Cited by 91Muscle Physiology and DisordersExercise and Physiological ResponsesMuscle metabolism and nutrition

Dissociation of force production from MHC and actin contents in muscles injured by eccentric contractions

Ingalls, Christopher P., Warren, Gordon L., Armstrong, R. B.·1998·Journal of Muscle Research & Cell Motility

Abstract

The primary purpose of this study was to determine the relationship between myosin heavy chain (MHC) and actin contents and maximum isometric tetanic force (Po) in mouse extensor digitorum longus (EDL) muscles following eccentric contraction-induced injury. Po and protein contents were measured in injured (n = 80) and contralateral control (n = 80) EDL muscles at the following time points after in vivo injury: sham, 0, 0.25, 1, 3, 5, 14, and 28 days. Po was reduced by 37 +/- 2.3% to 49 +/- 3.8% (p < or = 0.05), while MHC and actin contents were unaltered from 0 to 3 days after injury. Whereas Po partially recovered between 3 and 5 days (from -49 +/- 3.8% to -35 +/- 3.6%), MHC and actin contents in the injured muscles declined by 19 +/- 4.9% and 20 +/- 5.3%, respectively, by 5 days compared with control muscles. Decrements in Po were similar to the reductions in MHC and actin contents at 14 (approximately 24%) and 28 (approximately 11%) days. Evaluation of myofibrillar and soluble protein fractions indicated significant reductions in the content of major proteins at 5 and 14 days. Immunoblots of heat shock protein 72 revealed elevations starting at 0.25 days, peaking during 1-3 days, and declining after 5 days. These findings indicate that decreased contractile protein content is not related to the initial decrease in Po. However, decreased MHC and actin contents could account for 58% of the Po reduction at 5 days, and for nearly all the decrements in Po from 14 to 28 days.

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Crossref · 10.1023/a:1005368831198

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References 43 · Cited by 91

Authors
Ingalls, C. P., Warren, G. L., & Armstrong, R. B.
Affiliations
  • Texas A&M University (US)
  • Texas A&M University System (US)
Venue
Journal of Muscle Research & Cell Motility
Published
1998-04
Volume
19
Issue
3
Pages
215-224
ISSN
  • 0142-4319 (ISSN-L)
  • 1573-2657
OpenAlex
W62577265
Cited by
91
References
43
Citations by year
2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 4
FWCI
0.93
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Muscle Research and Cell Motility (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ar042761-03)
  • National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-42761)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords
myosin heavy chain, actin, extensor digitorum longus, muscle force production, HSP72, myofibrillar proteins, muscle recovery, muscle damage
MeSH terms
Actins, Animals, Female, Heat-Shock Proteins, Isometric Contraction, Mice, Inbred ICR, Myofibrils, Time Factors, Muscle, Skeletal, Myelin P0 Protein, Myosin Heavy Chains, HSP72 Heat-Shock Proteins, Mice

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