Evidence map›Paper›PMID 25567810›Full record

ArticleAmerican journal of physiology. Cell physiology2015

Myopathic changes in murine skeletal muscle lacking synemin.

Karla P García-Pelagio, Joaquin Muriel, Andrea O'Neill, Patrick F Desmond, Richard M Lovering, Linda Lund, Meredith Bond, Robert J Bloch

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Reorganization of chromatin architecture during prenatal development of porcine skeletal muscle.DNA research : an international journal for rapid publication of reports on genes and genomes · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Synemin Redefined: Multiple Binding Partners Results in Multifunctionality.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Deficiency of the intermediate filament synemin reduces bone mass in vivo.American journal of physiology. Cell physiology · 2016
    Article
  19. Article
  20. Effects of aging, exercise, and disease on force transfer in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2015
    Review
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

8 authors at 3 institutions in 1 country.

Karla P García-PelagioDepartment of Physiology, School of Medicine, University of Maryland, Baltimore, Maryland;
Joaquin MurielDepartment of Physiology, School of Medicine, University of Maryland, Baltimore, Maryland;
Andrea O'NeillDepartment of Physiology, School of Medicine, University of Maryland, Baltimore, Maryland;
Patrick F DesmondProgram in Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, Maryland;
Richard M LoveringDepartment of Orthopaedics, School of Medicine, University of Maryland, Baltimore, Maryland;
Linda LundMerrick School of Business, University of Baltimore, Baltimore, Maryland; and.
Meredith BondCollege of Sciences and Health Professions, Cleveland State University, Cleveland, Ohio.
Robert J BlochDepartment of Physiology, School of Medicine, University of Maryland, Baltimore, Maryland; rbloch@umaryland.edu.
University of Maryland, Baltimore · USCleveland State University · USUniversity of Baltimore · US

Funding

TRAINING PROGRAM IN INTEGRATIVE MEMBRANE BIOLOGYT32GM008181 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI RIZZO, MEGAN A, TRUDEAU, MATTHEW C · 1987 to 2022
$4.9M
TARGETING OF PKA BY AKAP100 IN AGING AND FAILING HEARTSR01AG016613 · NIA · UNIVERSITY OF MARYLAND BALTIMORE · PI BOND, MEREDITH · 2000 to 2009
$3.3M
Mechanisms of Force Loss in Injured and Dystrophic Skeletal MuscleR01AR059179 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI LOVERING, RICHARD M · 2010 to 2014
$1.4M
Synemin is an A-Kinase Anchoring Protein in the HeartR01HL079134 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI BOND, MEREDITH · 2005 to 2008
$1.4M
Intermediate Filaments & Costamere Structure & FunctionR01AR055928 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 2009 to 2010
$758k
NHLBI NIH HHS R01 HL079134NHLBI NIH HHS R01-HL-79134NIAMS NIH HHS R01 AR055928NIAMS NIH HHS R01-AR-055928NIAMS NIH HHS R01 AR059179NIA NIH HHS R01 AG016613NIA NIH HHS R01-AG-16613NIGMS NIH HHS T32 GM008181
6 · The paper itself

Abstract

Diseases of striated muscle linked to intermediate filament (IF) proteins are associated with defects in the organization of the contractile apparatus and its links to costameres, which connect the sarcomeres to the cell membrane. Here we study the role in skeletal muscle of synemin, a type IV IF protein, by examining mice null for synemin (synm-null). Synm-null mice have a mild skeletal muscle phenotype. Tibialis anterior (TA) muscles show a significant decrease in mean fiber diameter, a decrease in twitch and tetanic force, and an increase in susceptibility to injury caused by lengthening contractions. Organization of proteins associated with the contractile apparatus and costameres is not significantly altered in the synm-null. Elastimetry of the sarcolemma and associated contractile apparatus in extensor digitorum longus myofibers reveals a reduction in tension consistent with an increase in sarcolemmal deformability. Although fatigue after repeated isometric contractions is more marked in TA muscles of synm-null mice, the ability of the mice to run uphill on a treadmill is similar to controls. Our results suggest that synemin contributes to linkage between costameres and the contractile apparatus and that the absence of synemin results in decreased fiber size and increased sarcolemmal deformability and susceptibility to injury. Thus synemin plays a moderate but distinct role in fast twitch skeletal muscle.

Indexed as

Isometric ContractionMuscle StrengthAnimalsBiomechanical PhenomenaCostameresGenotypeIntermediate Filament ProteinsMaleMice, Inbred C57BLMice, KnockoutMuscle FatigueMuscle Fibers, Fast-TwitchMuscle, SkeletalMuscular DiseasesPhenotypeRunningIntermediate Filament Proteinssynemin protein, mousebiomechanical propertiescostamerescytoskeletondesminelastimetry

Identifiers

PMID25567810
PMCPMC4360028
OpenAlexW2324904309

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.