Bag-1 Silence Sensitizes Non-Small Cell Lung Cancer Cells To Cisplatin Through Multiple Gene Pathways

References

• Ferlay J, Soerjomataram I, Dikshit R, et al. Cancer incidence and mortality worldwide: sources, methods and major patterns in GLOBOCAN 2012. Int J Cancer. 2015;136(5):E359–E386. doi:10.1002/ijc.2921025220842
   PubMed Web of Science ®Google Scholar
• Chen W, Zheng R, Baade PD, et al. Cancer statistics in China, 2015. CA Cancer J Clin. 2016;66(2):115–132. doi:10.3322/caac.2133826808342
   PubMed Web of Science ®Google Scholar
• Zheng R, Zeng H, Zhang S, et al. Lung cancer incidence and mortality in China, 2010. Throac Cancer. 2014;5(4):330–336. doi:10.1111/1759-7714.12098
   PubMed Web of Science ®Google Scholar
• Takayama S, Sato T, Krajewski S, et al. Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell. 1995;80(2):279–284. doi:10.1016/0092-8674(95)90410-77834747
   PubMed Web of Science ®Google Scholar
• Doong H, Vrailas A, Kohn EC. What’s in the ‘BAG’?–A functional domain analysis of the BAG-family proteins. Cancer Lett. 2002;188(1–2):25–32. doi:10.1016/s0304-3835(02)00456-112406544
   PubMed Web of Science ®Google Scholar
• Packham G, Brimmell M, Cleveland JL. Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation. Biochem J. 1997;328(Pt 3):807–813. doi:10.1042/bj32808079396724
   PubMedGoogle Scholar
• Wang YD, Ha MW, Cheng J, et al. The role of expression and polymorphism of the BAG-1 gene in response to platinum-based chemotherapeutics in NSCLC. Oncol Rep. 2012;27(4):979–986. doi:10.3892/or.2011.159122179630
   PubMed Web of Science ®Google Scholar
• Lin PL, Wu TC, Wu DW, Wang L, Chen CY, Lee H. An increase in BAG-1 by PD-L1 confers resistance to tyrosine kinase inhibitor in non-small cell lung cancer via persistent activation of ERK signalling. Eur J Cancer. 2017;85:95–105. doi:10.1016/j.ejca.2017.07.02528892778
   PubMed Web of Science ®Google Scholar
• Liu H, Bai Y, Liu B, et al. [The expression of BAG-1 and its clinical significance in human lung cancer.]. Zhongguo Fei Ai Za Zhi. 2008;11(4):489–494. doi:10.3779/j.issn.1009-3419.2008.04.04020735955
   PubMedGoogle Scholar
• Leng XF, Chen MW, Xian L, Dai L, Ma GY, Li MH. Combined analysis of mRNA expression of ERCC1, BAG-1, BRCA1, RRM1 and TUBB3 to predict prognosis in patients with non-small cell lung cancer who received adjuvant chemotherapy. J Exp Clin Cancer Res. 2012;31:25. doi:10.1186/1756-9966-31-2522439756
   PubMed Web of Science ®Google Scholar
• Liu H, Liang Y, Li Y, et al. Gene silencing of BAG-1 modulates apoptotic genes and sensitizes lung cancer cell lines to cisplatin-induced apoptosis. Cancer Biol Ther. 2010;9(10):832–840. doi:10.4161/cbt.9.10.1158920404511
   PubMed Web of Science ®Google Scholar
• Hu D, Chen F, Guan C, Yang F, Qu Y. Anti-hypoxia effect of adenovirus-mediated expression of heat shock protein 70 (HSP70) on primary cultured neurons. J Neurosci Res. 2013;91(9):1174–1182. doi:10.1002/jnr.2324023686726
   PubMed Web of Science ®Google Scholar
• Srivastava RK, Pant AB, Kashyap MP, et al. Multi-walled carbon nanotubes induce oxidative stress and apoptosis in human lung cancer cell line-A549. Nanotoxicology. 2011;5(2):195–207. doi:10.3109/17435390.2010.50394420804439
