ArticleThe Journal of physiology2005
The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Paracrine HB-EGF signaling reduce enhanced contractile and energetic state of activated decidual fibroblasts by rebalancing SRF-MRTF-TCF transcriptional axis.Frontiers in cell and developmental biology · 2022Article
- Recent insights into the relative timing of myosin's powerstroke and release of phosphate.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Nonlinear cross-bridge elasticity and post-power-stroke events in fast skeletal muscle actomyosin.Biophysical journal · 2013Article
- The working stroke of the myosin II motor in muscle is not tightly coupled to release of orthophosphate from its active site.The Journal of physiology · 2013Article
- Orthovanadate and orthophosphate inhibit muscle force via two different pathways of the myosin ATPase cycle.Biophysical journal · 2011Article
- Emerging complex pathways of the actomyosin powerstroke.Trends in biochemical sciences · 2010Review
- Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.The Journal of physiology · 2010Review
- Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.The Journal of biological chemistry · 2010Article
- Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle.Biophysical journal · 2010Article
- A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle.Proceedings. Biological sciences · 2010Article
- Nebulin plays a direct role in promoting strong actin-myosin interactions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- Temperature change as a probe of muscle crossbridge kinetics: a review and discussion.Proceedings. Biological sciences · 2009Review
- Time course and strain dependence of ADP release during contraction of permeabilized skeletal muscle fibers.Biophysical journal · 2009Article
- Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas.Biophysical journal · 2008Article
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3 authors.
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Abstract
The time course of isometric force development following photolytic release of ATP in the presence of Ca(2+) was characterized in single skinned fibres from rabbit psoas muscle. Pre-photolysis force was minimized using apyrase to remove contaminating ATP and ADP. After the initial force rise induced by ATP release, a rapid shortening ramp terminated by a step stretch to the original length was imposed, and the time course of the subsequent force redevelopment was again characterized. Force development after ATP release was accurately described by a lag phase followed by one or two exponential components. At 20 degrees C, the lag was 5.6 +/- 0.4 ms (s.e.m., n = 11), and the force rise was well fitted by a single exponential with rate constant 71 +/- 4 s(-1). Force redevelopment after shortening-restretch began from about half the plateau force level, and its single-exponential rate constant was 68 +/- 3 s(-1), very similar to that following ATP release. When fibres were activated by the addition of Ca(2+) in ATP-containing solution, force developed more slowly, and the rate constant for force redevelopment following shortening-restretch reached a maximum value of 38 +/- 4 s(-1) (n = 6) after about 6 s of activation. This lower value may be associated with progressive sarcomere disorder at elevated temperature. Force development following ATP release was much slower at 5 degrees C than at 20 degrees C. The rate constant of a single-exponential fit to the force rise was 4.3 +/- 0.4 s(-1) (n = 22), and this was again similar to that after shortening-restretch in the same activation at this temperature, 3.8 +/- 0.2 s(-1). We conclude that force development after ATP release and shortening-restretch are controlled by the same steps in the actin-myosin ATPase cycle. The present results and much previous work on mechanical-chemical coupling in muscle can be explained by a kinetic scheme in which force is generated by a rapid conformational change bracketed by two biochemical steps with similar rate constants -- ATP hydrolysis and the release of inorganic phosphate -- both of which combine to control the rate of force development.
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