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Abrogating HSP Response Augments Cell Death Induced by As2O3 in Glioma Cell Lines

Published online by Cambridge University Press:  02 December 2014

Xueming Song ,
Zhiqiang Chen ,
Chunbo Wu  and
Shiguang Zhao
Xueming Song
Affiliation:
Department of Neurosurgery, 1st Affiliated Hospital of Harbin Medical University, Nangang District, Harbin, P.R. China
Zhiqiang Chen
Affiliation:
Department of Neurosurgery, 1st Affiliated Hospital of Harbin Medical University, Nangang District, Harbin, P.R. China
Chunbo Wu
Affiliation:
Department of Neurosurgery, 1st Affiliated Hospital of Harbin Medical University, Nangang District, Harbin, P.R. China
Shiguang Zhao*
Affiliation:
Department of Neurosurgery, 1st Affiliated Hospital of Harbin Medical University, Nangang District, Harbin, P.R. China
*
Department of Neurosurgery, 1st Affiliated Hospital of Harbin Medical University. No 23, Youzheng Street, Nangang District, Harbin, P.R. China, 150001.
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Abstract

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Objectives:

We previously reported that Arsenic trioxide (ATO) can inhibit glioma growth both in vitro and in vivo. While the use of ATO alone for solid tumor treatment sometimes was found to be ineffective which may be due to the protective pathways including heat shock proteins (HSPs) response induced by ATO. In this study, we modified HSPs expression to investigate whether HSPs had some effect on ATO induced glioma cell death.

Methods:

Trypan bule exclusion assay, mitochondrial membrane potential (MMP) Assay, and SubG1 detection were used to evaluate cell viability and western-blot was employed to detect HSPs and some apoptosis markers expression induced by ATO. Heat pre-treatment, HSPs inhibitor, or Heat Shock factor-1 (HSF1) knockdown by SiRNA was employed to modify HSPs levels.

Results:

It was showed that KNK437 (HSPs inhibitor) or HSF1 knockdown significantly enhanced cell death, MMP disruption, JNK phosphorylation and caspase-3 cleavage induced by ATO, which was accompanied by abrogation of HSPs induction, while heat pre-treatment with clear HSPs induction had strong protection on the effects mentioned above.

Conclusion:

Those data suggested that HSPs play protective roles on ATO induced cell death in glioma. Inhibition of HSPs may have a synergistic effect with ATO on glioma treatment.

Type
Original Article
Information
Canadian Journal of Neurological Sciences , Volume 37 , Issue 4 , July 2010 , pp. 504 - 511
Copyright
Copyright © The Canadian Journal of Neurological 2010

