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. 2010 Sep 1;299(5):C1171–C1179. doi: 10.1152/ajpcell.00514.2009

Fig. 1.

Fig. 1.

Effects of serum starvation on the phosphorylation status of potential insulin sensitivity factors. Shown are representative Western blots from cells incubated at 37°C in serum-containing medium (C, control) or serum-free medium (SS, serum starved) for 3 h. A: phosphorylated AMP-activated protein kinase (P-AMPK) and AMPK (n = 6/group). B: phosphorylated acetyl-CoA carboxylase (P-ACC) and ACC (probed with streptavidin) (n = 8–9/group). C: phosphorylated ataxia telangiectasia mutated (P-ATM)-S1981 and ATM (n = 8/group). D: P-Akt S473 and Akt (n = 15/group). E: P-Akt T308 and Akt (n = 6/group). F: phosphorylated Akt substrate (P-AS) and AS160 (n = 6/group). G: P-p38 and p38 (n = 6/group). H: P-PKCζ/λ and Akt (n = 3/group). I: Western blotting using lysates from control and serum-starved myotubes in parallel with lysates from livers of wild-type mice (ATM+/+) and transgenic mice (ATM−/−) lacking functional ATM. The ATM bands from myotubes correspond with the positive control ATM band from ATM+/+ mouse liver and are at the appropriate molecular weight. Values are means ± SE. *Significantly different corresponding value from non-serum-starved control (P < 0.05).