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. Author manuscript; available in PMC: 2014 Oct 31.
Published in final edited form as: Am J Physiol Gastrointest Liver Physiol. 2007 Aug 16;293(4):G894–G902. doi: 10.1152/ajpgi.00133.2007

Fig. 4.

Fig. 4

Betaine supplementation resulted in increased phosphorylation (p-) of hepatic AMP-activated protein kinase (AMPK) and inhibited acetyl-CoA carboxylase (ACC) activation. Male C57BL/6 mice were fed with high-sucrose diet in the presence or absence of betaine supplementation (1%) in the drinking water for 16 wk. Total protein extracts from liver tissues were prepared thereafter. Forty micrograms of protein were subjected to Western blot analysis for AMPK or ACC phosphorylation using antibodies specific for AMPK phosphorylated at Thr172 and ACC phosphorylated at Ser79. A: Western blot assay for AMPK. Betaine supplementation increased phosphorylation of liver AMPK (activation). B: quantification of p-AMPK protein levels in different groups. Levels were normalized to total AMPK. Data are means ± SD (n = 6–7). Bars with different letters differ significantly (P < 0.05). C: Western blot assay for ACC. Betaine supplementation attenuated the increase of ACC protein content induced by high-sucrose feeding and increased phosphorylation of ACC (inhibition) in the liver. D: quantification of p-ACC and total ACC protein levels in different groups. Levels were normalized to actin. Data are means ± SD (n = 6–7). Bars with different letters differ significantly (P < 0.05).