Evidence map›Paper›PMID 21565991›Full record

ArticleJournal of applied physiology (Bethesda, Md. : 1985)2011

Decreased specific force and power production of muscle fibers from myostatin-deficient mice are associated with a suppression of protein degradation.

Christopher L Mendias, Erdan Kayupov, Joshua R Bradley, Susan V Brooks, Dennis R Claflin

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of applied physiology (Bethesda, Md. : 1985), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.6field-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

34 citing papers in PubMed, 74 citations in OpenAlex.

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  5. Paraspinal muscle fibre structural and contractile characteristics demonstrate distinct irregularities in patients with spinal degeneration and deformity.European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society · 2024
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  15. Pharmacological inhibition of myostatin protects against skeletal muscle atrophy and weakness after anterior cruciate ligament tear.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2017
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Christopher L MendiasSchool of Kinesiology, Department of Orthopaedic Surgery, University of Michigan, 109 Zina Pitcher Pl., BSRB 2017, Ann Arbor, MI 48109-2200, USA. cmendias@umich.edu
Erdan Kayupov
Joshua R Bradley
Susan V Brooks
Dennis R Claflin
Institute of Biophysics and Biomedical Engineering · BGInternational College of Applied Kinesiology-USA · USSociety for Neuroscience · US

Funding

Mechanisms underlying mechanical properties of muscle-tendon unitsR01AR055624 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, SUSAN V · 2008 to 2012
$1.6M
Faculty Recruitment to Musculoskeletal Research ConsortiumP30AR058920 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GOLDSTEIN, STEVEN A · 2009 to 2010
$780k
NIAMS NIH HHS AR055624NIAMS NIH HHS AR058920NIAMS NIH HHS P30 AR058920NIAMS NIH HHS R01 AR055624
6 · The paper itself

Abstract

Myostatin (MSTN) is a member of the transforming growth factor-β superfamily of cytokines and is a negative regulator of skeletal muscle mass. Compared with MSTN(+/+) mice, the extensor digitorum longus muscles of MSTN(-/-) mice exhibit hypertrophy, hyperplasia, and greater maximum isometric force production (F(o)), but decreased specific maximum isometric force (sF(o); F(o) normalized by muscle cross-sectional area). The reason for the reduction in sF(o) was not known. Studies in myotubes indicate that inhibiting myostatin may increase muscle mass by decreasing the expression of the E3 ubiquitin ligase atrogin-1, which could impact the force-generating capacity and size of muscle fibers. To gain a greater understanding of the influence of myostatin on muscle contractility, we determined the impact of myostatin deficiency on the contractility of permeabilized muscle fibers and on the levels of atrogin-1 and ubiquitinated myosin heavy chain in whole muscle. We hypothesized that single fibers from MSTN(-/-) mice have a greater F(o), but no difference in sF(o), and a decrease in atrogin-1 and ubiquitin-tagged myosin heavy chain levels. The results indicated that fibers from MSTN(-/-) mice have a greater cross-sectional area, but do not have a greater F(o) and have a sF(o) that is significantly lower than fibers from MSTN(+/+) mice. The extensor digitorum longus muscles from MSTN(-/-) mice also have reduced levels of atrogin-1 and ubiquitinated myosin heavy chain. These findings suggest that myostatin inhibition in otherwise healthy muscle increases the size of muscle fibers and decreases atrogin-1 levels, but does not increase the force production of individual muscle fibers.

Indexed as

Isometric ContractionMuscle StrengthAnimalsHyperplasiaHypertrophyMaleMiceMice, Inbred C57BLMice, KnockoutMuscle Fibers, SkeletalMuscle ProteinsMyosin Heavy ChainsMyostatinProtein Processing, Post-TranslationalSKP Cullin F-Box Protein LigasesUbiquitinated ProteinsFbxo32 protein, mouseMstn protein, mouseMuscle ProteinsMyosin Heavy ChainsMyostatinSKP Cullin F-Box Protein LigasesUbiquitinated Proteins

Identifiers

PMID21565991
PMCPMC3137541
OpenAlexW2097306933

What OpenQuestion holds

Textmetadata
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.