Table 1.

Major trends in protein changes during skeletal muscle aging as revealed by mass spectrometry-based proteomics^*.

Proteomic approach	Muscle tissue	Fast-to-slow transitions	Glycolytic-to-oxidative shift	References
Proteomic profiling of urea-soluble proteome	Human vastus lateralis	Slow MLC2 ↑; fast MLC2 ↓; cardiac α-actin ↑; fast TnT ↓; TM-α ↓	ATP synthase ↑; ACO ↑; GAPDH ↓; ENO ↓; TPI ↓	Gelfi et al. (2006)
Proteomic profiling of urea-soluble proteome	Rat gastrocnemius	MHC IIB ↓; MHC I ↑; fast MLC2 ↓; slow MLC2 ↑; cardiac α-actin ↑; TM-α ↓	ATP synthase ↑; ICDH ↑; ACO ↑; SDH ↑; Cyt-c RED ↑; GAPDH ↓; ENO ↓; ALD ↓; TPI ↓; PGM ↓; PFK ↓; PK ↓; ALB ↑; MYO ↑; FABP3 ↑	Capitanio et al. (2009), O’Connell and Ohlendieck (2009), Lombardi et al. (2009), Doran et al. (2008), Piec et al. (2005)
Sub proteomic screening of contractile fraction	Rat gastrocnemius	Slow MLC2 ↑; various fast MLC ↓; fast TnT ↓; MHC I ↑; MHC II ↓	ATP synthase ↑; ENO ↓	Gannon et al. (2009)
Analysis of protein nitration, phosphorylation and glycosylation	Various rat muscles	Differential effects on PTMs; slow MLC2-P ↑	Differential effects on PTMs; various glycolytic enzymes ↓	Kanski et al. (2005), Gannon et al. (2008), O’Connell et al. (2008)

*The table lists markers of the contractile apparatus (MHC, myosin heavy chain; MLC, myosin light chain; TM, tropomyosin; TnT, troponin subunit T) and key enzymes of glycolysis (GAPDH, glyceraldehyde-3-phosphate dehydrogenase; ENO, enolase; ALD, aldolase; TPI, triosephosphate isomerase; PGM, phosphoglucomutase; PFK, phosphofructokinase; PK, pyruvate kinase) and oxidative metabolism (ICDH, isocitrate dehydrogenase; ACO, aconitase; SDH, succinate dehydrogenase; Cyt-c RED, cytochrome-c reductase; ALB, albumin; MYO, myoglobin; FABP, fatty acid binding-protein).