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Updated: Mar 20, 2026

Measurement of Insulin- and Contraction-Stimulated Glucose Uptake in Isolated and Incubated Mature Skeletal Muscle from Mice
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Glucocorticoids Enhance Muscle Proteolysis through a Myostatin-Dependent Pathway at the Early Stage

Ruxia Wang1, Hongchao Jiao1, Jingpeng Zhao1

  • 1Department of Animal Science, Shandong Agricultural University, Shandong Key Lab for Animal Biotechnology and Disease Control, Taian, Shandong, 271018, P. R. China.

Plos One
|May 27, 2016
PubMed

Insights

Glucocorticoids like dexamethasone increase myostatin, a protein regulating muscle mass, and promote muscle protein breakdown. However, myostatin does not significantly suppress muscle protein synthesis during short-term dexamethasone treatment.

Area of Science:

  • Muscle physiology and molecular biology
  • Endocrinology and metabolism

Background:

  • Myostatin is a key regulator of skeletal muscle mass.
  • Glucocorticoids, such as dexamethasone (DEX), are known to induce muscle atrophy.
  • The precise role of myostatin in glucocorticoid-induced muscle protein turnover remains incompletely understood.

Purpose of the Study:

  • To investigate the involvement of myostatin in muscle protein metabolism during dexamethasone (DEX) treatment.
  • To elucidate the effects of DEX on protein synthesis, degradation pathways, and key signaling molecules.

Main Methods:

  • Measurement of protein synthesis rates.
  • Quantification of gene and protein expression for myostatin, atrogin-1, MuRF1, FoxO1/3a, mTOR, and p70S6K.
  • Assessment of signaling pathway activation through phosphorylation.
  • Intervention with follistatin to block myostatin activity.

Main Results:

  • DEX decreased protein synthesis rates and increased myostatin abundance.
  • DEX elevated phospho-FoxO1/3a and MuRF1 expression, but not atrogin-1.
  • DEX reduced phosphorylation of mTOR and p70S6K.
  • Follistatin counteracted DEX-induced increases in myostatin, phospho-FoxO1/3a, and MuRF1.

Conclusions:

  • The myostatin signaling pathway is implicated in glucocorticoid-induced muscle protein catabolism early in exposure.
  • Myostatin is not the primary mediator of glucocorticoid-induced suppression of muscle protein synthesis.

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