Myricetin Induces Apoptosis in HepG2 Cells Through Akt/p70S6K/Bad Signaling and Mitochondrial Apoptotic Pathway
The present investigation was undertaken to gain insight into the molecular mechanism by which myricetin induces apoptosis
in human hepatocarcinoma HepG2 cells. Myricetin caused the disruption of mitochondrial membrane potential in a dose-dependent
manner. Moreover, myricetin triggered translocation of the pro-apoptotic protein Bax to the mitochondria, downregulation of anti-apoptotic
Bcl-2 expression and upregulated the expression of pro-apoptotic protein Bad in the mitochondria. The present study also showed that
myricetin promoted the release of cytochrome C from mitochondria into the cytosol followed by an increase in the proteolytic activation
of caspase-3 and the concomitant degradation of PARP protein. Additionally, western blot analysis showed that the Akt/p70s6k1
pathway was inhibited in myricetin-treated HepG2 cells, accordingly the phosphorylation of Bad at Ser136 was downregulated.
Collectively, these findings indicate that myricetin induced apoptosis in HepG2 cell through mitochondria apoptotic pathway and
Akt/p70s6k1/Bad signaling. Present results provide new information on the possible mechanisms for the anti-cancer activity of myricetin.
Keywords: Akt/p70s6k1/Bad signaling, apoptosis, HepG2 cell, mechanism, myricetin.
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