Puerarin increases the chemosensitivity of hepatocellular carcinoma cells
- Zhen Wu
- Jing Wu
- Ping Fang
- Shifeng Kan
Affiliations: Department of Clinical Laboratory, The Second Hospital of Shandong University, Jinan, Shangdong 250033, P.R. China, Department of Pharmacy, The Second Hospital of Shandong University, Jinan, Shangdong 250033, P.R. China, Department of Blood Transfusion, Qianfoshan Hospital of Shandong, Jinan, Shangdong 250014, P.R. China, Department of Clinical Laboratory, Qilu Hospital, Shandong University, Jinan, Shangdong 250012, P.R. China
- Published online on: July 5, 2017 https://doi.org/10.3892/ol.2017.6524
Copyright: © Wu
et al. This is an open access article distributed under the
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The present study investigated the effect of puerarin (Pu) on the sensitivity of HepG2 human hepatocellular carcinoma (HCC) cells to chemotherapeutic drugs to determine the possible mechanism. HepG2 cells were treated with different concentrations of Pu and cisplatin (CDDP), alone or in combination. MTT assay was used to determine the inhibitory effects of the different drugs on HepG2 cells. Cell morphology was observed by inverted microscopy. The expression of B-cell lymphoma 2 (Bcl-2) and Bax protein was measured by western blot analysis. Pu and CDDP, alone or in combination, inhibited the proliferation of HepG2 cells. The inhibitory effect of CDDP combined with Pu on HepG2 cells was significantly higher than that of the single drug treatments (p<0.01). In addition, compared with the single drug groups, cellular morphology was significantly altered and the apoptotic rate of cells and the expression of Bax protein were significantly increased (p<0.01). However, the expression of Bcl-2 protein was significantly decreased (p<0.01) in the combined drug group. In conclusion, Pu can increase the sensitivity of HCC to chemotherapeutic drugs, enhance the inhibitory effect of chemotherapeutic drugs on cell proliferation and synergistically induce apoptosis of HepG2 cells. The mechanism is likely related to the upregulation of Bax protein and the downregulation of Bcl-2 protein.