Literature DB >> 8910210

Salbutamol and chronic low-frequency stimulation of canine skeletal muscle.

P Hu1, K M Zhang, J J Feher, S W Wang, L D Wright, A S Wechsler, J A Spratt, F N Briggs.   

Abstract

1. The effect of simultaneous application of chronic muscle stimulation and salbutamol on the expression of mRNAs and proteins normally expressed by fast- or slow-twitch fibres was followed and the effects of changes in protein expression on mechanical performance were evaluated. Chronic low-frequency stimulation increased the myosin heavy chain (HC)-I level in the canine latissimus dorsi muscle and simultaneous administration of salbutamol partially blocked this change. Associated with the increase in HC-I level was a decrease in the velocity of shortening at zero load, VMAX. The change in VMAX was partially blocked by salbutamol. 2. Chronic low-frequency stimulation increased the levels of slow-twitch cardiac isoform sarco-/endoplasmic reticulum Ca(2+)-ATPase (SERCA2a) and phospholamban mRNA, and SERCA2a and phospholamban protein expression. These changes were associated with an increase in time-to-peak tension and a decrease in fusion frequency. Simultaneous administration of salbutamol blocked these changes in protein expression and muscle mechanics. Chronic stimulation of latissimus dorsi decreased the levels of the fast-twitch isoform of sarco-/endoplasmic reticulum Ca(2+)-ATPase (SERCA1a) and increased SERCA2a protein expression and decreased calcium uptake rate by muscle homogenates. These changes were blocked by salbutamol. 3. The loss of latissimus dorsi muscle weight by chronic stimulation was partially blocked by salbutamol.

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Year:  1996        PMID: 8910210      PMCID: PMC1160838          DOI: 10.1113/jphysiol.1996.sp021679

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


  29 in total

1.  Significance of the biopsy site of the latissimus dorsi muscle for fiber typing.

Authors:  O M Sola; S Herring; G Zhang; X Huang; N Hayashida; L C Haines; R Thomas; B A Kakulas; L R Sauvage
Journal:  J Heart Lung Transplant       Date:  1992 Sep-Oct       Impact factor: 10.247

2.  Phospholamban expressed in slow-twitch and chronically stimulated fast-twitch muscles minimally affects calcium affinity of sarcoplasmic reticulum Ca(2+)-ATPase.

Authors:  F N Briggs; K F Lee; A W Wechsler; L R Jones
Journal:  J Biol Chem       Date:  1992-12-25       Impact factor: 5.157

3.  Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle.

Authors:  A Termin; D Pette
Journal:  Eur J Biochem       Date:  1992-03-01

Review 4.  Altered gene expression in fast-twitch muscle induced by chronic low-frequency stimulation.

Authors:  D Pette; S Düsterhöft
Journal:  Am J Physiol       Date:  1992-03

5.  Stimulation of muscle growth by clenbuterol: lack of effect on muscle protein biosynthesis.

Authors:  P J Reeds; S M Hay; P M Dorwood; R M Palmer
Journal:  Br J Nutr       Date:  1986-07       Impact factor: 3.718

Review 6.  Muscle relaxation and sarcoplasmic reticulum function in different muscle types.

Authors:  L Dux
Journal:  Rev Physiol Biochem Pharmacol       Date:  1993       Impact factor: 5.545

7.  Stimulation-induced expression of slow muscle myosin in a fast muscle of the rat. Evidence of an unrestricted adaptive capacity.

Authors:  C N Mayne; T Mokrusch; J C Jarvis; S J Gilroy; S Salmons
Journal:  FEBS Lett       Date:  1993-08-02       Impact factor: 4.124

8.  Adaptation of energy metabolism of canine latissimus dorsi muscle in response to chronic electrical stimulation.

Authors:  J F Glatz; G J van der Vusse; M G Havenith; F H van der Veen; C M Lucas; O C Penn; H J Wellens
Journal:  Pflugers Arch       Date:  1992-01       Impact factor: 3.657

9.  Skeletal muscle as the potential power source for a cardiovascular pump: assessment in vivo.

Authors:  M A Acker; R L Hammond; J D Mannion; S Salmons; L W Stephenson
Journal:  Science       Date:  1987-04-17       Impact factor: 47.728

10.  Reciprocal changes in myosin isoform mRNAs of rabbit skeletal muscle in response to the initiation and cessation of chronic electrical stimulation.

Authors:  C Brownson; P Little; J C Jarvis; S Salmons
Journal:  Muscle Nerve       Date:  1992-06       Impact factor: 3.217

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  2 in total

1.  Myosin heavy chain profile of equine gluteus medius muscle following prolonged draught-exercise training and detraining.

Authors:  A L Serrano; J L Rivero
Journal:  J Muscle Res Cell Motil       Date:  2000-04       Impact factor: 2.698

2.  Analysis of myosin heavy chains at the protein level in horse skeletal muscle.

Authors:  J L Rivero; A L Serrano; E Barrey; J P Valette; M Jouglin
Journal:  J Muscle Res Cell Motil       Date:  1999-02       Impact factor: 2.698

  2 in total

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