CaMKKβ Is Involved in AMP-Activated Protein Kinase Activation by Baicalin in LKB1 Deficient Cell Lines (original) (raw)
Figure 1
Baicalin increases the phosphorylation of AMPKα and ACC without effect on ATP in HeLa cells.
Levels of AMPKα phosphorylated at Thr-172 (pAMPKα) and of AMPK substrate ACC phosphorylated at Ser-79 (pACC) as well as total AMPKα and ACC were determined by Western blotting. Cells were treated with baicalin or AICAR (500 µM) for the indicated times without (A) or with (B) pre-treatment of the AMPK inhibitor compound C (40 µM). Histograms represent the fold change in the pAMPKα/AMPKα or pACC/ACC ratio from at least three independent experiments. (C) Cells were incubated with baicalin for indicated times and ATP levels were measured. All values are the mean ± SE for three independent experiments. * p<0.05 compared to respective control; # p<0.05 compared to respective baicalin group in the absence of compound C. Representative Western blots are shown.