ArticleAmerican journal of physiology. Cell physiology2008
Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers.
Article in American journal of physiology. Cell physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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61 citing papers in PubMed, 108 citations in OpenAlex.
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- From amino-acid to disease: the effects of oxidation on actin-myosin interactions in muscle.Journal of muscle research and cell motility · 2023Review
- Molecular and Phenotypic Changes in FLExDUX4 Mice.Journal of personalized medicine · 2023Article
- Endogenous and Exogenous Antioxidants in Skeletal Muscle Fatigue Development during Exercise.Antioxidants (Basel, Switzerland) · 2023Review
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- Protein Quality Control at the Sarcomere: Titin Protection and Turnover and Implications for Disease Development.Frontiers in physiology · 2022Review
- Superoxide-mediated oxidative stress accelerates skeletal muscle atrophy by synchronous activation of proteolytic systems.GeroScience · 2020Article
- Actin-binding compounds, previously discovered by FRET-based high-throughput screening, differentially affect skeletal and cardiac muscle.The Journal of biological chemistry · 2020Article
- Membrane Repair Deficit in Facioscapulohumeral Muscular Dystrophy.International journal of molecular sciences · 2020Article
- Effects of high-intensity intermittent exercise on the contractile properties of human type I and type II skeletal muscle fibers.Journal of applied physiology (Bethesda, Md. : 1985) · 2020Article
- Diaphragm weakness and proteomics (global and redox) modifications in heart failure with reduced ejection fraction in rats.Journal of molecular and cellular cardiology · 2020Article
- The calmodulin redox sensor controls myogenesis.PloS one · 2020Article
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Redox responses are preserved across muscle fibres with differential susceptibility to aging.Journal of proteomics · 2018Article
- Carbonylation of atrial myosin prolongs its interaction with actin.European biophysics journal : EBJ · 2018Article
- A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Science advances · 2017Article
- Diaphragm abnormalities in heart failure and aging: mechanisms and integration of cardiovascular and respiratory pathophysiology.Heart failure reviews · 2017Review
- Physiological and pathophysiological reactive oxygen species as probed by EPR spectroscopy: the underutilized research window on muscle ageing.The Journal of physiology · 2016Review
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 4 institutions in 2 countries.
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Abstract
To understand the molecular mechanism of oxidation-induced inhibition of muscle contractility, we have studied the effects of hydrogen peroxide on permeabilized rabbit psoas muscle fibers, focusing on changes in myosin purified from these fibers. Oxidation by 5 mM peroxide decreased fiber contractility (isometric force and shortening velocity) without significant changes in the enzymatic activity of myofibrils and isolated myosin. The inhibitory effects were reversed by treating fibers with dithiothreitol. Oxidation by 50 mM peroxide had a more pronounced and irreversible inhibitory effect on fiber contractility and also affected enzymatic activity of myofibrils, myosin, and actomyosin. Peroxide treatment also affected regulation of contractility, resulting in fiber activation in the absence of calcium. Electron paramagnetic resonance of spin-labeled myosin in muscle fibers showed that oxidation increased the fraction of myosin heads in the strong-binding structural state under relaxing conditions (low calcium) but had no effect under activating conditions (high calcium). This change in the distribution of structural states of myosin provides a plausible explanation for the observed changes in both contractile and regulatory functions. Mass spectroscopy analysis showed that 50 mM but not 5 mM peroxide induced oxidative modifications in both isoforms of the essential light chains and in the heavy chain of myosin subfragment 1 by targeting multiple methionine residues. We conclude that 1) inhibition of muscle fiber contractility via oxidation of myosin occurs at high but not low concentrations of peroxide and 2) the inhibitory effects of oxidation suggest a critical and previously unknown role of methionines in myosin function.
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