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Cited by 274Heat shock proteins researchMuscle Physiology and DisordersGenetics, Aging, and Longevity in Model Organisms

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age‐related muscle dysfunction

McArdle, Anne, H. Dillmann, Wolfgang, Mestril, Ruben, A. Faulkner, John, J. Jackson, Malcolm·2004·The FASEB Journal
DOI 10.1096/fj.03-0395fje
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Abstract

Ageing is associated with skeletal muscle atrophy, a deficit in force generation, an increased susceptibility to contraction‐induced injury, and a permanent force deficit following severe injury. Muscles of young mice adapt rapidly following exercise by an increase in the production of heat shock proteins (HSPs), whereas muscles of old mice show a severely diminished response. We hypothesized that overexpression of HSP70 in muscle throughout life would reduce age‐related changes in function. The maximum tetanic force of extensor digitorum longus (EDL) muscles of adult and old wild‐type (WT) and HSP70 overexpressor transgenic mice was determined. EDL muscles were subjected to damaging lengthening contractions and the ability to generate force was assessed for up to 28 days following the contractions. Overexpression of HSP70 in muscles of old transgenic mice prevented the specific force deficit observed in muscles of old WT mice. The complete recovery of muscles of old HSP70 transgenic mice by 14 days following the contraction protocol was in contrast to the 44% force deficit, which remained in muscles of old WT mice at 28 days following the protocol. These data indicate that a diminished production of HSP70 in muscles of old mammals has a major effect on age‐related functional deficits.

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Crossref · 10.1096/fj.03-0395fje

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34 of 34 references verified0 citation errors · 0 not checkable

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Research works printed but not linked: 1

  1. Hadley E. C., 1993, Physical frailty: a treatable cause of dependance in old age, J. Gerontol., 48, 1

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Metadata

Authors
McArdle, A., H. Dillmann, W., Mestril, R., A. Faulkner, J., & J. Jackson, M.
Affiliations
  • University of Liverpool (GB)
  • Department of Medicine University of California San Diego CA
  • Loyola University Chicago (US)
  • Institute of Gerontology University of Michigan Ann Arbor MI
  • Department of Medicine University of Liverpool Liverpool L69 3GA UK
ORCID
Venue
The FASEB Journal
Publisher
Wiley
Published
2003-12-19
Volume
18
Issue
2
Pages
1-12
ISSN
  • 0892-6638 (ISSN-L)
  • 1530-6860
DOI
10.1096/fj.03-0395fje
OpenAlex
W2148331882
Cited by
274
References
34
Citations by year
2026: 3 · 2025: 4 · 2024: 7 · 2023: 7 · 2022: 4 · 2021: 8 · 2020: 13 · 2019: 11 · 2018: 10 · 2017: 12 · 2016: 15 · 2015: 15 · 2014: 14 · 2013: 21 · 2012: 11
FWCI
4.71
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • The FASEB Journal (publishedVersion)
  • PubMed (publishedVersion)
  • Deep Blue (University of Michigan) (acceptedVersion)
Funders
  • Wellcome Trust (043364/Z/95/Z)
  • National Institutes of Health (R37HL 049434)
  • Joe Andruzzi Foundation
  • National Institute on Aging (Ag20591)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords
HSP70, heat shock proteins, skeletal muscle aging, muscle atrophy, muscle damage, contraction-induced injury, transgenic overexpression, extensor digitorum longus, tetanic force, muscle force recovery, exercise adaptation
MeSH terms
Aging, Animals, Female, Male, Mice, Transgenic, Muscle Contraction, Muscular Diseases, Muscle, Skeletal, HSP70 Heat-Shock Proteins, Transgenes, Mice, Rats

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