ArticleBiophysical journal2006
Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 116 citations in OpenAlex.
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Impact of stretch on sarcomere length variability in isolated fully relaxed rat cardiac myocytes.Pflugers Archiv : European journal of physiology · 2023Article
- Impact of stretch on sarcomere length variability in isolated fully relaxed rat cardiac myocytes.Research square · 2023Article
- Characterizing residual and passive force enhancements in cardiac myofibrils.Biophysical journal · 2023Article
- Cardiomyocyte sarcomere length variability: Membrane fluorescence versus second harmonic generation myosin imaging.The Journal of general physiology · 2023Article
- Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023Review
- What Can We Learn from Single Sarcomere and Myofibril Preparations?Frontiers in physiology · 2022Review
- Contractile State Dependent Sarcomere Length Variability in Isolated Guinea-Pig Cardiomyocytes.Frontiers in physiology · 2022Article
- Sarcomere Length Nonuniformity and Force Regulation in Myofibrils and Sarcomeres.Biophysical journal · 2020Review
- Force enhancement after stretch of isolated myofibrils is increased by sarcomere length non-uniformities.Scientific reports · 2020Article
- Sarcomere length non-uniformities dictate force production along the descending limb of the force-length relation.Proceedings. Biological sciences · 2020Article
- Extraction of Thick Filaments in Individual Sarcomeres Affects Force Production by Single Myofibrils.Biophysical journal · 2020Article
- Measurement of Skeletal Muscle Fiber Contractility with High-Speed Traction Microscopy.Biophysical journal · 2020Article
- Sarcomere Lengths Become More Uniform Over Time in Intact Muscle-Tendon Unit During Isometric Contractions.Frontiers in physiology · 2020Article
- Effect of myofibril passive elastic properties on the mechanical communication between motor proteins on adjacent sarcomeres.Scientific reports · 2019Article
- The effects of fatigue and oxidation on contractile function of intact muscle fibers and myofibrils isolated from the mouse diaphragm.Scientific reports · 2019Article
- Single sarcomere contraction dynamics in a whole muscle.Scientific reports · 2018Article
- Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?American journal of physiology. Cell physiology · 2018Article
- Microfluidic perfusion shows intersarcomere dynamics within single skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Kinetic coupling of phosphate release, force generation and rate-limiting steps in the cross-bridge cycle.Journal of muscle research and cell motility · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study the dynamics of individual half-sarcomeres in striated muscle contraction, myofibrils prepared from rabbit psoas muscle and left ventricles of guinea pig were immunostained with two conjugated antibody complexes consisting of a primary antibody against either alpha-actinin or myomesin and a secondary fluorescently labeled Fab-fragment. We simultaneously measured force kinetics and determined the positions of the Z-line and M-band signals by fluorescence video microscopy and sophisticated computer vision (tracking) algorithms. Upon calcium activation, sarcomeres and half-sarcomeres shortened nonuniformly. Shortening occurred first rapidly and exponentially during the force rise and then slowly during the force plateau. In psoas myofibrils, time-resolved displacements of the A-band in sarcomeres were observed, i.e., the two halves of individual sarcomeres behaved nonuniformly. Nonuniformity in length changes between the two halves of sarcomeres was comparable to that between two adjacent half-sarcomeres of neighboring sarcomeres. Sequential lengthening of half-sarcomeres was observed in cardiac myofibrils during the rapid phase of force relaxation. The independent dynamics of the halves in a sarcomere reveals the half-sarcomere as the functional unit rather than the structural unit, the sarcomere. The technique will facilitate the study of filament sliding within individual half-sarcomeres and the mechanics of intersegmental chemomechanical coupling in multisegmental striated muscles.
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