Acknowledgement
This work was supported by a grant (NRF-2019R1A2C10861 5114 to J.-A.K.) from the National Research Foundation, Ministry of Science and ICT, and by the Korea Research Institute of Bioscience and Biotechnology (KRIBB) Research Initiative Program (171134054 to J.-A.K. and 1711170633 to J.-H.K and J.-A.K.).
References
- Llovet JM, Ricci S, Mazzaferro V et al (2008) Sorafenib in advanced hepatocellular carcinoma. N Engl J Med 359, 378-390 https://doi.org/10.1056/NEJMoa0708857
- Cheng AL, Kang YK, Chen Z et al (2009) Efficacy and safety of sorafenib in patients in the Asia-Pacific region with advanced hepatocellular carcinoma: a phase III randomised, double-blind, placebo-controlled trial. Lancet Oncol 10, 25-34 https://doi.org/10.1016/S1470-2045(08)70285-7
- Rimassa L and Worns MA (2020) Navigating the new landscape of second-line treatment in advanced hepatocellular carcinoma. Liver International 40, 1800-1811 https://doi.org/10.1111/liv.14533
- Xia S, Pan Y, Liang Y, Xu J and Cai X (2020) The microenvironmental and metabolic aspects of sorafenib resistance in hepatocellular carcinoma. EBioMedicine 51, 102610 https://doi.org/10.1016/j.ebiom.2019.102610
- Huang A, Yang XR, Chung WY, Dennison AR and Zhou J (2020) Targeted therapy for hepatocellular carcinoma. Signal Transduct Target Ther 5, 146 https://doi.org/10.1038/s41392-020-00264-x
- Rahmani M, Davis EM, Crabtree TR et al (2007) The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress. Mol Cell Biol 27, 5499-5513 https://doi.org/10.1128/MCB.01080-06
- Zhou T, Lv X, Guo X et al (2015) RACK1 modulates apoptosis induced by sorafenib in HCC cells by interfering with the IRE1/XBP1 axis. Oncol Rep 33, 3006-3014 https://doi.org/10.3892/or.2015.3920
- Won JK, Yu SJ, Hwang CY et al (2017) Protein disulfide isomerase inhibition synergistically enhances the efficacy of sorafenib for hepatocellular carcinoma. Hepatology 66, 855-868 https://doi.org/10.1002/hep.29237
- Zhou B, Lu Q, Liu J, Fan L et al (2019) Melatonin increases the sensitivity of hepatocellular carcinoma to sorafenib through the PERK-ATF4-Beclin1 pathway. Int J Biol Sci 15, 1905-1920 https://doi.org/10.7150/ijbs.32550
- Hetz C and Papa FR (2018) The unfolded protein response and cell fate control. Mol Cell 69, 169-181 https://doi.org/10.1016/j.molcel.2017.06.017
- Shimizu S, Takehara T, Hikita H et al (2012) Inhibition of autophagy potentiates the antitumor effect of the multikinase inhibitor sorafenib in hepatocellular carcinoma. Int J Cancer 131, 548-557 https://doi.org/10.1002/ijc.26374
- Ma MKF, Lau EYT, Leung DHW et al (2017) Stearoyl-CoA desaturase regulates sorafenib resistance via modulation of ER stress-induced differentiation. J Hepatol 67, 979-990 https://doi.org/10.1016/j.jhep.2017.06.015
- Tanaka K, Yu HA, Yang S et al (2021) Targeting Aurora B kinase prevents and overcomes resistance to EGFR inhibitors in lung cancer by enhancing BIM- and PUMA-mediated apoptosis. Cancer Cell 39, 1245-1261 e1246 https://doi.org/10.1016/j.ccell.2021.07.006
- Harris IS, Endress JE, Coloff JL et al (2019) Deubiquitinases maintain protein homeostasis and survival of cancer cells upon glutathione depletion. Cell Metab 29, 1166-1181 e1166 https://doi.org/10.1016/j.cmet.2019.01.020
- Broux M, Prieto C, Demeyer S et al (2019) Suz12 inactivation cooperates with JAK3 mutant signaling in the development of T-cell acute lymphoblastic leukemia. Blood 134, 1323-1336
- Niles AL, Moravec RA and Riss TL (2009) In vitro viability and cytotoxicity testing and same-well multi-parametric combinations for high throughput screening. Curr Chem Genomics 3, 33-41 https://doi.org/10.2174/1875397300903010033
- Sun Y, Jiang X, Chen S and Price BD (2006) Inhibition of histone acetyltransferase activity by anacardic acid sensitizes tumor cells to ionizing radiation. FEBS Lett 580, 4353-4356 https://doi.org/10.1016/j.febslet.2006.06.092
- Ghizzoni M, Wu J, Gao T et al (2012) 6-alkylsalicylates are selective Tip60 inhibitors and target the acetyl-CoA binding site. Eur J Med Chem 47, 337-344 https://doi.org/10.1016/j.ejmech.2011.11.001