   PubMed Web of Science ®Google Scholar
• Chen T, Gao F, Feng S, Yang T, Chen M. MicroRNA-134 regulates lung cancer cell H69 growth and apoptosis by targeting WWOX gene and suppressing the ERK1/2 signaling pathway. Biochem Biophys Res Commun. 2015;464(3):748–754. doi:10.1016/j.bbrc.2015.07.02126166818
   PubMed Web of Science ®Google Scholar
• Nakayama H, Fujio Y, Yamaguchi O. [Calcium dependent signaling in cardiac hypertrophy and cell death]. Clin Calcium. 2013;23(4):505–515. CliCa130450551523545740
   PubMedGoogle Scholar
• Seo SR, Seo JT. Calcium overload is essential for the acceleration of staurosporine-induced cell death following neuronal differentiation in PC12 cells. Exp Mol Med. 2009;41(4):269–276. doi:10.3858/emm.2009.41.4.03019299916
   PubMed Web of Science ®Google Scholar
• Li QQ, Wang G, Liang H, et al. beta-Elemene promotes cisplatin-induced cell death in human bladder cancer and other carcinomas. Anticancer Res. 2013;33(4):1421–1428.23564782
   PubMed Web of Science ®Google Scholar
• Ozaki K, Hanazawa S. Porphyromonas gingivalis fimbriae inhibit caspase-3-mediated apoptosis of monocytic THP-1 cells under growth factor deprivation via extracellular signal-regulated kinase-dependent expression of p21 Cip/WAF1. Infect Immun. 2001;69(8):4944–4950. doi:10.1128/IAI.69.8.4944-4950.200111447172
   PubMed Web of Science ®Google Scholar
• Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 1993;74(4):609–619. doi:10.1016/0092-8674(93)90509-o8358790
   PubMed Web of Science ®Google Scholar
• Hohfeld J, Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. Embo J. 1997;16(20):6209–6216. doi:10.1093/emboj/16.20.62099321400
   PubMed Web of Science ®Google Scholar
• Kabbage M, Dickman MB. The BAG proteins: a ubiquitous family of chaperone regulators. Cell Mol Life Sci. 2008;65(9):1390–1402. doi:10.1007/s00018-008-7535-218264803
   PubMed Web of Science ®Google Scholar
• Rampelt H, Mayer MP, Bukau B. Nucleotide exchange factors for Hsp70 chaperones. Methods Mol Biol. 2011;787:83–91. doi:10.1007/978-1-61779-295-3_721898229
   PubMedGoogle Scholar
• Takayama S, Bimston DN, Matsuzawa S, et al. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. Embo J. 1997;16(16):4887–4896. doi:10.1093/emboj/16.16.48879305631
   PubMed Web of Science ®Google Scholar
• Takayama S, Reed JC. Molecular chaperone targeting and regulation by BAG family proteins. Nat Cell Biol. 2001;3(10):E237–E241. doi:10.1038/ncb1001-e23711584289
   PubMed Web of Science ®Google Scholar
• Wang Y, Jia C, Li QS, Xie CY, Zhang N, Qu Y. BAG-1L protects SH-SY5Y neuroblastoma cells against hypoxia/re-oxygenation through up-regulating HSP70 and activating PI3K/AKT signaling pathway. Neurochem Res. 2017;42(10):2861–2868. doi:10.1007/s11064-017-2304-y28523530
   PubMed Web of Science ®Google Scholar
• Juric D, Krop I, Ramanathan RK, et al. Phase I dose-escalation study of taselisib, an oral PI3K inhibitor, in patients with advanced solid tumors. Cancer Discov. 2017;7(7):704–715. doi:10.1158/2159-8290.CD-16-108028331003
   PubMed Web of Science ®Google Scholar
• Jin G, Kim MJ, Jeon HS, et al. PTEN mutations and relationship to EGFR, ERBB2, KRAS, and TP53 mutations in non-small cell lung cancers. Lung Cancer. 2010;69(3):279–283. doi:10.1016/j.lungcan.2009.11.01220018398
