Literature DB >> 3897445

Myosin isoenzymes as molecular markers for muscle physiology.

R G Whalen.   

Abstract

Myosin is a major component of skeletal muscle and it plays a central role in determining the physiological performance of adult tissue. Developing muscles contain myosin molecules which are different from the adult forms, and these isoenzymes have been found to be characteristic markers of the diverse physiological and pathological states of muscle tissue. The differences between these isoenzymes may be demonstrated by protein chemical, immunochemical and genetic evidence. The study of the sequential transitions between isoenzymes represents a means for characterizing the dynamic nature of muscle development, and neuronal and hormonal influences have been identified which contribute to the regulation of these transitions. The perspectives for future work include genetic studies, elucidation of the pathways relating extracellular signals to changes in gene expression, and the possibility that studies of myosin isoenzymes might further understanding of muscle pathology.

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Year:  1985        PMID: 3897445     DOI: 10.1242/jeb.115.1.43

Source DB:  PubMed          Journal:  J Exp Biol        ISSN: 0022-0949            Impact factor:   3.312


  25 in total

1.  Expression of an alpha cardiac-like myosin heavy chain in muscle spindle fibres.

Authors:  F Pedrosa; T Soukup; L E Thornell
Journal:  Histochemistry       Date:  1990

2.  Expression of myosin heavy chain isoforms in myogenic clones obtained from developing quail breast muscle.

Authors:  Keith E Latham; Irwin R Konigsberg
Journal:  Rouxs Arch Dev Biol       Date:  1988-01

3.  Changes in muscle fibre type, muscle mass and IGF-I gene expression in rabbit skeletal muscle subjected to stretch.

Authors:  H Yang; M Alnaqeeb; H Simpson; G Goldspink
Journal:  J Anat       Date:  1997-05       Impact factor: 2.610

4.  Influence of exercise contraction mode and protein supplementation on human skeletal muscle satellite cell content and muscle fiber growth.

Authors:  Jean Farup; Stine Klejs Rahbek; Simon Riis; Mikkel Holm Vendelbo; Frank de Paoli; Kristian Vissing
Journal:  J Appl Physiol (1985)       Date:  2014-08-07

5.  Differentiation of fast and slow muscles in the rat after neonatal denervation: a physiological study.

Authors:  M H Elmubarak; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  1988-06       Impact factor: 2.698

6.  The non-selective innervation of muscle fibres and mixed composition of motor units in a muscle of neonatal rat.

Authors:  S P Jones; R M Ridge; A Rowlerson
Journal:  J Physiol       Date:  1987-05       Impact factor: 5.182

7.  Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres.

Authors:  H Baumann; M Jäggi; F Soland; H Howald; M C Schaub
Journal:  Pflugers Arch       Date:  1987-08       Impact factor: 3.657

8.  Impaired skeletal muscle repair after ischemia-reperfusion injury in mice.

Authors:  A Vignaud; C Hourde; F Medja; O Agbulut; G Butler-Browne; A Ferry
Journal:  J Biomed Biotechnol       Date:  2010-05-09

9.  Myosin isoform expression in rat rhabdomyosarcoma induced by Moloney murine sarcoma virus.

Authors:  G Azzarello; S Sartore; L Saggin; L Gorza; E D'Andrea; L Chieco-Bianchi; S Schiaffino
Journal:  J Cancer Res Clin Oncol       Date:  1987       Impact factor: 4.553

10.  Denervated chicken breast muscle displays discoordinate regulation and differential patterns of expression of alpha f and beta tropomyosin genes.

Authors:  M P Gupta; R J Wiesner; V Mouly; R Zak; M Lemonnier
Journal:  J Muscle Res Cell Motil       Date:  1993-08       Impact factor: 2.698

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