Literature DB >> 19948657

Temperature jump induced force generation in rabbit muscle fibres gets faster with shortening and shows a biphasic dependence on velocity.

K W Ranatunga1, H Roots, G W Offer.   

Abstract

We examined the tension responses to ramp shortening and rapid temperature jump (<0.2 ms, 3-4 degrees C T-jump) in maximally Ca(2+)-activated rabbit psoas muscle fibres at 8-9 degrees C (the fibre length (L(0)) was approximately 1.5 mm and sarcomere length 2.5 microm). The aim was to investigate the strain sensitivity of crossbridge force generation in muscle. The T-jump induced tension rise was examined during steady shortening over a wide range of velocities (V) approaching the V(max) (V range approximately 0.01 to approximately 1.5 L(0) s(1)). In the isometric state, a T-jump induced a biphasic tension rise consisting of a fast (approximately 50 s(1), phase 2b) and a slow (approximately 10 s(1), phase 3) component, but if treated as monophasic the rate was approximately 20 s(1). During steady shortening the T-jump tension rise was monophasic; the rate of tension rise increased linearly with shortening velocity, and near V(max) it was approximately 200 s(1), approximately 10x faster than in the isometric state. Relative to the tension reached after the T-jump, the amplitude increased with shortening velocity, and near V(max) it was 4x larger than in the isometric state. Thus, the temperature sensitivity of muscle force is markedly increased with velocity during steady shortening, as found in steady state experiments. The rate of tension decline during ramp shortening also increased markedly with increase of velocity. The absolute amplitude of T-jump tension rise was larger than that in the isometric state at the low velocities (<0.5 L(0) s(1)) but decreased to below that of the isometric state at the higher velocities. Such a biphasic velocity dependence of the absolute amplitude of T-jump tension rise implies interplay between, at least, two processes that have opposing effects on the tension output as the shortening velocity is increased, probably enhancement of crossbridge force generation and faster (post-stroke) crossbridge detachment by negative strain. Overall, our results show that T-jump force generation is strain sensitive and becomes considerably faster when exposed to negative strain. Thus the crossbridge force generation step in muscle is both temperature sensitive (endothermic) and strain sensitive.

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Year:  2009        PMID: 19948657      PMCID: PMC2825612          DOI: 10.1113/jphysiol.2009.179200

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  42 in total

1.  Tension responses to joule temperature jump in skinned rabbit muscle fibres.

Authors:  S Y Bershitsky; A K Tsaturyan
Journal:  J Physiol       Date:  1992-02       Impact factor: 5.182

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Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

3.  Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres.

Authors:  Y E Goldman; J A McCray; K W Ranatunga
Journal:  J Physiol       Date:  1987-11       Impact factor: 5.182

4.  Force generation by muscle fibers in rigor: a laser temperature-jump study.

Authors:  J S Davis; W F Harrington
Journal:  Proc Natl Acad Sci U S A       Date:  1987-02       Impact factor: 11.205

5.  Double-hyperbolic force-velocity relation in frog muscle fibres.

Authors:  K A Edman
Journal:  J Physiol       Date:  1988-10       Impact factor: 5.182

6.  Control of sarcomere length in skinned muscle fibres of Rana temporaria during mechanical transients.

Authors:  Y E Goldman; R M Simmons
Journal:  J Physiol       Date:  1984-05       Impact factor: 5.182

7.  Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle.

Authors:  M Kawai; H R Halvorson
Journal:  Biophys J       Date:  1991-02       Impact factor: 4.033

8.  Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres.

Authors:  J A Dantzig; Y E Goldman; N C Millar; J Lacktis; E Homsher
Journal:  J Physiol       Date:  1992       Impact factor: 5.182

9.  Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres.

Authors:  H Higuchi; Y E Goldman
Journal:  Nature       Date:  1991-07-25       Impact factor: 49.962

10.  Tension responses to rapid pressure release in glycerinated rabbit muscle fibers.

Authors:  N S Fortune; M A Geeves; K W Ranatunga
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-15       Impact factor: 11.205

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  5 in total

Review 1.  Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  2010-10-01       Impact factor: 5.182

2.  The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.

Authors:  Gerald Offer; K W Ranatunga
Journal:  J Physiol       Date:  2015-02-11       Impact factor: 5.182

Review 3.  Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.

Authors:  Gerald Offer; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2010-12-04       Impact factor: 2.698

4.  ATP binding and cross-bridge detachment steps during full Ca²⁺ activation: comparison of myofibril and muscle fibre mechanics by sinusoidal analysis.

Authors:  Bogdan Iorga; Li Wang; Robert Stehle; Gabriele Pfitzer; Masataka Kawai
Journal:  J Physiol       Date:  2012-05-14       Impact factor: 5.182

Review 5.  Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.

Authors:  K W Ranatunga
Journal:  Int J Mol Sci       Date:  2018-05-22       Impact factor: 5.923

  5 in total

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