ArticleThe Journal of physiology2010
Force-generating capacity of human myosin isoforms extracted from single muscle fibre segments.
Article in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Effects of age on human skeletal muscle: a systematic review and meta-analysis of myosin heavy chain isoform protein expression, fiber size, and distribution.American journal of physiology. Cell physiology · 2024Pooled it
- Effects of ageing on single muscle fibre contractile function following short-term immobilisation.The Journal of physiology · 2011Trial
- Fiber-type traps: revisiting common misconceptions about skeletal muscle fiber types with application to motor control, biomechanics, physiology, and biology.Journal of applied physiology (Bethesda, Md. : 1985) · 2024Review
- Quantum dot-based thermometry uncovers decreased myosin efficiency in an experimental intensive care unit model.Frontiers in physiology · 2024Article
- Fiber-Type Shifting in Sarcopenia of Old Age: Proteomic Profiling of the Contractile Apparatus of Skeletal Muscles.International journal of molecular sciences · 2023Review
- A neuromuscular perspective of sarcopenia pathogenesis: deciphering the signaling pathways involved.GeroScience · 2022Article
- Age-related differences in calf muscle recruitment strategies in the time-frequency domain during walking as a function of task demand.Journal of applied physiology (Bethesda, Md. : 1985) · 2021Article
- Sarcopenia versus cancer cachexia: the muscle wasting continuum in healthy and diseased aging.Biogerontology · 2021Review
- A Modular Mathematical Model of Exercise-Induced Changes in Metabolism, Signaling, and Gene Expression in Human Skeletal Muscle.International journal of molecular sciences · 2021Article
- Sex differences in muscle fatigue following isokinetic muscle contractions.Scientific reports · 2021Article
- Contractile Properties of MHC I and II Fibers From Highly Trained Arm and Leg Muscles of Cross-Country Skiers.Frontiers in physiology · 2021Article
- Chaperone co-inducer BGP-15 mitigates early contractile dysfunction of the soleus muscle in a rat ICU model.Acta physiologica (Oxford, England) · 2020Article
- Sarcopenia: Aging-Related Loss of Muscle Mass and Function.Physiological reviews · 2019 · on this mapReview
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Aberrant post-translational modifications compromise human myosin motor function in old age.Aging cell · 2015Article
- Molecular determinants of force production in human skeletal muscle fibers: effects of myosin isoform expression and cross-sectional area.American journal of physiology. Cell physiology · 2015Article
- Hormone replacement therapy improves contractile function and myonuclear organization of single muscle fibres from postmenopausal monozygotic female twin pairs.The Journal of physiology · 2013Article
- Molecular mechanisms underlying skeletal muscle weakness in human cancer: reduced myosin-actin cross-bridge formation and kinetics.Journal of applied physiology (Bethesda, Md. : 1985) · 2013Article
- Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms.The Journal of physiology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle, motor unit and muscle fibre type-specific differences in force-generating capacity have been investigated for many years, but there is still no consensus regarding specific differences between slow- and fast-twitch muscles, motor units or muscle fibres. This is probably related to a number of different confounding factors disguising the function of the molecular motor protein myosin. We have therefore studied the force-generating capacity of specific myosin isoforms or combination of isoforms extracted from short single human muscle fibre segments in a modified single fibre myosin in vitro motility assay, in which an internal load (actin-binding protein) was added in different concentrations to evaluate the force-generating capacity. The force indices were the x-axis intercept and the slope of the relationship between the fraction of moving filaments and the α-actinin concentration. The force-generating capacity of the β/slow myosin isoform (type I) was weaker (P < 0.05) than the fast myosin isoform (type II), but the force-generating capacity of the different human fast myosin isoforms types IIa and IIx or a combination of both (IIax) were indistinguishable. A single fibre in vitro motility assay for both speed and force of specific myosin isoforms is described and used to measure the difference in force-generating capacity between fast and slow human myosin isoforms. The assay is proposed as a useful tool for clinical studies on the effects on muscle function of specific mutations or post-translational modifications of myosin.
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