloading, but it does not influence the transition of MyHC isoforms.

Indexed as

AMP-Activated Protein KinasesAnimalsHindlimb SuspensionHSP72 Heat-Shock ProteinsMaleMiceMice, Inbred C57BLMuscle, SkeletalMuscular AtrophyMyosin Heavy ChainsPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaProtein IsoformsSirtuin 1AMP-Activated Protein KinasesHSP72 Heat-Shock ProteinsMyosin Heavy ChainsPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPpargc1a protein, mousePrkaa2 protein, mouseProtein IsoformsSirt1 protein, mouseSirtuin 1atrophyfiber-typeheat shock proteinperoxisome proliferator-activated receptor gamma coactivator 1-α (PGC1α)regrowthsirtuin 1 (SIRT1)

Identifiers

PMID30262782
PMCPMC6212939
OpenAlexW2893764131

What OpenQuestion holds

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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.