ArticleMechanisms of ageing and development2004
Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats.
Article in Mechanisms of ageing and development, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Impact of aging and oxidative stress on specific components of excitation contraction coupling in regulating force generation.Science advances · 2022Article
- Age affects myosin relaxation states in skeletal muscle fibers of female but not male mice.PloS one · 2018Article
- Sod1 gene ablation in adult mice leads to physiological changes at the neuromuscular junction similar to changes that occur in old wild-type mice.Free radical biology & medicine · 2015Article
- Store-operated Ca2+ entry in muscle physiology and diseases.BMB reports · 2014Review
- Novel excitation-contraction coupling related genes reveal aspects of muscle weakness beyond atrophy-new hopes for treatment of musculoskeletal diseases.Frontiers in physiology · 2014Review
- Murine models of atrophy, cachexia, and sarcopenia in skeletal muscle.Biochimica et biophysica acta · 2013Review
- Article
- Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers.American journal of physiology. Cell physiology · 2008Article
- Skeletal muscle changes after hemiparetic stroke and potential beneficial effects of exercise intervention strategies.Journal of rehabilitation research and development · 2008Review
- Age-related decline in actomyosin structure and function.Experimental gerontology · 2007Review
- Protein nitration with aging in the rat semimembranosus and soleus muscles.The journals of gerontology. Series A, Biological sciences and medical sciences · 2006Article
- Age-related muscle dysfunction.Experimental gerontologyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We tested the hypothesis that Ca(2+)-activated myosin ATPase activity is lower in muscles of aged rats relative to muscles of young rats, independent of changes in myosin isoform expression. Myofibrils were prepared from permeabilized fibers of soleus, plantaris, and semimembranosus muscles of young (8-12 months) and aged (32-38 months) F344 x BN rats and assayed for resting myosin ATPase, Ca(2+)-activated myosin ATPase, and myosin heavy chain (MHC) and myosin light chain (MLC) isoform compositions. Resting myosin ATPases were not affected by age in any muscle (P > or = 0.42). Ca(2+)-activated myosin ATPases of soleus and plantaris myofibrils were not affected by age (P > or = 0.31) but were 16% lower in semimembranosus myofibrils from aged rats (0.448 +/- 0.019 micromol P(i)/min/mg) compared to young rats (0.533 +/- 0.031 micromol P(i)/min/mg; P = 0.03). Correspondingly, maximal unloaded shortening velocity of single semimembranosus fibers from aged rats was slow (4.6 +/- 0.2 fiber lengths/s) compared with fibers from young rats (5.8 +/- 0.3 fiber lengths/s; P < 0.01). No age-related changes in MHC or regulatory MLC isoforms were detected in any muscle (P > or = 0.08) but changes in the essential MLC occurred in plantaris and semimembranosus muscles. The data indicate that Ca(2+)-activated myosin ATPase activity is reduced with age in semimembranosus muscle, independent of age-related changes in MHC isoform expression, and is one mechanism contributing to age-related slowing of contraction in that muscle.
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