References

1. Berger, F, Gay, E, Pelletier, L, Tropel, P, Wion, D. Development of gliomas: potential role of asymmetrical cell division of neural stem cells. Lancet Oncol. 2004;5(8):511–4.Google Scholar
2. Carpentier, AF. Neuro-oncology: the growing role of chemotherapy in glioma. Lancet Neurol. 2005;4(1):4–5.Google Scholar
3. Jeong, M, Kwon, YS, Park, SH, Kim, CY, Jeun, SS, Song, KW, et al. Possible novel therapy for malignant gliomas with secretable trimeric TRAIL. PLoS One. 2009;4(2):e4545.Google Scholar
4. Zhao, S, Zhang, X, Zhang, J, Zhang, J, Zou, H, Liu, Y, et al. Intravenous administration of arsenic trioxide encapsulated in liposomes inhibits the growth of C6 gliomas in rat brains. J Chemother. 2008;20(2):253–62.Google Scholar
5. Zhao, S, Zhang, J, Zhang, X, Dong, X, Sun, X. Arsenic trioxide induces different gene expression profiles of genes related to growth and apoptosis in glioma cells dependent on the p53 status. Mol Biol Rep. 2008;35(3):421–9.Google Scholar
6. Zhao, S, Tsuchida, T, Kawakami, K, Shi, C, Kawamoto, K. Effect of As2O3 on cell cycle progression and cyclins D1 and B1 expression in two glioblastoma cell lines differing in p53 status. Int J Oncol. 2002;21(1):49–55.Google Scholar
7. Simeonova, PP, Wang, S, Toriuma, W, Kommineni, V, Matheson, J, Unimye, N, et al. Arsenic mediates cell proliferation and gene expression in the bladder epithelium: association with activating protein-1 transactivation. Cancer Res. 2000;60(13):3445–53.Google Scholar
8. Miller, WH Jr, Schipper, HM, Lee, JS, Singer, J, Waxman, S. Mechanisms of action of arsenic trioxide. Cancer Res. 2002;62 (14):3893–903.Google Scholar
9. Wu, YC, Yen, WY, Lee, TC, Yih, LH. Heat shock protein inhibitors, 17-DMAG and KNK437, enhance arsenic trioxide-induced mitotic apoptosis. Toxicol Appl Pharmacol. 2009;236(2):231–8.Google Scholar
10. Yih, LH, Peck, K, Lee, TC. Changes in gene expression profiles of human fibroblasts in response to sodium arsenite treatment. Carcinogenesis. 2002;23(5):867–76.Google Scholar
11. Dilda, PJ, Hogg, PJ. Arsenical-based cancer drugs. Cancer Treat Rev. 2007;33(6):542–64.Google Scholar
12. Liu, B, Pan, S, Dong, X, Qiao, H, Jiang, H, Krissansen, GW, et al. Opposing effects of arsenic trioxide on hepatocellular carcinomas in mice. Cancer Sci. 2006;97(7):675–81.Google Scholar
13. Liu, J, Kadiiska, MB, Liu, Y, Lu, T, Qu, W, Waalkes, MP. Stress-related gene expression in mice treated with inorganic arsenicals. Toxicol Sci. 2001;61(2):314–20.Google Scholar
14. Khalil, S, Luciano, J, Chen, W, Liu, AY. Dynamic regulation and involvement of the heat shock transcriptional response in arsenic carcinogenesis. J Cell Physiol. 2006;207(2):562–9.Google Scholar
15. Wetzler, M, Earp, JC, Brady, MT, Keng, MK, Jusko, WJ. Synergism between arsenic trioxide and heat shock protein 90 inhibitors on signal transducer and activator of transcription protein 3 activity-pharmacodynamic drug-drug interaction modeling. Clin Cancer Res. 2007;13(7):2261–70.Google Scholar
16. Arndt, V, Rogon, C, Höhfeld, J. To be, or not to be — molecular chaperones in protein degradation. Cell Mol Life Sci. 2007;64 (19-20):2525–41.Google Scholar
17. Picard, D. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci. 2002;59(10):1640–8.Google Scholar
18. Brodsky, JL, Chiosis, G. Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Curr. Top Med Chem. 2006;6(11):1215–25.Google Scholar
19. Camphausen, K, Tofilon, PJ. Inhibition of Hsp90: a multitarget approach to radiosensitization. Clin Cancer Res. 2007;13(15 Pt 1):4326–30.Google Scholar
20. Jiang, B, Xiao, W, Shi, Y, Liu, M, Xiao, X. Heat shock pretreatment inhibited the release of Smac/DIABLO from mitochondria and apoptosis induced by hydrogen peroxide in cardiomyocytes and C2C12 myogenic cells. Cell Stress Chaperon. 2005;10(3): 252–62.Google Scholar
21. Beere, HM, Wolf, BB, Cain, K, Mosser, DD, Mahboubi, A, Kuwana, T, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol. 2000;2(8):469–75.Google Scholar
22. Bivik, C, Rosdahl, I, Ollinger, K. Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes. Carcinogenesis. 2007;28 (3):537–44.CrossRefGoogle ScholarPubMed
23. Beere, HM. Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways. J Clin Invest. 2005;115(10):2633–9.Google Scholar
24. Bross, PF, Kane, R, Farrell, AT, Abraham, S, Benson, K, Brower, ME, et al. Approval summary for bortezomib for injection in the treatment of multiple myeloma. Clin Cancer Res. 2004;10(12 Pt 1):3954–64.Google Scholar
25. Westerheide, SD, Morimoto, RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem. 2005;280(39):33097–100.Google Scholar
26. Jolly, C, Morimoto, RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst. 2000;92(19):1564–72.Google Scholar
27. Gorman, AM, Heavey, B, Creagh, E, Cotter, TG, Samali, A. Antioxidant-mediated inhibition of the heat shock response leads to apoptosis. FEBS Lett. 1999;445(1):98–102.Google Scholar
28. Khalil, S, Luciano, J, Chen, W, Liu, AY. Dynamic regulation and involvement of the heat shock transcriptional response in arsenic carcinogenesis. J Cell Physiol. 2006;207(2):562–9.Google Scholar
29. Gabai, VL, Meriin, AB, Mosser, DD, Caron, AW, Rits, S, Shifrin, VI, et al. Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance. J Biol Chem. 1997;272 (29):18033–7.Google Scholar
30. Gabai, VL, Yaglom, JA, Volloch, V, Meriin, AB, Force, T, Koutroumanis, M, et al. Hsp72-mediated suppression of c-Jun Nterminal kinase is implicated in development of tolerance to caspase-independent cell death. Mol Cell Biol. 2000;20(18): 6826–36.Google Scholar
31. Park, HS, Lee, JS, Huh, SH, Seo, JS, Choi, EJ. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J. 2001;20(3):446–56.Google Scholar
32. Volloch, V, Gabai, VL, Rits, S, Force, T, Sherman, MY. HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK. Cell Stress Chaperones. 2000;5(2):139–47.Google Scholar
33. Gabai, VL, Meriin, AB, Yaglom, JA, Wei, JY, Mosser, DD, Sherman, MY. Suppression of stress kinase JNK is involved in HSP72-mediated protection of myogenic cells from transient energy deprivation. HSP72 alleviates the stress-induced inhibition of JNK dephosphorylation. J Biol Chem. 2000;275(48):38088–94.Google Scholar