Cited by 51Muscle Physiology and DisordersSpaceflight effects on biologyCell Adhesion Molecules Research

Costamere remodeling with muscle loading and unloading in healthy young men

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Li, Ruowei, Narici, Marco V., Erskine, Robert M., Seynnes, Olivier R., Rittweger, Jörn, Pišot, Rado, Šimunič, Boštjan, Flück, Martin·2013·Journal of Anatomy

Abstract

Costameres are mechano‐sensory sites of focal adhesion in the sarcolemma that provide a structural anchor for myofibrils. Their turnover is regulated by integrin‐associated focal adhesion kinase (FAK). We hypothesized that changes in content of costamere components (beta 1 integrin, FAK, meta‐vinculin, gamma‐vinculin) with increased and reduced loading of human anti‐gravity muscle would: (i) relate to changes in muscle size and molecular parameters of muscle size regulation [p70 S 6 K, myosin heavy chain (MHC)1 and MHC II A]; (ii) correspond to adjustments in activity and expression of FAK, and its negative regulator, FRNK; and (iii) reflect the temporal response to reduced and increased loading. Unloading induced a progressive decline in thickness of human vastus lateralis muscle after 8 and 34 days of bedrest (−4% and −14%, respectively; n = 9), contrasting the increase in muscle thickness after 10 and 27 days of resistance training (+5% and +13%; n = 6). Changes in muscle thickness were correlated with changes in cross‐sectional area of type I muscle fibers (r = 0.66) and beta 1 integrin content (r = 0.76) at the mid‐point of altered loading. Changes in meta‐vinculin and FAK‐p Y 397 content were correlated (r = 0.85) and differed, together with the changes of beta 1 integrin, MHCI, MHCII and p70 S 6 K, between the mid‐ and end‐point of resistance training. By contrast, costamere protein level changes did not differ between time points of bedrest. The findings emphasize the role of FAK‐regulated costamere turnover in the load‐dependent addition and removal of myofibrils, and argue for two phases of muscle remodeling with resistance training, which do not manifest at the macroscopic level.

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  • Changes in the extracellular matrix with unloading may contribute to the nonuniform force loss.

    “Additionally, as the extracellular matrix contributes to lateral force transmission (via costameres that enable nonmyofascial force transmission), changes in the extracellular matrix with unloading may contribute to the nonuniform force loss (89–91).”

    From Nonuniform loss of muscle strength and atrophy during bed rest: a systematic review (2021) · cites this paper as [91]

    The Introduction (page unavailable) describes costameres as links between neighboring muscle fibers through extracellular-matrix receptors, and the Discussion (page unavailable) reports altered costamere regulation during bedrest. The paper does not establish that these changes contribute to nonuniform force loss; it reports changes in muscle size and adhesion-related proteins, not a pattern of force loss. (LLM, conf=0.83)

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Authors
Li, R., Narici, M. V., Erskine, R. M., Seynnes, O. R., Rittweger, J., Pišot, R., Šimunič, B., & Flück, M.
Affiliations
  • Manchester Metropolitan University (GB)
  • University of Primorska (SI)
Corresponding author
Flück, Martin
Venue
Journal of Anatomy
Publisher
Wiley
Published
2013-09-08
Volume
223
Issue
5
Pages
525-536
ISSN
  • 0021-8782 (ISSN-L)
  • 1469-7580
OpenAlex
W2167107375
Cited by
51
References
7
Citations by year
2026: 2 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 9 · 2021: 4 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 7 · 2016: 4 · 2015: 7 · 2014: 4
FWCI
2.24
Type
journal article
Language
en
Open access
Locations
  • Journal of Anatomy (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Repository of the University of Primorsk (University of Primorska) (publishedVersion, other-oa)
  • elib (German Aerospace Center) (acceptedVersion)
  • Liverpool John Moores University (acceptedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
  • NORA - Norwegian Open Research Archives (submittedVersion, cc-by-nc)
  • Padua Research Archive (University of Padova) (submittedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
Funders
  • European Commission (223576)
  • Medical Research Council (MR/K00414X/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Physiology › Spaceflight effects on biology
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords
beta1 integrin, focal adhesion kinase, muscle loading, muscle unloading, resistance training, bed rest, vastus lateralis, muscle thickness, p70S6K, myosin heavy chain, type I muscle fibers, FRNK, sarcolemma
MeSH terms
Adult, Analysis of Variance, Cytoskeletal Proteins, Humans, Male, Rest, Exercise, Muscle Fibers, Skeletal, Focal Adhesion Protein-Tyrosine Kinases, Quadriceps Muscle, Costameres, Young Adult

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