Myricetin Induces Apoptosis in HepG2 Cells Through Akt/p70S6K/Bad Signaling and Mitochondrial Apoptotic Pathway

Author(s): Xiao-Hong Zhang, Shi-Yong Chen, Lin Tang, Ying-Zhuo Shen, Lin Luo, Chen-Wei Xu, Qiong Liu, Duo Li

Journal Name: Anti-Cancer Agents in Medicinal Chemistry
(Formerly Current Medicinal Chemistry - Anti-Cancer Agents)

Volume 13 , Issue 10 , 2013

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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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Article Details

Year: 2013
Published on: 06 December, 2013
Page: [1575 - 1581]
Pages: 7
DOI: 10.2174/1871520613666131125123059
Price: $65

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