   PubMed Web of Science ®Google Scholar
• Ali K, Soond DR, Pineiro R, et al. Inactivation of PI(3)K p110delta breaks regulatory T-cell-mediated immune tolerance to cancer. Nature. 2014;510(7505):407–411. doi:10.1038/nature1344424919154
   PubMed Web of Science ®Google Scholar
• Cidado J, Park BH. Targeting the PI3K/Akt/mTOR pathway for breast cancer therapy. J Mammary Gland Biol Neoplasia. 2012;17(3–4):205–216. doi:10.1007/s10911-012-9264-222865098
   PubMed Web of Science ®Google Scholar
• Zhao R, Chen M, Jiang Z, et al. Platycodin-D induced autophagy in non-small cell lung cancer cells via PI3K/Akt/mTOR and MAPK signaling pathways. J Cancer. 2015;6(7):623–631. doi:10.7150/jca.1129126078792
   PubMed Web of Science ®Google Scholar
• Klemke RL, Cai S, Giannini AL, Gallagher PJ, de Lanerolle P, Cheresh DA. Regulation of cell motility by mitogen-activated protein kinase. J Cell Biol. 1997;137(2):481–492. doi:10.1083/jcb.137.2.4819128257
   PubMed Web of Science ®Google Scholar
• Kiyokawa E, Takai S, Tanaka M, et al. Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in various human tumors. Cancer Res. 1994;54(14):3645–3650.8033077
   PubMed Web of Science ®Google Scholar
• Bravo-Sagua R, Parra V, Lopez-Crisosto C, Diaz P, Quest AF, Lavandero S. Calcium transport and signaling in mitochondria. Compr Physiol. 2017;7(2):623–634. doi:10.1002/cphy.c16001328333383
   PubMed Web of Science ®Google Scholar
• Pinton P, Giorgi C, Siviero R, Zecchini E, Rizzuto R. Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis. Oncogene. 2008;27(50):6407–6418. doi:10.1038/onc.2008.30818955969
   PubMed Web of Science ®Google Scholar
• Vanderheyden V, Devogelaere B, Missiaen L, De Smedt H, Bultynck G, Parys JB. Regulation of inositol 1,4,5-trisphosphate-induced Ca2+ release by reversible phosphorylation and dephosphorylation. Biochim Biophys Acta. 2009;1793(6):959–970. doi:10.1016/j.bbamcr.2008.12.00319133301
   PubMed Web of Science ®Google Scholar
• Hockenbery DM, Zutter M, Hickey W, Nahm M, Korsmeyer SJ. BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death. Proc Natl Acad Sci U S A. 1991;88(16):6961–6965. doi:10.1073/pnas.88.16.69611871110
   PubMed Web of Science ®Google Scholar
• Rong YP, Bultynck G, Aromolaran AS, et al. The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor. Proc Natl Acad Sci U S A. 2009;106(34):14397–14402. doi:10.1073/pnas.090755510619706527
   PubMed Web of Science ®Google Scholar
• Chen R, Valencia I, Zhong F, et al. Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate. J Cell Biol. 2004;166(2):193–203. doi:10.1083/jcb.20030914615263017
   PubMed Web of Science ®Google Scholar
• Hanson CJ, Bootman MD, Distelhorst CW, Wojcikiewicz RJ, Roderick HL. Bcl-2 suppresses Ca2+ release through inositol 1,4,5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content. Cell Calcium. 2008;44(3):324–338. doi:10.1016/j.ceca.2008.01.00318407350
   PubMed Web of Science ®Google Scholar
• Leone V, Langella C, Esposito F, et al. Ccdc6 knock-in mice develop thyroid hyperplasia associated to an enhanced CREB1 activity. Oncotarget. 2015;6(17):15628–15638. doi:10.18632/oncotarget.385825970781
   PubMedGoogle Scholar