Literature DB >> 6215428

The effect of calcium on the maximum velocity of shortening in skinned skeletal muscle fibres of the rabbit.

R L Moss.   

Abstract

The relationship between maximum shortening velocity (Vmax) and free calcium concentration has been studied in skinned single fibres from rabbit psoas and soleus muscles. At both 10 and 15 degrees C, Vmax measured in the psoas fibres was found to decrease by 40% when the pCa(-log[Ca2+]) was increased from 5.49 (maximally activating) to 6.21. Further decreases in Vmax were observed when the pCa was increased to 6.32. Vmax measured in soleus fibres at 15 degrees C also decreased when the Ca2+ concentration was lowered, though the magnitude of this effect was slightly less than in the psoas fibres. Thus, a distinct effect of Ca2+ upon Vmax has been shown to occur in mammalian skeletal muscle. The occurrence of this effect in both fast and slow muscle types may indicate that the underlying mechanism in the two cases is similar.

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Year:  1982        PMID: 6215428     DOI: 10.1007/bf00713039

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  25 in total

1.  Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle.

Authors:  A G Weeds; R Hall; N C Spurway
Journal:  FEBS Lett       Date:  1975-01-01       Impact factor: 4.124

2.  Phosphorylation-dephosphorylation of the 18,000-dalton light chain of myosin during the contraction-relaxation cycle of frog muscle.

Authors:  K Bárány; M Bárány; J M Gillis; M J Kushmerick
Journal:  J Biol Chem       Date:  1979-05-10       Impact factor: 5.157

3.  Force-velocity characteristics for calcium-activated mammalian slow-twitch and fast-twitch skeletal fibers from the guinea pig.

Authors:  J Gulati
Journal:  Proc Natl Acad Sci U S A       Date:  1976-12       Impact factor: 11.205

4.  Evidence for structural changes in vertebrate thick filaments induced by calcium.

Authors:  K Morimoto; W F Harrington
Journal:  J Mol Biol       Date:  1974-09-25       Impact factor: 5.469

5.  The relation between intrinsic speed of shortening and duration of the active state of muscle.

Authors:  R Close
Journal:  J Physiol       Date:  1965-10       Impact factor: 5.182

6.  The effect on tension of non-uniform distribution of length changes applied to frog muscle fibres.

Authors:  F J Julian; D L Morgan
Journal:  J Physiol       Date:  1979-08       Impact factor: 5.182

7.  Myosin light chain phosphorylation and phosphorylase A activity in rat extensor digitorum longus muscle.

Authors:  D R Manning; J T Stull
Journal:  Biochem Biophys Res Commun       Date:  1979-09-12       Impact factor: 3.575

8.  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

9.  The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPase.

Authors:  S M Pemrick
Journal:  J Biol Chem       Date:  1980-09-25       Impact factor: 5.157

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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  28 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.  Measurement of nucleotide exchange rate constants in single rabbit soleus myofibrils during shortening and lengthening using a fluorescent ATP analog.

Authors:  I Shirakawa; S Chaen; C R Bagshaw; H Sugi
Journal:  Biophys J       Date:  2000-02       Impact factor: 4.033

3.  Contribution of damped passive recoil to the measured shortening velocity of skinned rabbit and sheep muscle fibres.

Authors:  C Y Seow; L E Ford
Journal:  J Muscle Res Cell Motil       Date:  1992-06       Impact factor: 2.698

4.  Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.

Authors:  Richard K Brizendine; Diego B Alcala; Michael S Carter; Brian D Haldeman; Kevin C Facemyer; Josh E Baker; Christine R Cremo
Journal:  Proc Natl Acad Sci U S A       Date:  2015-08-20       Impact factor: 11.205

5.  Force-velocity and power-load curves in rat skinned cardiac myocytes.

Authors:  K S McDonald; M R Wolff; R L Moss
Journal:  J Physiol       Date:  1998-09-01       Impact factor: 5.182

6.  Mechanical characterization of skeletal muscle myofibrils.

Authors:  A L Friedman; Y E Goldman
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

7.  Thin filament regulation of shortening velocity in rat skinned skeletal muscle: effects of osmotic compression.

Authors:  J M Metzger; R L Moss
Journal:  J Physiol       Date:  1988-04       Impact factor: 5.182

8.  The role of calcium ions in the activation of rabbit psoas muscle.

Authors:  A J Farrow; G H Rossmanith; J Unsworth
Journal:  J Muscle Res Cell Motil       Date:  1988-06       Impact factor: 2.698

9.  The necessity of using two parameters to describe isotonic shortening velocity of muscle tissues: the effect of various interventions upon initial shortening velocity (vi) and curvature (b).

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

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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