ArticleThe Journal of general physiology2010
Regulatory mechanism of length-dependent activation in skinned porcine ventricular muscle: role of thin filament cooperative activation in the Frank-Starling relation.
Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- Cross-bridge model for predicting muscle short-range stiffness during movement.PLoS computational biology · 2026Article
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- Titin force in muscle cells alters lattice order, thick and thin filament protein formation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Functional and structural differences between skinned and intact muscle preparations.The Journal of general physiology · 2022Review
- Effects of omecamtiv mecarbil on the contractile properties of skinned porcine left atrial and ventricular muscles.Frontiers in physiology · 2022Article
- Synchrony of sarcomeric movement regulates left ventricular pump function in the in vivo beating mouse heart.The Journal of general physiology · 2021Article
- Mechanisms of Frank-Starling law of the heart and stretch activation in striated muscles may have a common molecular origin.Journal of muscle research and cell motility · 2021Article
- Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC).Scientific reports · 2020Article
- Microscopic heat pulses activate cardiac thin filaments.The Journal of general physiology · 2019Article
- Role of the C-terminus mobile domain of cardiac troponin I in the regulation of thin filament activation in skinned papillary muscle strips.Archives of biochemistry and biophysics · 2018Article
- Functional significance of C-terminal mobile domain of cardiac troponin I.Archives of biochemistry and biophysics · 2017Article
- Titin-mediated thick filament activation, through a mechanosensing mechanism, introduces sarcomere-length dependencies in mathematical models of rat trabecula and whole ventricle.Scientific reports · 2017Article
- Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.Archives of biochemistry and biophysics · 2016Article
- Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm (20ΔRRM) Mice.Frontiers in physiology · 2016Article
- Spontaneous oscillatory contraction (SPOC) in cardiomyocytes.Biophysical reviews · 2015Article
- Cardiac thin filament regulation and the Frank-Starling mechanism.The journal of physiological sciences : JPS · 2014Review
- Interleukin-16 promotes cardiac fibrosis and myocardial stiffening in heart failure with preserved ejection fraction.PloS one · 2013Article
- Myocardial twitch duration and the dependence of oxygen consumption on pressure-volume area: experiments and modelling.The Journal of physiology · 2012Article
- Sarcomere imaging by quantum dots for the study of cardiac muscle physiology.Journal of biomedicine & biotechnology · 2012Review
- Sarcomere length-dependent Ca2+ activation in skinned rabbit psoas muscle fibers: coordinated regulation of thin filament cooperative activation and passive force.The journal of physiological sciences : JPS · 2011Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cardiac sarcomeres produce greater active force in response to stretch, forming the basis of the Frank-Starling mechanism of the heart. The purpose of this study was to provide the systematic understanding of length-dependent activation by investigating experimentally and mathematically how the thin filament "on-off" switching mechanism is involved in its regulation. Porcine left ventricular muscles were skinned, and force measurements were performed at short (1.9 µm) and long (2.3 µm) sarcomere lengths. We found that 3 mM MgADP increased Ca(2+) sensitivity of force and the rate of rise of active force, consistent with the increase in thin filament cooperative activation. MgADP attenuated length-dependent activation with and without thin filament reconstitution with the fast skeletal troponin complex (sTn). Conversely, 20 mM of inorganic phosphate (Pi) decreased Ca(2+) sensitivity of force and the rate of rise of active force, consistent with the decrease in thin filament cooperative activation. Pi enhanced length-dependent activation with and without sTn reconstitution. Linear regression analysis revealed that the magnitude of length-dependent activation was inversely correlated with the rate of rise of active force. These results were quantitatively simulated by a model that incorporates the Ca(2+)-dependent on-off switching of the thin filament state and interfilament lattice spacing modulation. Our model analysis revealed that the cooperativity of the thin filament on-off switching, but not the Ca(2+)-binding ability, determines the magnitude of the Frank-Starling effect. These findings demonstrate that the Frank-Starling relation is strongly influenced by thin filament cooperative activation.
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