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

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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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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: McArdle, Anne
Mestril, Ruben
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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Overexpression of HSP70 in mouse skeletal muscle protects against muscle damage and age‐related muscle dysfunction

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