SREBP1 is produced as a precursor protein that’s inserted to the endoplasmic reticulum. The SREBP1 precursor migrates in the Flupirtine for the Golgi and undergoes sequential proteolytic processing to produce the transcriptionally active form. Once the mature, active nuclear form of SREBP1 is translocated into the nucleus, it binds to sterol regulatory elements and activates the transcription of SREBP1 responsive genes, therefore promot ing lipogenesis in the liver. Nuclear protein amounts of SREBP1 were evaluated after treatment with BA for approximately 24 h, to explore the effect of BA on the translocation of SREBP1 into the nucleus. As shown in Fig. 1E, BA inhibited the translocation of mature SREBP1 into the nucleus in a dependent manner, suggesting that BA curbs hepatic fat accumulation by inhibiting SREBP1s maturation and thus stopping its transloca tion into the nucleus. Next, we examined whether BA stimulates the phosphorylation of AMPK in HepG2 cells because activated AMPK is well known to suppress SREBP1 cleavage and nuclear translocation, leading to reduced lipogenesis and fat accumulation in the liver. As shown in Fig. 2A and B, BA treatment led to significant increases in phosphorylation Skin infection of AMPK and its direct substrate ACC in a concentration dependent manner and time. The results of BA on AMPK phosphorylation and SREBP1, FAS, SCD1, PPARa and CD36 mRNA expression were all corrected in the presence of compound C. The inhibitory effect of BA on activity was also blunted in the presence of substance D, an AMPK inhibitor. These data show that AMPK is important for BA to suppress lipogenesis and to boost lipolysis by modulating gene transcription in hepatocytes. To further verify if the activation of AMPK inhibits intracellular lipid accumulation, HepG2 cells were pretreated with compound C and then stimulated with 40 mM BA. In the presence of substance D, the BA induced decrease in lipid content, as measured by Oil Red O staining, was changed almost to the amount observed in PF 573228 automobile treated control cells. While BA activates AMPK in HepG2 cells, it did not trigger recombinant AMPK kinase, meaning that BA activates AMPK ultimately. Liver kinase B 1 and Ca calmodulin depen dent protein kinase kinase are well-known upstream kinases for AMPK, and our data show that BA treatment increases CAMKK protein expression. BA induced increases of ACC and AMPK protein levels and decreases in hepatic lipid content were all reversed when the cells were pretreated with STO 609, showing that CAMKK works as an upstream kinase for AMPK in BA treated HepG2 cells. Previous studies have demonstrated that lipogenesis and SREBP1 activation involves the mTOR/S6K process. It seems likely that inhibition of SREBP1 action following glucose deprivation or AMPK activation is mediated by mTOR.