Research progress of oxidative stress in the sensitivity of chemoradiotherapy for gliomas

Abstract

Abstract:

Following oxidative stress, reactive oxygen species are produced and accumulate in glioma cells in large quantities, and to avoid the occurrence of cellular dysfunction, glioma cells can respond adaptively in the biological processes of DNA damage repair, lipid peroxidation and protein modification to produce radiotherapy resistance. The expression of nuclear factor erythroid 2-related factor 2, solute carrier family 7 member 11, glutathione and microRNA, as key regulatory molecules, can regulate reactive oxygen species levels, alter glioma oxidative stress status, and affect radiochemotherapy sensitivity. Further study on the relationship between oxidative stress and sensitivity to radiotherapy and chemotherapy of glioma can provide theoretical basis for precise treatment of glioma.

Key words:Glioma,Oxidative stress,Chemoradiotherapy,Radiation tolerance,Reactive oxygen species

Xiao Nan, Sun Pengfei. Research progress of oxidative stress in the sensitivity of chemoradiotherapy for gliomas[J]. Journal of International Oncology, 2022, 49(6): 357-361.

References37

[1]	Jiang T, Nam DH, Ram Z, et al. Clinical practice guidelines for the management of adult diffuse gliomas[J]. Cancer Lett, 2021, 499: 60-72. DOI: 10.1016/j.canlet.2020.10.050. doi:10.1016/j.canlet.2020.10.050pmid:33166616
[2]	Sies H. Oxidative stress: concept and some practical aspects[J]. Antioxidants (Basel), 2020, 9(9): 852. DOI: 10.3390/antiox9090852. doi:10.3390/antiox9090852
[3]	Moloney JN, Cotter TG. ROS signalling in the biology of cancer[J]. Semin Cell Dev Biol, 2018, 80: 50-64. DOI: 10.1016/j.semcdb.2017.05.023. doi:10.1016/j.semcdb.2017.05.023
[4]	Olivier C, Oliver L, Lalier L, et al. Drug resistance in glioblastoma: the two faces of oxidative stress[J]. Front Mol Biosci, 2020, 7: 620677. DOI: 10.3389/fmolb.2020.620677. doi:10.3389/fmolb.2020.620677
[5]	Srinivas US, Tan BWQ, Vellayappan BA, et al. ROS and the DNA damage response in cancer[J]. Redox Biol, 2019, 25: 101084. DOI: 10.1016/j.redox.2018.101084. doi:10.1016/j.redox.2018.101084
[6]	Venere M, Hamerlik P, Wu Q, et al. Therapeutic targeting of constitutive PARP activation compromises stem cell phenotype and survival of glioblastoma-initiating cells[J]. Cell Death Differ, 2014, 21(2): 258-269. DOI: 10.1038/cdd.2013.136. doi:10.1038/cdd.2013.136pmid:24121277
[7]	Sim HW, Galanis E, Khasraw M. PARP inhibitors in glioma: a review of therapeutic opportunities[J]. Cancers (Basel), 2022, 14(4): 1003. DOI: 10.3390/cancers14041003. doi:10.3390/cancers14041003
[8]	Ghorai A, Mahaddalkar T, Thorat R, et al. Sustained inhibition of PARP-1 activity delays glioblastoma recurrence by enhancing radiation-induced senescence[J]. Cancer Lett, 2020, 490: 44-53. DOI: 10.1016/j.canlet.2020.06.023. doi:S0304-3835(20)30353-0pmid:32645394
[9]	Su LJ, Zhang JH, Gomez H, et al. Reactive oxygen species-induced lipid peroxidation in apoptosis, autophagy, and ferroptosis[J]. Oxid Med Cell Longev, 2019, 2019: 5080843. DOI: 10.1155/2019/5080843. doi:10.1155/2019/5080843
[10]	Stockwell BR, Friedmann Angeli JP, Bayir H, et al. Ferroptosis: a regulated cell death nexus linking metabolism, redox biology, and disease[J]. Cell, 2017, 171(2): 273-285. DOI: 10.1016/j.cell.2017.09.021. doi:S0092-8674(17)31070-Xpmid:28985560
[11]	Koppula P, Zhuang L, Gan B. Cystine transporter SLC7A11/xCT in cancer: ferroptosis, nutrient dependency, and cancer therapy[J]. Protein Cell, 2021, 12(8): 599-620. DOI: 10.1007/s13238-020-00789-5. doi:10.1007/s13238-020-00789-5
[12]	Cheng J, Fan YQ, Liu BH, et al. ACSL 4 suppresses glioma cells proliferation via activating ferroptosis[J]. Oncol Rep, 2020, 43(1): 147-158. DOI: 10.3892/or.2019.7419. doi:10.3892/or.2019.7419pmid:31789401
