ArticleBiophysical journal1995
Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation.Frontiers in physiology · 2022Pooled it
- Various challenges in understanding the thick filaments, within and outside skeletal and cardiac muscles.Biophysical reviews · 2025Article
- Article
- Skeletal muscle fiber hypercontraction induced by Bothrops asper myotoxic phospholipases APflugers Archiv : European journal of physiology · 2023Article
- Eliminating the First Inactive State and Stabilizing the Active State of the Cardiac Regulatory System Alters Behavior in Solution and in Ordered Systems.Biochemistry · 2020Article
- Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers.Frontiers in physiology · 2020Article
- Altered force generation and cell-to-cell contractile imbalance in hypertrophic cardiomyopathy.Pflugers Archiv : European journal of physiology · 2019Review
- Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating CaBiophysical journal · 2018Article
- Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Biochemistry · 2017Article
- Disease causing mutations of troponin alter regulated actin state distributions.Journal of muscle research and cell motility · 2012Review
- The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.Biophysical journal · 2012Article
- Acrylodan-labeled smooth muscle tropomyosin reports differences in the effects of troponin and caldesmon in the transition from the active state to the inactive state.Biochemistry · 2011Article
- Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.Biophysical journal · 2010Article
- Kinetics of regulated actin transitions measured by probes on tropomyosin.Biophysical journal · 2010Article
- Impaired organization and function of myofilaments in single muscle fibers from a mouse model of Pompe disease.Journal of applied physiology (Bethesda, Md. : 1985) · 2010Article
- Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.Biophysical journal · 2009Article
- Structural characterization of the binding of Myosin*ADP*Pi to actin in permeabilized rabbit psoas muscle.Biophysical journal · 2006Article
- Initiation of the power stroke in muscle: insights from the phosphate analog AlF4.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates.The Journal of physiology · 2005Article
- Mechanical properties of single myosin molecules probed with the photonic force microscope.Biophysical journal · 2005Article
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Authors and funding
4 authors.
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Abstract
Previously we showed that stiffness of relaxed fibers and active force generated in single skinned fibers of rabbit psoas muscle are inhibited in parallel by actin-binding fragments of caldesmon, an actin-associated protein of smooth muscle, under conditions in which a large fraction of cross-bridges is weakly attached to actin (ionic strength of 50 mM and temperature of 5 degrees C). These results suggested that weak cross-bridge attachment to actin is essential for force generation. The present study provides evidence that this is also true for physiological ionic strength (170 mM) at temperatures up to 30 degrees C, suggesting that weak cross-bridge binding to actin is generally required for force generation. In addition, we show that the inhibition of active force is not a result of changes in cross-bridge cycling kinetics but apparently results from selective inhibition of weak cross-bridge binding to actin. Together with our previous biochemical, mechanical, and structural studies, these findings support the proposal that weak cross-bridge attachment to actin is an essential intermediate on the path to force generation and are consistent with the concept that isometric force mainly results from an increase in strain of the attached cross-bridge as a result of a structural change associated with the transition from a weakly bound to a strongly bound actomyosin complex. This mechanism is different from the processes responsible for quick tension recovery that were proposed by Huxley and Simmons (Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.) to represent the elementary mechanism of force generation.
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