Literature DB >> 8785299

Tension relaxation after stretch in resting mammalian muscle fibers: stretch activation at physiological temperatures.

G Mutungi1, K W Ranatunga.   

Abstract

Tension responses to ramp stretches of 1-3% Lo (fiber length) in amplitude were examined in resting muscle fibers of the rat at temperatures ranging from 10 degrees C to 36 degrees C. Experiments were done using bundles of approximately 10 intact fibers isolated from the extensor digitorum longus (a fast muscle) and the soleus (a slow muscle). At low temperatures (below approximately 20 degrees C), the tension response consisted of an initial rise to a peak during the ramp followed by a complex tension decay to a plateau level; the tension decay occurred at approximately constant sarcomere length. The tension decay after a standard stretch at approximately 3-4.Lo/s contained a fast, an intermediate, and a (small amplitude) slow component, which at 10 degrees C (sarcomere length approximately 2.5 microns) were approximately 2000.s-1, approximately 150.s-1, and approximately 25.s-1 for fast fibers and approximately 2000.s-1, approximately 70.s-1 and approximately 8.s-1 for slow fibers, respectively. The fast component may represent the decay of interfilamentary viscous resistance, and the intermediate component may be due to viscoelasticity in the gap (titin, connectin) filament. The two- to threefold fast-slow muscle difference in the rate of passive tension relaxation (in the intermediate and the slow components) compares with previously reported differences in the speed of their active contractions; this suggests that "passive viscoelasticity" is appropriately matched to contraction speed in different muscle fiber types. At approximately 35 degrees C, the fast and intermediate components of tension relaxation were followed by a delayed tension rise at approximately 10.s-1 (fast fibers) and 2.5.s-1 (slow fibers); the delayed tension rise was accompanied by sarcomere shortening. BDM (5-10 mM) reduced the active twitch and tetanic tension responses and the delayed tension rise at 35 degrees C; the results indicate stretch sensitive activation in mammalian sarcomeres at physiological temperatures.

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Mesh:

Year:  1996        PMID: 8785299      PMCID: PMC1225069          DOI: 10.1016/S0006-3495(96)79702-3

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  26 in total

1.  ATPase activity and superprecipitation of skeletal muscle actomyosin of frog and rabbit: effect of temperature on calcium sensitivity.

Authors:  F Fuchs; D J Hartshorne; E M Barns
Journal:  Comp Biochem Physiol B       Date:  1975-06-15

2.  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

3.  The effect of temperature in the range 0-35 degrees C on the resting tension of frog's muscle.

Authors:  D K Hill
Journal:  J Physiol       Date:  1970-07       Impact factor: 5.182

4.  Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad.

Authors:  D G Stephenson; D A Williams
Journal:  J Physiol       Date:  1985-03       Impact factor: 5.182

5.  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

6.  The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  1984-06       Impact factor: 5.182

7.  Myofibrils bear most of the resting tension in frog skeletal muscle.

Authors:  A Magid; D J Law
Journal:  Science       Date:  1985-12-13       Impact factor: 47.728

8.  Temperature-dependence of shortening velocity and rate of isometric tension development in rat skeletal muscle.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  1982-08       Impact factor: 5.182

9.  Thermal inactivation of the calcium regulatory mechanism of human skeletal muscle actomyosin: a possible contributing factor in the rigidity of malignant hyperthermia.

Authors:  F Fuchs
Journal:  Anesthesiology       Date:  1975-05       Impact factor: 7.892

10.  Muscle cross-bridges bound to actin are disordered in the presence of 2,3-butanedione monoxime.

Authors:  L Zhao; N Naber; R Cooke
Journal:  Biophys J       Date:  1995-05       Impact factor: 4.033

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  13 in total

1.  Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils.

Authors:  A Minajeva; M Kulke; J M Fernandez; W A Linke
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

2.  The effects of ramp stretches on active contractions in intact mammalian fast and slow muscle fibres.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

3.  Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest.

Authors:  K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

4.  Do cross-bridges contribute to the tension during stretch of passive muscle? A response.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2000-04       Impact factor: 2.698

5.  Cardiac titin: molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium.

Authors:  Wolfgang A Linke; Julio M Fernandez
Journal:  J Muscle Res Cell Motil       Date:  2002       Impact factor: 2.698

6.  Dynamic behaviour of half-sarcomeres during and after stretch in activated rabbit psoas myofibrils: sarcomere asymmetry but no 'sarcomere popping'.

Authors:  I A Telley; R Stehle; K W Ranatunga; G Pfitzer; E Stüssi; J Denoth
Journal:  J Physiol       Date:  2006-03-09       Impact factor: 5.182

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

Authors:  K W Ranatunga; H Roots; G W Offer
Journal:  J Physiol       Date:  2009-11-30       Impact factor: 5.182

8.  Temperature-dependent changes in the viscoelasticity of intact resting mammalian (rat) fast- and slow-twitch muscle fibres.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Physiol       Date:  1998-04-01       Impact factor: 5.182

9.  The viscous, viscoelastic and elastic characteristics of resting fast and slow mammalian (rat) muscle fibres.

Authors:  G Mutungi; K W Ranatunga
Journal:  J Physiol       Date:  1996-11-01       Impact factor: 5.182

10.  The viscoelastic properties of passive eye muscle in primates. II: testing the quasi-linear theory.

Authors:  Christian Quaia; Howard S Ying; Lance M Optican
Journal:  PLoS One       Date:  2009-08-03       Impact factor: 3.240

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