Literature DB >> 6715527

Chemical energy usage and myosin light chain phosphorylation in mammalian skeletal muscle.

R J Barsotti, T M Butler.   

Abstract

The purpose of this study was to ascertain whether phosphorylation of the regulatory light chain of myosin plays a role in modulating the rate of chemical energy usage in mammalian skeletal muscle. There was no change in the average rate of chemical energy usage with duration of isometric stimulation in the rat extensor digitorum longus (EDL), even though the degree of light chain phosphorylation increased from 5% at rest to above 60% after 7 s of stimulation. When the initial degree of phosphorylation was increased to 73% by prestimulation of the muscle, there was still no change in the chemical energy usage under isometric conditions. In contrast, under the conditions used, the mouse EDL showed changes in the average rate of energy usage that depended upon both tetanus duration and stimulation history. However, there was no consistent relationship between phosphorylation of the light chain and average rate of chemical energy usage. These results suggest that while there are factors which can change crossbridge cycling rate in mammalian skeletal muscle, phosphorylation of the regulatory light chain of myosin is neither necessary nor sufficient to cause such changes.

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Year:  1984        PMID: 6715527     DOI: 10.1007/bf00713151

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


  40 in total

1.  The estimation of creatine and of diacetyl.

Authors:  P Eggleton; S R Elsden; N Gough
Journal:  Biochem J       Date:  1943       Impact factor: 3.857

2.  The binding of actin to phosphorylated and dephosphorylated myosin.

Authors:  M Michnicka; K Kasman; I Kakol
Journal:  Biochim Biophys Acta       Date:  1982-06-24

3.  Myosin phosphorylation regulates the ATPase activity of permeable skeletal muscle fibers.

Authors:  R Cooke; K Franks; J T Stull
Journal:  FEBS Lett       Date:  1982-07-19       Impact factor: 4.124

4.  The phosphorylation-dephosphorylation process as a myosin-linked regulation of superprecipitation of fast skeletal muscle actomyosin.

Authors:  I Kakol; K Kasman; M Michnicka
Journal:  Biochim Biophys Acta       Date:  1982-06-24

5.  Regulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal muscles.

Authors:  J T Stull; D K Blumenthal; R Cooke
Journal:  Biochem Pharmacol       Date:  1980-10-01       Impact factor: 5.858

6.  Physiological effects accompanying the removal of myosin LC2 from skinned skeletal muscle fibers.

Authors:  R L Moss; G G Giulian; M L Greaser
Journal:  J Biol Chem       Date:  1982-08-10       Impact factor: 5.157

7.  Light chain phosphorylation alters the conformation of skeletal muscle myosin.

Authors:  C J Ritz-Gold; R Cooke; D K Blumenthal; J T Stull
Journal:  Biochem Biophys Res Commun       Date:  1980-03-13       Impact factor: 3.575

8.  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

9.  Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme.

Authors:  V Guerriero; D R Rowley; A R Means
Journal:  Cell       Date:  1981-12       Impact factor: 41.582

10.  Effects of previous activity on the energetics of activation in frog skeletal muscle.

Authors:  J A Rall
Journal:  J Gen Physiol       Date:  1980-06       Impact factor: 4.086

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  11 in total

1.  Myosin regulatory light chain phosphorylation inhibits shortening velocities of skeletal muscle fibers in the presence of the myosin inhibitor blebbistatin.

Authors:  Melanie Stewart; Kathy Franks-Skiba; Roger Cooke
Journal:  J Muscle Res Cell Motil       Date:  2009-01-06       Impact factor: 2.698

2.  Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction.

Authors:  H L Sweeney; J T Stull
Journal:  Proc Natl Acad Sci U S A       Date:  1990-01       Impact factor: 11.205

3.  Metabolic recovery of mouse extensor digitorum longus and soleus muscle.

Authors:  W J Leijendekker; G Elzinga
Journal:  Pflugers Arch       Date:  1990-04       Impact factor: 3.657

4.  The turnover of phosphate bound to myosin light chain-2 in perfused rat heart.

Authors:  B P Herring; P J England
Journal:  Biochem J       Date:  1986-11-15       Impact factor: 3.857

5.  The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate.

Authors:  R Cooke; K Franks; G B Luciani; E Pate
Journal:  J Physiol       Date:  1988-01       Impact factor: 5.182

6.  Comparison of the effects of 2,3-butanedione monoxime on force production, myosin light chain phosphorylation and chemical energy usage in intact and permeabilized smooth and skeletal muscles.

Authors:  M J Siegman; S U Mooers; T B Warren; D M Warshaw; M Ikebe; T M Butler
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

7.  Post-tetanic potentiation increases energy cost to a higher extent than work in rat fast skeletal muscle.

Authors:  F Abbate; J Van Der Velden; G J Stienen; A De Haan
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

Review 8.  Energy turnover for Ca2+ cycling in skeletal muscle.

Authors:  C J Barclay; R C Woledge; N A Curtin
Journal:  J Muscle Res Cell Motil       Date:  2007-09-20       Impact factor: 2.698

9.  The effects of ADP and phosphate on the contraction of muscle fibers.

Authors:  R Cooke; E Pate
Journal:  Biophys J       Date:  1985-11       Impact factor: 4.033

Review 10.  Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models.

Authors:  Rene Vandenboom; William Gittings; Ian C Smith; Robert W Grange; James T Stull
Journal:  J Muscle Res Cell Motil       Date:  2013-10-27       Impact factor: 2.698

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