Apoptotic effect of MG-132 on human tongue squamous cell carcinoma

被引:10
作者
Chen, Shuang-feng [2 ]
Chen, Hai-ying [2 ]
Liu, Xian-bin [3 ]
Zhang, Ying-xin [2 ]
Liu, Wei [2 ]
Wang, Wei-hua [2 ]
Zhang, Bin [3 ]
Wang, Le-Xin [1 ]
机构
[1] Charles Sturt Univ, Sch Biomed Sci, Wagga Wagga, NSW 2650, Australia
[2] Taishan Med Univ, Cent Lab Expt Med, Liaocheng Peoples Hosp, Liaocheng & Liaocheng Clin Sch, Liaocheng 252000, Shandong, Peoples R China
[3] Taishan Med Univ, Dept Dent & Facial Surg, Liaocheng Peoples Hosp, Liaocheng & Liaocheng Clin Sch, Liaocheng 252000, Shandong, Peoples R China
关键词
MG-132; Apoptosis; E3 ubiquitin ligases; Tca-8113; cells; Squamous cell carcinoma; ENDOPLASMIC-RETICULUM STRESS; UNFOLDED PROTEIN RESPONSE; CANCER-CELLS; UBIQUITIN; DEATH; ENHANCEMENT; PROTEASOME;
D O I
10.1016/j.biopha.2011.04.009
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
The aim of this study was to investigate the apoptotic effect of a proteasome inhibitor MG-132 on Tca-8113, a cell line of human tongue squamous cell carcinoma. Tca-8113 cells were treated with 10, 20, and 30 mu M of MG-132, or 5 mu M thapsigargin. Apoptosis rate was determined with annexin V/propidium iodide double staining. Expression of E3ubiquitin-protein ligase was determined by ELISA, and Grp78 and caspase-12 mRNA, and Grp78 and caspase-12 protein was assessed by RT-PCR and Western blot, respectively. Apoptosis was observed 18 h after MG-132 treatment. The apoptotic rate in the 10, 20, and 30 mu M MG-132 group was 13.5, 19.6 and 34.7%, respectively, which was higher than in the thapsigargin (8.5%, P < 0.01) or control group (0.5%, P < 0.01). The expression of E3 ubiquitin-protein ligase in the 10, 20, and 30 mM MG-132 group was 28.75 +/- 2.28, 18.16 +/- 0.65, 8.85 +/- 0.72, respectively, which was lower than in the thapsigargin (38.96 +/- 0.33, P < 0.05 or 0.01) or control (40.88 +/- 4.52, P < 0.05 or 0.01) group. The levels of Grp78 and capase-12 mRNA, Grp78 and caspase-12 protein in the MG-132 groups were higher than in the control group (P < 0.01). In conclusion, MG-132 induces apoptosis in Tca-8113 cells in a concentration-dependent manner. The MG-132-induced apoptosis may involve downregulation of E3 ubiquitin ligase, and upregulation of Grp78 and caspase-12. Crown Copyright (C) 2011 Published by Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:322 / 327
页数:6
相关论文
共 24 条
[1]   Mammalian OS-9 Is Upregulated in Response to Endoplasmic Reticulum Stress and Facilitates Ubiquitination of Misfolded Glycoproteins [J].
Alcock, Felicity ;
Swanton, Eileithyia .
JOURNAL OF MOLECULAR BIOLOGY, 2009, 385 (04) :1032-1042
[2]  
Austin RC, 2009, ANTIOXID REDOX SIGN, V11, P2279, DOI [10.1089/ars.2009.2686, 10.1089/ARS.2009.2686]
[3]   RING Finger E3 Ubiquitin Ligases: Structure and Drug Discovery [J].
Chasapis, Christos T. ;
Spyroulias, Georgios A. .
CURRENT PHARMACEUTICAL DESIGN, 2009, 15 (31) :3716-3731
[4]   p28GANK inhibits endoplasmic reticulum stress-induced cell death via enhancement of the endoplasmic reticulum adaptive capacity [J].
Dai, Rong-Yang ;
Chen, Yao ;
Fu, Jing ;
Dong, Li-Wei ;
Ren, Yi-Bin ;
Yang, Guang-Zhen ;
Qian, You-Wen ;
Cao, Jie ;
Tang, Shan-Hua ;
Yang, Sheng-Li ;
Wang, Hong-Yang .
CELL RESEARCH, 2009, 19 (11) :1243-1257
[5]   Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism [J].
Di Sano, F ;
Ferraro, E ;
Tufi, R ;
Achsel, T ;
Piacentini, M ;
Cecconi, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (05) :2693-2700
[6]   Medical progress - Head and neck cancer [J].
Forastiere, A ;
Koch, W ;
Trotti, A ;
Sidransky, D .
NEW ENGLAND JOURNAL OF MEDICINE, 2001, 345 (26) :1890-1900
[7]   Overexpression of endoplasmic reticulum-resident chaperone attenuates cardiomyocyte death induced by proteasome inhibition [J].
Fu, Hai Ying ;
Minamino, Tetsuo ;
Tsukamoto, Osamu ;
Sawada, Tamaki ;
Asai, Mitsutoshi ;
Kato, Hisakazu ;
Asano, Yoshihiro ;
Fujita, Masashi ;
Takashima, Seiji ;
Hori, Masatsugu ;
Kitakaze, Masafumi .
CARDIOVASCULAR RESEARCH, 2008, 79 (04) :600-610
[8]   The endoplasmic reticulum:: Folding, calcium homeostasis, signaling, and redox control [J].
Goerlach, Agnes ;
Klappa, Peter ;
Kietzmann, Thomas .
ANTIOXIDANTS & REDOX SIGNALING, 2006, 8 (9-10) :1391-1418
[9]   Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death [J].
Haynes, CM ;
Titus, EA ;
Cooper, AA .
MOLECULAR CELL, 2004, 15 (05) :767-776
[10]   ER signaling in unfolded protein response [J].
Kaneko, M ;
Nomura, Y .
LIFE SCIENCES, 2003, 74 (2-3) :199-205