Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization

Robert J. Isfort, Feng Wang, Kenneth D. Greis, Yiping Sun, Thomas W. Keough, Sue C. Bodine, N. Leigh Anderson

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

A proteomic analysis was performed comparing normal slow twitch type fiber rat soleus muscle and normal fast twitch type fiber tibialis anterior muscle to immobilized soleus and tibialis anterior muscles at 0.5, 1, 2, 4, 6, 8 and 10 days post immobilization. Muscle mass measurements demonstrate mass changes throughout the period of immobilization. Proteomic analysis of normal and atrophied soleus muscle demonstrated statistically significant changes in the relative levels of 17 proteins. Proteomic analysis of normal and atrophied tibialis anterior muscle demonstrated statistically significant changes in the relative levels of 45 proteins. Protein identification using mass spectrometry was attempted for all differentially regulated proteins from both soleus and tibialis anterior muscles. Four differentially regulated soleus proteins and six differentially regulated tibialis anterior proteins were identified. The identified proteins can be grouped according to function as metabolic proteins, chaperone proteins, and contractile apparatus proteins. Together these data demonstrate that coordinated temporally regulated changes in the proteome occur during immobilization-induced atrophy in both slow twitch and fast twitch fiber type skeletal muscle.

Original languageEnglish (US)
Pages (from-to)323-332
Number of pages10
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume769
Issue number2
DOIs
StatePublished - Apr 5 2002
Externally publishedYes

Keywords

  • Muscles
  • Proteins
  • Proteomic analysis

ASJC Scopus subject areas

  • Biochemistry

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