Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization.
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.
Isfort
Robert J
RJ
Research Division, Health Care Research Center, Procter & Gamble Pharmaceuticals, Mason, OH 45040-9317, USA. isfortrj@pg.com
Wang
Feng
F
Greis
Kenneth D
KD
Sun
Yiping
Y
Keough
Thomas W
TW
Bodine
Sue C
SC
Anderson
N Leigh
NL
D000595:Amino Acid Sequence; D000818:Animals; D019417:Hindlimb Suspension; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000032:analysis* / Q000737:chemistry; D018482:Muscle, Skeletal / Q000737:chemistry*; D020543:Proteome; D051381:Rats
D009124:Muscle Proteins; D020543:Proteome