Turnover of skeletal muscle contractile proteins in glucocorticoid myopathy

@article{Sne1994TurnoverOS,
  title={Turnover of skeletal muscle contractile proteins in glucocorticoid myopathy},
  author={T. P. S{\'e}{\'e}ne},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  year={1994},
  volume={50},
  pages={1-4}
}
  • T. Sééne
  • Published 1 July 1994
  • Biology
  • The Journal of Steroid Biochemistry and Molecular Biology
View on Elsevier
doi.org
50 Citations
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Background Citations
21
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50 Citations

Role of Myofibrillar Protein Catabolism in Development of Glucocorticoid Myopathy: Aging and Functional Activity Aspects

The aim of the present short review is to assess the role of myofibrillar protein catabolism in the development of glucocorticoid-caused myopathy from aging and physical activity aspects.

EXERCISE MYOPATHY: CHANGES IN MYOFIBRILS OF FAST-TWITCH MUSCLE FIBRES

Myofibrils in both types of fast-twitch myopathic muscle fibres are significantly thinner as the result of more intensive protein degradation, and Regeneration capacity according to the presence of satellite cells is higher in type IIA fibres than intype IIB fibres in myopathic Muscle.

The effect of glucocorticoids on the myosin heavy chain isoforms’ turnover in skeletal muscle

The effect of glucocorticoid myopathy, unloading and reloading on the skeletal muscle contractile apparatus and extracellular matrix

During three weeks of hindlimb suspension muscle mass decreased 36% (p Soleus (Sol) muscle, 17% ( p tendences to decrease in plantaris (Pla) (15%) and in extensor digitorum longus (EDL) (8%) muscles), and specific mRNA level for type I collagen decreased during three weeksOf unloading in Sol muscle by 28% and type III collagen level by 22%.

Influence of corticosteroids on myonuclear domain size in the rat diaphragm muscle.

MND size does not appear to be regulated during CoS-induced DIAm atrophy, and little, if any, loss of myonuclei was associated with Cos-induced atrophy of M HC2X or MHC2B DIAM fibers.

Review on aging, unloading and reloading: changes in skeletal muscle quantity and quality.

Relationship between extracellular matrix, contractile apparatus, muscle mass and strength in case of glucocorticoid myopathy

Fine architectonics and protein turnover rate in myofibrils of glucocorticoid caused myopathic rats

A positive correlation was found between the area of myofibrils where myofilaments disappeared and the my ofibrillar protein degradation rate.

Ageing and dexamethasone associated sarcopenia: Peculiarities of regeneration

Myofibrillar protein catabolism is rapidly suppressed following protein feeding.

The results suggest that the suppression of myofibrillar protein degradation by food intake was regulated by dietary proteins.

References

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Effect of glucocorticoids on contractile apparatus of rat skeletal muscle.

The catabolic effect of glucocorticoids on different types of skeletal muscle fibres and its dependence upon muscle activity and interaction with anabolic steroids.

Effect of glucocorticoids on the turnover rate of actin and myosin heavy and light chains on different types of skeletal muscle fibres.

Oxidative metabolism of skeletal muscle in steroid atrophy.

Mitochondrial defects do not represent the primary lesion in steroid atrophy, and additional hormonal actions are probably involved in the pathogenesis of steroids atrophy.

Oxidative respiration of skeletal muscle in experimental corticosteroid myopathy.

Resistance of individual muscles to corticosteroids appears to depend on multiple factors including the biochemical potential and relative proportion of the various fiber types in a specific muscle as well as the ability of mitochondria to oxidize fatty acids.

Protein turnover in skeletal muscle. II. Effects of denervation and cortisone on protein catabolism in skeletal muscle.

  • A. Goldberg
  • Biology
    The Journal of biological chemistry
  • 1969
In contrast to denervation atrophy, cortisone-atrophy affected the breakdown of myofibrillar and soluble proteins similarly and increased protein degradation and decreased protein synthesis.

Protein turnover in skeletal muscle. I. Protein catabolism during work-induced hypertrophy and growth induced with growth hormone.

  • A. Goldberg
  • Biology
    The Journal of biological chemistry
  • 1969
It is indicated that unlike work-induced hypertrophy, growth hormone increased protein synthesis in muscle without changing protein degradative rates.

Differences in response of proteolytic activity in cardiac, skeletal and diaphragm muscles to hormones and catabolic conditions

Contractile responses of rat fast‐twitch and slow‐twitch muscles to glucocorticoid treatment

The treatment‐induced enhancement of the specific twitch tension was more pronounced in the gastrocnemius muscles than in the soleus muscles, suggesting that the difference in response to steroid treatment may reflect structural and functional difference in fast‐ and slow‐muscle membrane systems.

Respiratory and skeletal muscle function in steroid-dependent bronchial asthma.

The results support the clinical impression that steroids, at the doses usually administered in chronic severe asthma, do not cause muscular weakness and find that malnutrition rather than corticosteroids is the most important contributory factor to type 2 muscle fiber atrophy in steroid-dependent asthma.