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Expressions of the gastrocnemius and soleus muscle proteins were measured by western blot. The gastrocnemius and soleus muscles were homogenized in 500 μl of homogenization buffer (5 mM Tris-HCl pH 7.4, 0.15 M NaCl, 1% NP40, 0.25% Sodium deoxycholate, 5 mM EDTA, and 1 mM ethylene glycol-bis(2-aminoethyl-ether)-N, N, N, N-tetraacetic acid). The homogenates were centrifuged at 13,200 g for 40 minutes at 4°C. Protein (50 μg) was then separated by SDS-PAGE in 8% polyacrylamide and electrotransferred to polyvinylidene difluoride membranes. The membranes were incubated in blocking solution (5% milk) at room temperature for 2 hours. The membranes were then incubated with primary antibody including SIRT1 (sc-74465, Santa Cruz, USA), PGC-1α (#516557, Calbiochem, USA), FOXO3a (# 2497, Cell Signaling, USA), AMPK (sc-33524, Santa Cruz, USA), and α-tubulin (sc-74465, Santa Cruz, USA) overnight at 4°C. After washing, the membranes were incubated with a goat anti-rabbit (Santa Cruz, USA) or goat anti-mouse IgG (Santa Cruz, USA) peroxidase-conjugated secondary antibody directed against the primary antibody. The membranes were developed by an enhanced chemiluminescence western blot detection system..