Proteomic analysis of hepatocellular carcinoma HepG2 cells treated with platycodin D.
10.1016/S1875-5364(15)30065-0
- Author:
Jin-Jian LU
1
;
De-Zhao LU
2
;
Yu-Fei CHEN
2
;
Ya-Ting DONG
2
;
Jun-Ren ZHANG
2
;
Ting LI
3
;
Zheng-Hai TANG
3
;
Zhen YANG
2
Author Information
1. State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macao, China. Electronic address: jinjian.lu@163.com.
2. College of Life Sciences, Zhejiang Chinese Medical University, Hangzhou 310053, China.
3. State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macao, China.
- Publication Type:Journal Article
- Keywords:
2-D DIGE;
HepG2;
Platycodin D;
Proteome
- MeSH:
Antineoplastic Agents, Phytogenic;
pharmacology;
therapeutic use;
Apoptosis;
Blotting, Western;
Campanulaceae;
chemistry;
Carcinoma, Hepatocellular;
drug therapy;
metabolism;
Cell Proliferation;
Cell Survival;
Hep G2 Cells;
Humans;
Liver Neoplasms;
drug therapy;
metabolism;
Phytotherapy;
Plant Extracts;
pharmacology;
therapeutic use;
Proteome;
metabolism;
Proteomics;
Saponins;
pharmacology;
therapeutic use;
Triterpenes;
pharmacology;
therapeutic use;
Up-Regulation
- From:
Chinese Journal of Natural Medicines (English Ed.)
2015;13(9):673-679
- CountryChina
- Language:English
-
Abstract:
Platycodin D (PD), a triterpenoid saponin isolated from Platycodonis Radix, is a famous Chinese herbal medicine that has been shown to have anti-proliferative effects in several cancer cell lines. The aim of this study was to determine the changes in cellular proteins after the treatment of hepatocellular carcinoma HepG2 cells with PD using proteomics approaches. The cell viability was determined using the MTT assay. The proteome was analyzed by two-dimensional difference gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Western blot analysis was used to confirm the expression of changed proteins. Our results showed that PD inhibited the proliferation of HepG2 cells in concentration- and time-dependent manners. Sixteen proteins were identified to be up-regulated in PD-treated HepG2 cells, including ATP5H, OXCT1, KRT9, CCDC40, ERP29, RCN1, ZNF175, HNRNPH1, HSP27, PA2G4, PHB, BANF1, TPM3, ECH1, LGALS1, and MYL6. Three proteins (i.e., RPS12, EMG1, and KRT1) decreased in HepG2 cells after treatment with PD. The changes in HSP27 and PHB were further confirmed by Western blotting. In conclusion, our results shed new lights on the mechanisms of action for the anti-cancer activity of PD.
