ArticleThe Journal of physiology2004
Actomyosin energy turnover declines while force remains constant during isometric muscle contraction.
Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- The predominant stride-frequency for routine swimming in catsharks (Scyliorhinus canicula) generates high power at high efficiency in the red musculature.Journal of muscle research and cell motility · 2023Article
- A century of exercise physiology: key concepts in muscle energetics.European journal of applied physiology · 2023Review
- The legacy of A. V. Hill's Nobel Prize winning work on muscle energetics.The Journal of physiology · 2022Article
- Maximal strength training increases muscle force generating capacity and the anaerobic ATP synthesis flux without altering the cost of contraction in elderly.Experimental gerontology · 2018Article
- Roger C. Woledge 1938-2015.Journal of muscle research and cell motility · 2015Article
- Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula.The Journal of physiology · 2012Article
- Paying the piper: the cost of Ca2+ pumping during the mating call of toadfish.The Journal of physiology · 2011Article
- Effect of phosphate and temperature on force exerted by white muscle fibres from dogfish.Journal of muscle research and cell motility · 2010Article
- Time course and strain dependence of ADP release during contraction of permeabilized skeletal muscle fibers.Biophysical journal · 2009Article
- Effect of strain on actomyosin kinetics in isometric muscle fibers.Biophysical journal · 2006Article
- Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres.The Journal of physiology · 2005Article
- Smooth muscle myosin: regulation and properties.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy turnover was measured during isometric contractions of intact and Triton-permeabilized white fibres from dogfish (Scyliorhinus canicula) at 12 degrees C. Heat + work from actomyosin in intact fibres was determined from the dependence of heat + work output on filament overlap. Inorganic phosphate (Pi) release by permeabilized fibres was recorded using the fluorescent protein MDCC-PBP, N-(2-[1-maleimidyl]ethyl)-7-diethylamino-coumarin-3 carboxamide phosphate binding protein. The steady-state ADP release rate was measured using a linked enzyme assay. The rates decreased five-fold during contraction in both intact and permeabilized fibres. In intact fibres the rate of heat + work output by actomyosin decreased from 134 +/-s.e.m. 28 microW mg(-1) (n = 17) at 0.055 s to 42% of this value at 0.25 s, and to 20% at 3.5 s. The force remained constant between 0.25 and 3.5 s. Similarly in permeabilized fibres the Pi release rate decreased from 5.00 +/- 0.39 mmol l(-1) s(-1) at 0.055 s to 39% of this value at 0.25 s and to 19% at 0.5 s. The steady-state ADP release rate at 15 s was 21% of the Pi rate at 0.055 s. Using a single set of rate constants, the time courses of force, heat + work and Pi release were described by an actomyosin model that took account of the transition from the initial state (rest or rigor) to the contracting state, shortening and the consequent work against series elasticity, and reaction heats. The model suggests that increasing Pi concentration slows the cycle in intact fibres, and that changes in ATP and ADP slow the cycle in permeabilized fibres.
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