Effects of ginkgol C17:1 on cisplatin‑induced autophagy and apoptosis in HepG2 cells
- Jun Liu
- Yueying Li
- Xiaoming Yang
- Yan Dong
- Jing Wu
- Min Chen
Published online on: November 14, 2017
Copyright: © Liu et al.
This is an open access article distributed under the terms of Creative Commons Attribution License.
Previous studies have demonstrated that ginkgol C17:1 significantly inhibits human liver cancer cells and enhances the anticancer activity of cisplatin in vivo and in vitro. However, the mechanism and biological function of ginkgol C17:1 on cells undergoing chemotherapy remain unclear. The aim of the present study was to determine the antitumor activity and mechanism of ginkgol C17:1 in combination with cisplatin in human hepatoblastoma HepG2 cells. The green fluorescent protein (GFP)‑light chain 3 (LC3) adenovirus was transfected into HepG2 cells and autophagic flux was determined using fluorescence microscopy. Western blot analysis was also conducted to measure the expression of proteins associated with apoptosis, autophagy and their associated signaling pathways. Compared with the control group, autophagic flux and nucleus aberration rates were significantly increased (P<0.05), and the expression of proteins associated with autophagy and apoptosis were increased in the groups treated with cisplatin or ginkgol C17:1, respectively. However, following co‑treatment with ginkgol C17:1 and cisplatin, the autophagic flux and the expression of autophagy proteins decreased; however, the nucleus aberration rate and apoptosis protein expression significantly increased (P<0.05) compared with the group treated with cisplatin alone. Additionally, the signaling pathways of autophagy and apoptosis were also activated following treatment with cisplatin, alone and in combination with ginkgol C17:1. Taken together, these results indicate that ginkgol C17:1 inhibits cisplatin‑induced autophagy via AMP‑activated protein kinase/ULK1signaling and increases cisplatin‑induced apoptosis in HepG2 cells via the phosphoinositide 3‑kinase/Akt/mechanistic target of rapamycin pathway.