Basic Study
Copyright ©The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. Mar 21, 2016; 22(11): 3186-3195
Published online Mar 21, 2016. doi: 10.3748/wjg.v22.i11.3186
Melittin induces human gastric cancer cell apoptosis via activation of mitochondrial pathway
Gui-Mei Kong, Wen-Hua Tao, Ya-Li Diao, Peng-Hua Fang, Ji-Jun Wang, Ping Bo, Feng Qian
Gui-Mei Kong, Wen-Hua Tao, Peng-Hua Fang, Ji-Jun Wang, Ping Bo, Feng Qian, Department of Jiangsu Key Laboratory of Integrated Traditional Chinese and Western Medicine for Prevention and Treatment of Senile Diseases, Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Medical School of Yangzhou University, Yangzhou 225001, Jiangsu Province, China
Ya-Li Diao, Department of Gastroenterology, 1st Hospital of Yangzhou, Yangzhou 225009, Jiangsu Province, China
Author contributions: Kong GM and Tao WH contributed equally to this work; Bo P and Qian F designed the research; Kong GM, Tao WH and Diao YL performed the research; Tao WH, Fang PH and Wang JJ analyzed the data; and Kong GM wrote the paper.
Supported by the Natural Science Foundation of China, No. 30801497, No. 81272537 and No. 81472815; and the Natural Science Fund for Colleges and Universities in Jiangsu Province, No. 11KJD360003.
Institutional review board statement: The study was reviewed and approved by the medical school of Yangzhou University Institutional Review Board.
Institutional animal care and use committee statement: This article does not include animal trials.
Conflict-of-interest statement: To the best of our knowledge, no conflict of interest exists.
Data sharing statement: No additional data are available.
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Correspondence to: Feng Qian, MD, Department of Jiangsu Key Laboratory of Integrated Traditional Chinese and Western Medicine for Prevention and Treatment of Senile Diseases, Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Medical School of Yangzhou University, No. 88 Road, Yangzhou 225001, Jiangsu Province, China. amawy@126.com
Telephone: +86-514-87978872 Fax: +86-514-87341733
Received: September 5, 2015
Peer-review started: September 6, 2015
First decision: November 5, 2015
Revised: November 17, 2015
Accepted: December 12, 2015
Article in press: December 12, 2015
Published online: March 21, 2016
Processing time: 190 Days and 13.6 Hours
Abstract

AIM: To investigate the apoptotic effects of melittin on SGC-7901 cells via activation of the mitochondrial signaling pathway in vitro.

METHODS: SGC-7901 cells were stimulated by melittin, and its effect on proliferation and apoptosis of was investigated by methyl thiazolyl tetrazolium assay, morphologic structure with transmission electron microscopy, annexin-V/propidium iodide double-staining assay, measuring mitochondrial membrane potential (MMP) levels, and analyzing reactive oxygen species (ROS) concentrations were analyzed by flow cytometry. Cytochrome C (Cyt C), apoptosis-inducing factor (AIF), endonuclease G (Endo G), second mitochondria-derived activator of caspases (Smac)/direct IAP binding protein with low isoelectric point (Diablo), and FAS were analyzed by western blot. The expression of caspase-3 and caspase-8 was measured using activity assay kits.

RESULTS: Melittin was incubated at 1.0, 2.0, 4.0, or 6.0 μg/mL for 1, 2, 4, 6, or 8 h and showed a time- and concentration-dependent inhibition of SGC-7901 cell growth. Melittin induced SGC-7901 cell apoptosis, which was confirmed by typical morphological changes. Treatment with 4 μg/mL melittin induced early apoptosis of SGC-7901 cells, and the early apoptosis rates were 39.97% ± 3.19%, 59.27% ± 3.94%, and 71.50% ± 2.87% vs 32.63% ± 2.75% for 1, 2, and 4 h vs 0 h (n = 3, P < 0.05); the ROS levels were 616.53% ± 79.78%, 974.81% ± 102.40%, and 1330.94% ± 93.09% vs 603.74% ± 71.99% (n = 3, P < 0.05); the MMP values were 2.07 ± 0.05, 1.78 ± 0.29, and 1.16 ± 0.25 vs 2.55 ± 0.42 (n = 3, P < 0.05); caspase-3 activity was significantly higher compared to the control (5492.3 ± 321.1, 6562.0 ± 381.3, and 8695.7 ± 449.1 vs 2330.0 ± 121.9), but the caspase activity of the non-tumor cell line L-O2 was not different from that of the control. With the addition of the caspase-3 inhibitor (Ac-DEVD-CHO), caspase-3 activity was significantly decreased compared to the control group (1067.0 ± 132.5 U/g vs 8695.7 ± 449.1 U/g). The expression of the Cyt C, Endo G, and AIF proteins in SGC-7901 cells was significantly higher than those in the control (P < 0.05), while the expression of the Smac/Diablo protein was significantly lower than the control group after melittin exposure (P < 0.01). Ac-DEVD-CHO did not, however, have any effect on the expression of caspase-8 and FAS in the SGC-7901 cells.

CONCLUSION: Melittin can induce apoptosis of human gastric cancer (GC) cells through the mitochondria pathways, and it may be a potent agent in the treatment of human GC.

Keywords: Melittin; Gastric cancer; Mitochondrial; Apoptosis; Cytochrome C

Core tip: SGC-7901 cells stimulated by melittin displayed typical apoptotic morphology. In addition, reactive oxygen species release was induced, and the mitochondrial membrane permeability was rendered irreversibly open, causing a reduction in the mitochondrial membrane potential. These changes increased the release of cytochrome C, apoptosis-inducing factor, and endonuclease G and decreased second mitochondria-derived activator of caspases (Smac)/direct IAP binding protein with low isoelectric point (Diablo), which activated downstream caspase-3 and induced apoptosis.