ArticleAmerican journal of physiology. Cell physiology2020
The load dependence and the force-velocity relation in intact myosin filaments from skeletal and smooth muscles.
Article in American journal of physiology. Cell physiology, 2020. 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, 18 citations in OpenAlex.
- MYO18B promotes lysosomal exocytosis by facilitating focal adhesion maturation.The Journal of cell biology · 2025Article
- Mechanistic insights into effects of the cardiac myosin activator omecamtiv mecarbil from mechanokinetic modelling.Frontiers in physiology · 2025Article
- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
- Cooperative motility, force generation and mechanosensing in a foraging non-photosynthetic diatom.Open biology · 2023Article
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Insights into Muscle Contraction Derived from the Effects of Small-Molecular Actomyosin-Modulating Compounds.International journal of molecular sciences · 2022Article
- 3D printed protein-based robotic structures actuated by molecular motor assemblies.Nature materials · 2022Article
- Critical Evaluation of Current Hypotheses for the Pathogenesis of Hypertrophic Cardiomyopathy.International journal of molecular sciences · 2022Review
- Effects of Knee Joint Angle and Contraction Intensity on the Triceps Surae Stiffness.Frontiers in bioengineering and biotechnology · 2022Article
- Molecular Events of the Crossbridge Cycle Reflected in the Force-Velocity Relationship of Activated Muscle.Frontiers in physiology · 2022Review
- Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021Review
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study we evaluated the load dependence of force produced by isolated muscle myosin filaments interacting with fluorescently labeled actin filaments, using for the first time whole native myosin filaments. We used a newly developed approach that allowed the use of physiological levels of ATP. Single filaments composed of either skeletal or smooth muscle myosin and single filaments of actin were attached between pairs of nano-fabricated cantilevers of known stiffness. The filaments were brought into contact to produce force, which caused sliding of the actin filaments over the myosin filaments. We applied load to the system by either pushing or pulling the filaments during interactions and observed that increasing the load increased the force produced by myosin and decreasing the load decreased the force. We also performed additional experiments in which we clamped the filaments at predetermined levels of force, which caused the filaments to slide to adjust the different loads, allowing us to measure the velocity of length changes to construct a force-velocity relation. Force values were in the range observed previously with myosin filaments and molecules. The force-velocity curves for skeletal and smooth muscle myosins resembled the relations observed for muscle fibers. The technique can be used to investigate many issues of interest and debate in the field of muscle biophysics.
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