Literature DB >> 3795099

Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation.

R L Moss.   

Abstract

The effect of Ca2+ upon maximum shortening velocity (Vmax) has been investigated in skinned single fibres from rabbit psoas muscles. Vmax was obtained at 15 degrees C by measuring the amounts of time (delta t) required to take up various amounts of slack (delta l) imposed at one end of the fibre. During maximal activation with Ca2+, plots of delta l vs. delta t were well fitted by a single straight line. Calculation of Vmax from the slopes of the fitted lines yielded a Vmax of 4.44 +/- 0.15 (S.E. of mean) muscle lengths per second (m.l./s). However, at lower levels of Ca2+ activation, plots of delta l vs. delta t were biphasic, containing an initial phase of steady high-velocity shortening and a subsequent phase of steady low-velocity shortening. The transition between these two phases occurred following active shortening equivalent to 60-80 nm/half-sarcomere. Vmax during the high-velocity phase was relatively insensitive to Ca2+ concentration between pCas (i.e. -log [Ca2+]) of 4.5 and 6.0; however, Vmax fell to 3.58 +/- 0.40 m.l./s at pCa 6.1 and further to 1.02 +/- 0.30 m.l./s at pCa 6.2. Vmax during the low-velocity phase decreased as Ca2+ was lowered within the entire range of pCas studied to a minimum value of 0.35 +/- 0.09 m.l./s at pCa 6.2. The degree of thin-filament activation at a particular pCa was varied by partial extraction of troponin-C, which resulted in a permanent though reversible inactivation of parts of the thin filaments. Partial extraction of troponin-C altered the plots of delta l vs. delta t obtained at pCa 4.5 to a biphasic form. In addition, Vmax during the high- and low-velocity phases of shortening was reduced at each pCa greater than 4.5. Vmax values obtained in control fibres at low Ca2+ concentrations and extracted fibres were in good agreement when generated isometric tensions were equivalent. This was the case for both the high- and low-velocity phases of shortening. Fibres were also activated in the absence of Ca2+ by partial removal of total troponin complexes. These fibres developed steady tensions less than 30% of maximum and underwent biphasic shortening, indicating that this phenomenon cannot be the result of shortening-induced dissociation of Ca2+ from troponin-C.(ABSTRACT TRUNCATED AT 400 WORDS)

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Year:  1986        PMID: 3795099      PMCID: PMC1182845          DOI: 10.1113/jphysiol.1986.sp016199

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


  28 in total

1.  Muscle structure and theories of contraction.

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

2.  Thick-filament-linked calcium regulation in vertebrate striated muscle.

Authors:  W Lehman
Journal:  Nature       Date:  1978-07-06       Impact factor: 49.962

3.  Mechanical deactivation induced by active shortening in isolated muscle fibres of the frog.

Authors:  K A Edman
Journal:  J Physiol       Date:  1975-03       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

5.  Sarcomere length-tension relations of frog skinned muscle fibres during calcium activation at short lengths.

Authors:  R L Moss
Journal:  J Physiol       Date:  1979-07       Impact factor: 5.182

6.  Cooperation within actin filament in vertebrate skeletal muscle.

Authors:  R D Bremel; A Weber
Journal:  Nat New Biol       Date:  1972-07-26

7.  The effect of calcium on the force-velocity relation of briefly glycerinated frog muscle fibres.

Authors:  F J Julian
Journal:  J Physiol       Date:  1971-10       Impact factor: 5.182

8.  The relation between calcium and contraction kinetics in skinned muscle fibres.

Authors:  R J Podolsky; L E Teichholz
Journal:  J Physiol       Date:  1970-11       Impact factor: 5.182

9.  The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres.

Authors:  K A Edman
Journal:  J Physiol       Date:  1979-06       Impact factor: 5.182

10.  Ionic strength and the contraction kinetics of skinned muscle fibers.

Authors:  M D Thames; L E Teichholz; R J Podolsky
Journal:  J Gen Physiol       Date:  1974-04       Impact factor: 4.086

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  52 in total

1.  Ca2+ dependence of loaded shortening in rat skinned cardiac myocytes and skeletal muscle fibres.

Authors:  K S McDonald
Journal:  J Physiol       Date:  2000-05-15       Impact factor: 5.182

2.  Strong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca(2+).

Authors:  D R Swartz; R L Moss
Journal:  J Physiol       Date:  2001-06-01       Impact factor: 5.182

3.  A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation.

Authors:  Julien Ochala; Hiroyuki Iwamoto; Lars Larsson; Naoto Yagi
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-10       Impact factor: 11.205

4.  Unloaded shortening after a quick release of a contracting, single fibre from crayfish slow muscle.

Authors:  T Tameyasu
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

5.  Cardiac myosin binding protein C and its phosphorylation regulate multiple steps in the cross-bridge cycle of muscle contraction.

Authors:  Arthur T Coulton; Julian E Stelzer
Journal:  Biochemistry       Date:  2012-04-06       Impact factor: 3.162

Review 6.  Changes in the force-velocity relationship of fatigued muscle: implications for power production and possible causes.

Authors:  David A Jones
Journal:  J Physiol       Date:  2010-06-14       Impact factor: 5.182

7.  Maximum velocity of shortening of three fibre types from horse soleus muscle: implications for scaling with body size.

Authors:  L C Rome; A A Sosnicki; D O Goble
Journal:  J Physiol       Date:  1990-12       Impact factor: 5.182

8.  Unloaded shortening of skinned mammalian skeletal muscle fibres: effects of the experimental approach and passive force.

Authors:  S Galler; K Hilber
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

9.  Thin filament activation and unloaded shortening velocity of rabbit skinned muscle fibres.

Authors:  Carl A Morris; Larry S Tobacman; Earl Homsher
Journal:  J Physiol       Date:  2003-05-02       Impact factor: 5.182

10.  Mechanisms underlying reduced maximum shortening velocity during fatigue of intact, single fibres of mouse muscle.

Authors:  H Westerblad; A J Dahlstedt; J Lännergren
Journal:  J Physiol       Date:  1998-07-01       Impact factor: 5.182

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