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BioMed Research International
Volume 2016, Article ID 5013409, 8 pages
Research Article

FBS or BSA Inhibits EGCG Induced Cell Death through Covalent Binding and the Reduction of Intracellular ROS Production

1Department of Toxicology, Zhejiang University School of Public Health, Hangzhou, Zhejiang 310058, China
2Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597
3Department of Toxicology, School of Public Health, Hangzhou Normal University, 16 Xue Lin Street, Hangzhou, Zhejiang 310036, China
4Collaborative Innovation Center for the Diagnosis and Treatment of Infectious Diseases, National Key Laboratory for the Diagnosis and Treatment of Infectious Diseases, The First Affiliated Hospital, Zhejiang University, Hangzhou, Zhejiang 310003, China

Received 3 June 2016; Revised 5 August 2016; Accepted 24 August 2016

Academic Editor: Jayesh Mudgal

Copyright © 2016 Yin Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Previously we have shown that ()-epigallocatechin gallate (EGCG) can induce nonapoptotic cell death in human hepatoma HepG2 cells only under serum-free condition. However, the underlying mechanism for serum in determining the cell fate remains to be answered. The effects of fetal bovine serum (FBS) and its major component bovine serum albumin (BSA) on EGCG-induced cell death were investigated in this study. It was found that BSA, just like FBS, can protect cells from EGCG-induced cell death in a dose-dependent manner. Detailed analysis revealed that both FBS and BSA inhibited generation of ROS to protect against toxicity of EGCG. Furthermore, EGCG was shown to bind to certain cellular proteins including caspase-3, PARP, and α-tubulin, but not LC3 nor β-actin, which formed EGCG-protein complexes that were inseparable by SDS-gel. On the other hand, addition of FBS or BSA to culture medium can block the binding of EGCG to these proteins. In silico docking analysis results suggested that BSA had a stronger affinity to EGCG than the other proteins. Taken together, these data indicated that the protective effect of FBS and BSA against EGCG-induced cell death could be due to (1) the decreased generation of ROS and (2) the competitive binding of BSA to EGCG.