ArticleThe Journal of physiology2010
The mechanism of the resistance to stretch of isometrically contracting single muscle fibres.
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 29 papers.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Evidence for multi-scale power amplification in skeletal muscle.The Journal of experimental biology · 2023Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- The effects of inorganic phosphate on muscle force development and energetics: challenges in modelling related to experimental uncertainties.Journal of muscle research and cell motility · 2021Article
- Evidence for Muscle Cell-Based Mechanisms of Enhanced Performance in Stretch-Shortening Cycle in Skeletal Muscle.Frontiers in physiology · 2020Review
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin.Biophysical journal · 2018Article
- The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentration.The Journal of physiology · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task.Frontiers in physiology · 2018Article
- Sarcomere Stiffness during Stretching and Shortening of Rigor Skeletal Myofibrils.Biophysical journal · 2017Article
- Reinterpretation of the Tension Response of Muscle to Stretches and Releases.Biophysical journal · 2016Article
- Force and number of myosin motors during muscle shortening and the coupling with the release of the ATP hydrolysis products.The Journal of physiology · 2015Article
- The cross-bridge of skeletal muscle is not synchronized either by length or force step.International journal of molecular sciences · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.Journal of muscle research and cell motility · 2014Article
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
- Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.The Journal of physiology · 2014Article
- The non-linear elasticity of the muscle sarcomere and the compliance of myosin motors.The Journal of physiology · 2014Article
- Why muscle is an efficient shock absorber.PloS one · 2014Article
- Stiffness, working stroke, and force of single-myosin molecules in skeletal muscle: elucidation of these mechanical properties via nonlinear elasticity evaluation.Cellular and molecular life sciences : CMLS · 2013Review
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7 authors at 1 institution in 1 country.
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Abstract
Rapid attachment to actin of the detached motor domain of myosin dimers with one motor domain already attached has been hypothesized to explain the stretch-induced changes in X-ray interference and stiffness of active muscle. Here, using half-sarcomere mechanics in single frog muscle fibres (2.15 microm sarcomere length and 4 degrees C), we show that: (1) an increase in stiffness of the half-sarcomere under stretch is specific to isometric contraction and does not occur in rigor, indicating that the mechanism of stiffness increase is an increase in the number of attached motors; (2) 2 ms after 100 micros stretches (amplitude 2-8 nm per half-sarcomere) imposed during an isometric tetanus, the stiffness of the array of myosin motors in each half-sarcomere (e(m)) increases above the isometric value (e(m0)); (3) e(m) has a sigmoidal dependence on the distortion of the motor domains (Delta z) attached in isometric contraction, with a maximum approximately 2 e(m0) for a distortion of approximately 6 nm; e(m) is influenced by detachment of motors at z > 6 nm; (4) at the end of the 100 micros stretch the relation between e(m)/e(m0) and Delta z lies slightly but not significantly above that at 2 ms. These results support the idea that stretch-induced sliding of the actin filament distorts the actin-attached motor domain of the myosin dimers away from the centre of the sarcomere, providing the steric conditions for rapid attachment of the second motor domain. The rate of new motor attachment must be as high as 7.5 x 10(4) s(1) and explains the rapid and efficient increase of the resistance of active muscle to stretch.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.