Figure 6. DHMBA-indcuced activation of AMPK and ACC in C2C12 myotubes. C2C12 myotubes were incubated with 500 μM DHMBA in the differentiation medium for the time periods indicated. Oligomycin A and Compound C were used as a positive and negative control, respectively. Cells were lysed and Western blotting was performed to measure the phosphorylated and total protein expression of AMPKα, AMPKβ1, and ACC. β-actin protein levels were used as a control for equal protein loading. A ratio between phosphorylated form and total form of AMPK, ACC is presented in the bar graph. Data are the means ± SD of four separate experiments. a, P <0.05;b, P<0.01, as compared to control : Improvement of Mitochondrial Function and Lipid Utilization by 3,5-dihydroxy-4-methoxybenzyl Alcohol, an Oyster-derived polyphenol, in Oleate-loaded C2C12 Myotubes : Science and Education Publishing

Figure 6. DHMBA-indcuced activation of AMPK and ACC in C2C12 myotubes. C2C12 myotubes were incubated with 500 μM DHMBA in the differentiation medium for the time periods indicated. Oligomycin A and Compound C were used as a positive and negative control, respectively. Cells were lysed and Western blotting was performed to measure the phosphorylated and total protein expression of AMPKα, AMPKβ1, and ACC. β-actin protein levels were used as a control for equal protein loading. A ratio between phosphorylated form and total form of AMPK, ACC is presented in the bar graph. Data are the means ± SD of four separate experiments. ^a, P <0.05;^b, P<0.01, as compared to control

Journal of Food and Nutrition Research. 2016, 4(8), 498-507 doi:10.12691/jfnr-4-8-3