Literature DB >> 8506362

On the regeneration of the actin-myosin power stroke in contracting muscle.

Y D Chen1, B Brenner.   

Abstract

The transient behavior of muscle in double-or multiple-step length perturbations [Lombardi, V., Piazzesi, G. & Linari, M. (1992) Nature (London) 355, 638-641] is simulated with a "conventional" cross-bridge model, which has been reported [Eisenberg, E., Hill, T. L. & Chen, Y. (1980) Biophys. J. 29, 195-227] to account for many mechanical, as well as biochemical, muscle data. The quick recovery of tension after double- or multiple-length perturbations was calculated for the model without any readjustment of its original parameters. The regeneration rate of the quick tension recovery of the model is fast and comparable to that measured experimentally by Lombardi et al. For multiple-step "stair-case"-type length releases, the tension response reaches a steady-state shape after three or four steps, and the average ATP turnover is much slower than the regeneration of the quick tension recovery. Our simulation shows that the experimental findings of Lombardi et al. can easily be reproduced by this simple conventional cross-bridge model, in which the completion of one work-producing power stroke is coupled to the hydrolysis of one ATP molecule. Thus, to account for the data of Lombardi et al., there is no need to assume that cross-bridges can execute multiple power strokes per ATPase cycle, although cross-bridges may well be able to do so. The mechanism that underlies the fast regeneration of the quick tension recovery in the conventional model used here is discussed.

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Year:  1993        PMID: 8506362      PMCID: PMC46672          DOI: 10.1073/pnas.90.11.5148

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  15 in total

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Authors:  A F HUXLEY
Journal:  Prog Biophys Biophys Chem       Date:  1957

2.  Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle.

Authors:  B Brenner
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-01       Impact factor: 11.205

3.  The contractile response during steady lengthening of stimulated frog muscle fibres.

Authors:  V Lombardi; G Piazzesi
Journal:  J Physiol       Date:  1990-12       Impact factor: 5.182

4.  Tension responses to sudden length change in stimulated frog muscle fibres near slack length.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

Review 5.  Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution.

Authors:  B Brenner
Journal:  Annu Rev Physiol       Date:  1987       Impact factor: 19.318

6.  The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution.

Authors:  B Brenner
Journal:  Basic Res Cardiol       Date:  1986       Impact factor: 17.165

Review 7.  Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I.

Authors:  T L Hill
Journal:  Prog Biophys Mol Biol       Date:  1974       Impact factor: 3.667

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Authors:  A F Huxley; R M Simmons
Journal:  Nature       Date:  1971-10-22       Impact factor: 49.962

9.  Initiation of active contraction by photogeneration of adenosine-5'-triphosphate in rabbit psoas muscle fibres.

Authors:  Y E Goldman; M G Hibberd; D R Trentham
Journal:  J Physiol       Date:  1984-09       Impact factor: 5.182

10.  Cross-bridge model of muscle contraction. Quantitative analysis.

Authors:  E Eisenberg; T L Hill; Y Chen
Journal:  Biophys J       Date:  1980-02       Impact factor: 4.033

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  18 in total

Review 1.  Cooperativity of myosin molecules through strain-dependent chemistry.

Authors:  T Duke
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

2.  Instabilities in the transient response of muscle.

Authors:  Andrej Vilfan; Thomas Duke
Journal:  Biophys J       Date:  2003-08       Impact factor: 4.033

Review 3.  Recent X-ray diffraction studies of muscle contraction and their implications.

Authors:  Hugh E Huxley
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2004-12-29       Impact factor: 6.237

Review 4.  The stroke size of myosins: a reevaluation.

Authors:  Bernhard Brenner
Journal:  J Muscle Res Cell Motil       Date:  2006-02-10       Impact factor: 2.698

5.  Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.

Authors:  A Radocaj; T Weiss; W I Helsby; B Brenner; T Kraft
Journal:  Biophys J       Date:  2009-02-18       Impact factor: 4.033

6.  A cross-bridge cycle with two tension-generating steps simulates skeletal muscle mechanics.

Authors:  Gerald Offer; K W Ranatunga
Journal:  Biophys J       Date:  2013-08-20       Impact factor: 4.033

7.  Nonlinear cross-bridge elasticity and post-power-stroke events in fast skeletal muscle actomyosin.

Authors:  Malin Persson; Elina Bengtsson; Lasse ten Siethoff; Alf Månsson
Journal:  Biophys J       Date:  2013-10-15       Impact factor: 4.033

8.  Reversal of the myosin power stroke induced by fast stretching of intact skeletal muscle fibers.

Authors:  Barbara Colombini; Marta Nocella; Giulia Benelli; Giovanni Cecchi; Peter J Griffiths; M Angela Bagni
Journal:  Biophys J       Date:  2009-12-02       Impact factor: 4.033

9.  Stretch activation and nonlinear elasticity of muscle cross-bridges.

Authors:  N Thomas; R A Thornhill
Journal:  Biophys J       Date:  1996-06       Impact factor: 4.033

10.  Mechanokinetics of rapid tension recovery in muscle: the Myosin working stroke is followed by a slower release of phosphate.

Authors:  David A Smith; John Sleep
Journal:  Biophys J       Date:  2004-07       Impact factor: 4.033

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