SMHS1 is involved in oxidative/glycolytic-energy metabolism balance of muscle fibers

Biochem Biophys Res Commun. 2005 Jan 28;326(4):788-93. doi: 10.1016/j.bbrc.2004.11.111.

Abstract

With the aim of finding important mediators of muscle atrophy, we cloned SMHS1, a novel gene that was found to be upregulated in rat soleus muscle atrophied by restriction of activity. The SMHS1 amino acid sequence shares 65% similarity with RTP801-which is a cellular stress response protein regulated by HIF-1-but SMHS1 expression was demonstrated to be independent of HIF-1. SMHS1 was found to be mainly expressed in skeletal muscle, and comparisons of its expression in atrophied versus hypertrophied muscles and in oxidative versus glycolytic muscles suggested that SMHS1 contributes to the muscle energy metabolism phenotypes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Energy Metabolism*
  • Female
  • Glycolysis / physiology*
  • Homeostasis
  • Mice
  • Molecular Sequence Data
  • Muscle Fibers, Skeletal / classification*
  • Muscle Fibers, Skeletal / metabolism*
  • Muscle, Skeletal / metabolism*
  • Muscle, Skeletal / pathology
  • Muscular Atrophy / metabolism*
  • Muscular Atrophy / pathology
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism*
  • Organ Specificity
  • Oxidation-Reduction
  • Rats
  • Rats, Sprague-Dawley
  • Sequence Homology, Amino Acid
  • Tissue Distribution
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism*

Substances

  • Ddit4l2 protein, rat
  • Nuclear Proteins
  • Transcription Factors