Literature DB >> 9490847

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

G Mutungi1, K W Ranatunga.   

Abstract

1. The tension and sarcomere length responses induced by ramp stretches (at amplitudes of 1-3 % fibre length (Lo) and speeds of 0.01-12 Lo s-1) were examined at different temperatures (range, 10-35 degrees C) in resting intact muscle fibre bundles isolated from the soleus (a slow-twitch muscle) and extensor digitorum longus (a fast-twitch muscle) of the rat. Some observations are also presented on the effects of chemical skinning on passive viscoelasticity at 10 degrees C. 2. As previously reported, the tension response to a ramp stretch, in different preparations and under various conditions, could be resolved into a viscous (P1), a viscoelastic (P2) and an elastic (P3) component and showed characteristic differences between slow and fast muscle fibres. 3. Chemical skinning of the muscle fibres led to a decrease in the amplitude of all three tension components. However, the fast-slow fibre differences remained after skinning. For example, the viscosity coefficient derived from P1 tension data decreased from 0.84 +/- 0.06 before skinning to 0.44 +/- 0.06 kN s m-2 after skinning in fast fibres; the corresponding values in slow fibres were 2.1 +/- 0.08 and 0.87 +/- 0.09 kN s m-2, respectively. 4. Increasing the experimental temperature from 10 to 35 degrees C led to a decrease in all the tension components in both fast and slow muscle fibre bundles. The decrease of P1 (viscous) tension was such that the viscosity coefficient calculated using P1 data was reduced from 0.84 +/- 0.1 to 0.43 +/- 0.05 kN s m-2 in fast fibres and from 2.0 +/- 0.1 to 1.0 +/- 0.1 kN s m-2 in slow fibres (Q10 of approximately 1.3 in both). 5. In both fast and slow muscle fibre preparations, the plateau tension of the viscoelastic component (P2) decreased by 60-80 % as the temperature was increased from 10 to 35 degrees C giving P2 tension a Q10 of approximately 1.4 in slow fibres and approximately 1.7 in the fast fibres. Additionally, the relaxation time of the viscoelasticity decreased from 11.9 +/- 1 ms (fast) and 43.1 +/- 1 ms (slow) at 10 degrees C to 3 +/- 0.5 ms (fast) at 25 C degrees and 8. 7 +/- 0.6 ms (slow) at 35 degrees C (Q10 of approximately 2.0 in slow and approximately 2.5 in fast fibres). 6. The fast-slow fibre differences in passive viscoelasticity remained at the high physiological temperatures. The physiological significance of such fibre-type differences and their possible underlying mechanisms are discussed.

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Year:  1998        PMID: 9490847      PMCID: PMC2230871          DOI: 10.1111/j.1469-7793.1998.253br.x

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


  26 in total

1.  Pressure sensitivity of active tension in glycerinated rabbit psoas muscle fibres: effects of ADP and phosphate.

Authors:  N S Fortune; M A Geeves; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  1989-04       Impact factor: 2.698

2.  X-ray diffraction studies on skinned single fibres of frog skeletal muscle.

Authors:  I Matsubara; G F Elliott
Journal:  J Mol Biol       Date:  1972-12-30       Impact factor: 5.469

3.  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

4.  Elasticity and unfolding of single molecules of the giant muscle protein titin.

Authors:  L Tskhovrebova; J Trinick; J A Sleep; R M Simmons
Journal:  Nature       Date:  1997-05-15       Impact factor: 49.962

5.  Lateral filamentary spacing in chemically skinned murine muscles during contraction.

Authors:  I Matsubara; Y Umazume; N Yagi
Journal:  J Physiol       Date:  1985-03       Impact factor: 5.182

6.  Characterization of the myosin adenosine triphosphate (M.ATP) crossbridge in rabbit and frog skeletal muscle fibers.

Authors:  M Schoenberg
Journal:  Biophys J       Date:  1988-07       Impact factor: 4.033

7.  Critical dependence of calcium-activated force on width in highly compressed skinned fibers of the frog.

Authors:  J Gulati; A Babu
Journal:  Biophys J       Date:  1985-11       Impact factor: 4.033

8.  The stiffness of frog skinned muscle fibres at altered lateral filament spacing.

Authors:  Y E Goldman; R M Simmons
Journal:  J Physiol       Date:  1986-09       Impact factor: 5.182

9.  Effects of 2,3-butanedione monoxime on the contractile activation properties of fast- and slow-twitch rat muscle fibres.

Authors:  M W Fryer; I R Neering; D G Stephenson
Journal:  J Physiol       Date:  1988-12       Impact factor: 5.182

10.  Effect of osmotic compression on the force-velocity properties of glycerinated rabbit skeletal muscle cells.

Authors:  L E Ford; K Nakagawa; J Desper; C Y Seow
Journal:  J Gen Physiol       Date:  1991-01       Impact factor: 4.086

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  24 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.  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

3.  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

4.  Crossbridge and non-crossbridge contributions to tension in lengthening rat muscle: force-induced reversal of the power stroke.

Authors:  G J Pinniger; K W Ranatunga; G W Offer
Journal:  J Physiol       Date:  2006-04-20       Impact factor: 5.182

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.  Mechanism of force enhancement during and after lengthening of active muscle: a temperature dependence study.

Authors:  H Roots; G J Pinniger; G W Offer; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2012-06-16       Impact factor: 2.698

Review 7.  Do cross-bridges contribute to the tension during stretch of passive muscle?

Authors:  U Proske; D L Morgan
Journal:  J Muscle Res Cell Motil       Date:  1999-08       Impact factor: 2.698

8.  Acute Effects of Dynamic Stretching on Mechanical Properties Result From both Muscle-Tendon Stretching and Muscle Warm-Up.

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Journal:  J Sports Sci Med       Date:  2019-06-01       Impact factor: 2.988

9.  Stretching Combined with Repetitive Small Length Changes of the Plantar Flexors Enhances Their Passive Extensibility while Not Compromising Strength.

Authors:  Naoki Ikeda; Takayuki Inami; Yasuo Kawakami
Journal:  J Sports Sci Med       Date:  2019-02-11       Impact factor: 2.988

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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