Proteomic analysis of the inhibitory effect of epigallocatechin gallate on lipid accumulation in human HepG2 cells

Author:

Liu Zhonghua,Li Qin,Huang Jianan,Liang Qionglin,Yan Yujun,Lin Haiyan,Xiao Wenjun,Lin Yong,Zhang Sheng,Tan Bin,Luo Guoan

Abstract

Abstract Background (−)-Epigallocatechin-3-gallate (EGCG), the most abundant catechin found in green tea, effectively reduces body weight and tissue and blood lipid accumulation. To explore the mechanism by which EGCG inhibits cellular lipid accumulation in free fatty acid (FFA) induced HepG2 cell culture, we investigated the proteome change of FFA-induced HepG2 cells exposed to EGCG using two-dimensional gel electrophoresis and mass spectrometry. Results In this study, 36 protein spots showed a significant change in intensity by more than 1.5-fold from the control group to the FFA group and from the FFA group to the FFA + EGCG group. Among them, 24 spots were excised from gels and identified by LC-MS/MS. In total, 18 proteins were successfully identified. All identified proteins were involved in lipid metabolism, glycometabolism, antioxidant defense, respiration, cytoskeleton organization, signal transduction, DNA repair, mRNA processing, iron storage, or were chaperone proteins. This indicated that these physiological processes may play roles in the mechanism of inhibition of lipid accumulation by EGCG in FFA-induced HepG2 cells. Western blotting analysis was used to verify the expression levels of differentially expressed proteins, which agree with the proteomic results. Conclusions From the proteomic analysis, we hypothesized that EGCG reduced cellular lipid accumulation in FFA-induced HepG2 cells through the activation of AMP-activated protein kinase (AMPK) resulting from the generation of reactive oxygen species (ROS). The induction of ROS may be a result of EGCG regulation of the antioxidant defense system. Activation of AMPK shifted some FFA toward oxidation, away from lipid and triglyceride storage, and suppressed hepatic gluconeogenesis. The findings of this study improve our understanding of the molecular mechanisms of inhibition of lipid accumulation by EGCG in HepG2 cells.

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Biochemistry

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