- Balasubramanyam K, Swaminathan V, Ranganathan A and Kundu TK (2003) Small molecule modulators of histone acetyltransferase p300. J Biol Chem 278, 19134-19140 https://doi.org/10.1074/jbc.M301580200
- Kusakabe Y, Chiba T, Oshima M et al (2021) EZH1/2 inhibition augments the anti-tumor effects of sorafenib in hepatocellular carcinoma. Sci Rep 11, 21396 https://doi.org/10.1038/s41598-021-00889-0
- Green AS, Maciel TT, Hospital MA et al (2015) Pim kinases modulate resistance to FLT3 tyrosine kinase inhibitors in FLT3-ITD acute myeloid leukemia. Sci Adv 1, e1500221 https://doi.org/10.1126/sciadv.1500221
- Yu H, Kim DJ, Choi HY et al (2021) Prospective pharmacological methodology for establishing and evaluating anti-cancer drug resistant cell lines. BMC Cancer 21, 1049 https://doi.org/10.1186/s12885-021-08784-7
- Chou TC (2010) Drug combination studies and their synergy quantification using the Chou-Talalay Method. Cancer Res 70, 440-446 https://doi.org/10.1158/0008-5472.CAN-09-1947
- Oslowski CM and Urano F (2011) Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol 490, 71-92 https://doi.org/10.1016/B978-0-12-385114-7.00004-0
- Lee CH, Han JH, Kim S et al (2020) Metformin ameliorates bile duct ligation-induced acute hepatic injury via regulation of ER stress. BMB Rep 53, 311-316 https://doi.org/10.5483/BMBRep.2020.53.6.169
- Oyadomari S and Mori M (2004) Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 11, 381-389 https://doi.org/10.1038/sj.cdd.4401373
- Novoa I, Zeng H, Harding HP and Ron D (2001) Feedback inhibition of the unfolded protein response by GADD34- mediated dephosphorylation of eIF2alpha. J Cell Biol 153, 1011-1022 https://doi.org/10.1083/jcb.153.5.1011
- Ogata M, Hino S, Saito A et al (2006) Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 26, 9220-9231 https://doi.org/10.1128/MCB.01453-06
- Hetz C, Chevet E and Oakes SA (2015) Proteostasis control by the unfolded protein response. Nat Cell Biol 17, 829-838 https://doi.org/10.1038/ncb3184
- Lee S, Jeong Y, Roe JS, Huh H, Paik SH and Song J (2021) Mitochondrial dysfunction induced by callyspongiolide promotes autophagy-dependent cell death. BMB Rep 54, 227-232 https://doi.org/10.5483/BMBRep.2021.54.4.037
- Kaizuka T, Morishita H, Hama Y et al (2016) An autophagic flux probe that releases an internal control. Mol Cell 64, 835-849 https://doi.org/10.1016/j.molcel.2016.09.037
- Shen D, Coleman J, Chan E et al (2011) Novel cell- and tissue-based assays for detecting misfolded and aggregated protein accumulation within aggresomes and inclusion bodies. Cell Biochem Biophys 60, 173-185 https://doi.org/10.1007/s12013-010-9138-4
- Wang C, Yu J, Huo L, Wang L, Feng W and Wang CC (2012) Human protein-disulfide isomerase is a redoxregulated Chaperone activated by oxidation of domain a'. J Biol Chem 287, 1139-1149 https://doi.org/10.1074/jbc.M111.303149
- Coriat R, Nicco C, Chereau C et al (2012) Sorafenib-induced hepatocellular carcinoma cell death depends on reactive oxygen species production in vitro and in vivo. Mol Cancer Ther 11, 2284-2293 https://doi.org/10.1158/1535-7163.MCT-12-0093
- Song Y, Kim JS, Kim SH et al (2018) Patient-derived multicellular tumor spheroids towards optimized treatment for patients with hepatocellular carcinoma. J Exp Clin Cancer Res 37, 109 https://doi.org/10.1186/s13046-018-0752-0
- Corazzari M, Gagliardi M, Fimia GM and Piacentini M (2017) Endoplasmic reticulum stress, unfolded protein response, and cancer cell fate. Front Oncol 7, 78 https://doi.org/10.3389/fonc.2017.00078
- Zou Y, Cong YS and Zhou J (2020) Implications of telomerase reverse transcriptase in tumor metastasis. BMB Rep 53, 458-465 https://doi.org/10.5483/BMBRep.2020.53.9.108
- Lin A, Giuliano CJ, Palladino A et al (2019) Off-target toxicity is a common mechanism of action of cancer drugs undergoing clinical trials. Sci Transl Med 11, eaaw8412 https://doi.org/10.1126/scitranslmed.aaw8412