Force generation, but not myosin ATPase activity, declines with age in rat muscle fibers
Abstract
We tested the hypothesis that age-associated decline in muscle function is related to a change in myosin ATPase activity. Single, glycerinated semimembranosus fibers from young (8–12 mo) and aged (32–37 mo) Fischer 344 × Brown Norway male rats were analyzed simultaneously for force and myosin ATPase activity over a range of Ca 2+ concentrations. Maximal force generation was ∼20% lower in fibers from aged animals ( P = 0.02), but myosin ATPase activity was not different between fibers from young and aged rats: 686 ± 46 ( n = 30) and 697 ± 46 μM/s ( n = 33) ( P = 0.89). The apparent rate constant for the dissociation of strong-binding myosin from actin was calculated to be ∼30% greater in fibers from aged animals ( P = 0.03), indicating that the lower force produced by fibers from aged animals is due to a greater flux of myosin heads from the strong-binding state to the weak-binding state during contraction. This is in agreement with our previous electron paramagnetic resonance experiments that showed a reduced fraction of myosin heads in the strong-binding state during a maximal isometric contraction in fibers from older rats.
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- Authors
- Lowe, D. A., Thomas, D. D., & Thompson, L. V.
- Affiliations
- Department of Biochemistry, Molecular Biology, and Biophysics,
- University of Minnesota (US)
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2002-07-01
- Volume
- 283
- Issue
- 1
- Pages
- C187-C192
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2156047359
- Cited by
- 83
- References
- 37
- Citations by year
- 2023: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 6 · 2013: 1 · 2012: 4
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1r03ag018156-01)
- National Institute on Aging (F32AG005815, AG-00198, AG17768, AG18156, R01AG017768)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR 32961)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Keywords
- muscle aging, myosin ATPase activity, muscle force production, calcium sensitivity, isometric contraction
- MeSH terms
- Adenosine Triphosphate, Aging, Animals, Male, Myosins, Rats, Inbred BN, Rats, Inbred F344, Muscle Fibers, Skeletal, Myosin Heavy Chains, Protein Isoforms, Rats, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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