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Multiple muscle wasting-related transcription factors are acetylated in dexamethasone-treated muscle cells

Wei Chamberlain1, Patricia Gonnella, Nima Alamdari

  • 1Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|February 2, 2012
PubMed

Insights

Acetylation of muscle-wasting transcription factors increases during muscle atrophy. The histone acetyltransferase p300 regulates this acetylation, impacting muscle loss and suggesting new therapeutic targets.

Area of Science:

  • Muscle physiology
  • Molecular biology
  • Biochemistry

Background:

  • Histone acetyltransferase p300 activity is elevated in muscle wasting.
  • Posttranslational modifications, like acetylation, affect transcription factor function.
  • The acetylation status of muscle mass regulators in atrophy is unknown.

Purpose of the Study:

  • To investigate the acetylation of key transcription factors in muscle wasting.
  • To determine the role of p300 in transcription factor acetylation and muscle atrophy.

Main Methods:

  • Dexamethasone treatment of L6 myotubes to model muscle wasting.
  • Quantification of acetylated transcription factors (C/EBPβ, C/EBPδ, FOXO1, FOXO3a, NF-kB/p65).
  • p300 siRNA to assess p300's role in acetylation and atrophy.

Main Results:

  • Dexamethasone increased acetylation of C/EBPβ, C/EBPδ, FOXO1, FOXO3a, and p65.
  • p300 downregulation reduced transcription factor acetylation.
  • Reduced p300 also decreased dexamethasone-induced myotube atrophy and MuRF1 expression.

Conclusions:

  • Muscle wasting involves acetylation of transcription factors like C/EBP, FOXO, and NF-kB.
  • p300-mediated acetylation plays a role in glucocorticoid-induced muscle atrophy.
  • Targeting acetylation pathways may offer strategies to combat muscle wasting.

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