Premium
Identification of Molecular Target Proteins in Berberine‐treated Cervix Adenocarcinoma HeLa Cells by Proteomic and Bioinformatic Analyses
Author(s) -
Lu Binan,
Zhao Jing,
Xu Lina,
Xu Yousong,
Wang Xiaona,
Peng Jinyong
Publication year - 2012
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.3615
Subject(s) - berberine , hela , annexin , apoptosis , annexin a2 , prohibitin , microbiology and biotechnology , heat shock protein , hsp70 , interactome , biology , chemistry , biochemistry , cell , gene
In this study, the apoptosis of HeLa cells induced by berberine was investigated. Fifty‐one differentially expressed proteins were identified before and after berberine treatment by a proteomic method, which either interacted with each other directly or through one intermediate protein to form a connected protein interaction sub‐network. Nine of them were selected and validated. Compared with the cells in the control group, the expressions of 14‐3‐3σ and lamin‐A/C of the cells treated by berberine for 48 h increased by 94.12 and 5.24 times, respectively, and the expressions of annexin A5, cytokeratin 17, prohibitin, heat shock cognate 71 kDa protein (HSPA8), programmed cell death 6 and vimentin decreased by 4.1, 1.34, 23.8, 11.85, 4.63 and 5.24 times, respectively. In addition, tubulin‐β decreased from 9537 to 6908 ng/L. Furthermore, the inverse dock program (INVDOCK) was used to predict the possible drug‐target of berberine's anticancer activity, and the results showed that HSPA8 and annexin A5 might be the drug targets. This study suggests that the anticancer effect of berberine on HeLa cells was a complex process based on affecting multiple protein expression and acting on an interaction network. Our work could be helpful to elucidate the mechanism of berberine's anticancer activity on HeLa cells. Copyright © 2011 John Wiley & Sons, Ltd.