[13]	Magtanong L, Ko PJ, To M, et al. Exogenous monounsaturated fatty acids promote a ferroptosis-resistant cell state[J]. Cell Chem Biol, 2019, 26(3): 420-432. e9. DOI: 10.1016/j.chembiol.2018.11.016. doi:S2451-9456(18)30438-0pmid:30686757
[14]	Ye LF, Chaudhary KR, Zandkarimi F, et al. Radiation-induced lipid peroxidation triggers ferroptosis and synergizes with ferroptosis inducers[J]. ACS Chem Biol, 2020, 15(2): 469-484. DOI: 10.1021/acschembio.9b00939. doi:10.1021/acschembio.9b00939
[15]	Alnajjar KS, Sweasy JB. A new perspective on oxidation of DNA repair proteins and cancer[J]. DNA Repair (Amst), 2019, 76: 60-69. DOI: 10.1016/j.dnarep.2019.02.006. doi:10.1016/j.dnarep.2019.02.006
[16]	Hauck AK, Huang Y, Hertzel AV, et al. Adipose oxidative stress and protein carbonylation[J]. J Biol Chem, 2019, 294(4): 1083-1088. DOI: 10.1074/jbc.R118.003214. doi:10.1074/jbc.R118.003214pmid:30563836
[17]	Moldogazieva NT, Lutsenko SV, Terentiev AA. Reactive oxygen and nitrogen species-induced protein modifications: implication in carcinogenesis and anticancer therapy[J]. Cancer Res, 2018, 78(21): 6040-6047. DOI: 10.1158/0008-5472.CAN-18-0980. doi:10.1158/0008-5472.CAN-18-0980pmid:30327380
[18]	Vandenberk L, Garg AD, Verschuere T, et al. Irradiation of necrotic cancer cells, employed for pulsing dendritic cells (DCs), potentiates DC vaccine-induced antitumor immunity against high-grade glioma[J]. Oncoimmunology, 2015, 5(2): e1083669. DOI: 10.1080/2162402X.2015.1083669. doi:10.1080/2162402X.2015.1083669
[19]	张永丽, 张若佳, 范焕彩, 等. TXNDC5-Prx2途径对前列腺癌细胞耐药性的调控[J]. 国际肿瘤学杂志, 2021, 48(8): 473-478. DOI: 10.3760/cma.j.cn371439-20210324-00090. doi:10.3760/cma.j.cn371439-20210324-00090
[20]	Yao A, Storr SJ, Al-Hadyan K, et al. Thioredoxin system protein expression is associated with poor clinical outcome in adult and paediatric gliomas and medulloblastomas[J]. Mol Neurobiol, 2020, 57(7): 2889-2901. DOI: 10.1007/s12035-020-01928-z. doi:10.1007/s12035-020-01928-z
[21]	Jovanović M, Dragoj M, Zhukovsky D, et al. Novel TrxR1 inhibitors show potential for glioma treatment by suppressing the invasion and sensitizing glioma cells to chemotherapy[J]. Front Mol Biosci, 2020, 7: 586146. DOI: 10.3389/fmolb.2020.586146. doi:10.3389/fmolb.2020.586146
[22]	Burić SS, Podolski-Renić A, Dinić J, et al. Modulation of antioxidant potential with coenzyme Q10 suppressed invasion of temozolomide-resistant rat glioma in vitro and in vivo[J]. Oxid Med Cell Longev, 2019, 2019: 3061607. DOI: 10.1155/2019/3061607. doi:10.1155/2019/3061607
[23]	Frontiñán-Rubio J, Santiago-Mora RM, Nieva-Velasco CM, et al. Regulation of the oxidative balance with coenzyme Q10 sensitizes human glioblastoma cells to radiation and temozolomide[J]. Radiother Oncol, 2018, 128(2): 236-244. DOI: 10.1016/j.radonc.2018.04.033. doi:S0167-8140(18)30240-8pmid:29784452
[24]	Zhu Z, Du S, Du Y, et al. Glutathione reductase mediates drug resistance in glioblastoma cells by regulating redox homeostasis[J]. J Neurochem, 2018, 144(1): 93-104. DOI: 10.1111/jnc.14250. doi:10.1111/jnc.14250
[25]	Zimta AA, Cenariu D, Irimie A, et al. The role of Nrf2 activity in cancer development and progression[J]. Cancers (Basel), 2019, 11(11): 1755. DOI: 10.3390/cancers11111755. doi:10.3390/cancers11111755
[26]	Cockfield JA, Schafer ZT. Antioxidant defenses: a context-specific vulnerability of cancer cells[J]. Cancers (Basel), 2019, 11(8): 1208. DOI: 10.3390/cancers11081208. doi:10.3390/cancers11081208
[27]	Wang J, Wang H, Sun K, et al. Chrysin suppresses proliferation, migration, and invasion in glioblastoma cell lines via mediating the ERK/Nrf2 signaling pathway[J]. Drug Des Devel Ther, 2018, 12: 721-733. DOI: 10.2147/DDDT.S160020. doi:10.2147/DDDT.S160020
[28]	Liu Y, Lu Y, Celiku O, et al. Targeting IDH1-mutated malignancies with NRF2 blockade[J]. J Natl Cancer Inst, 2019, 111(10): 1033-1041. DOI: 10.1093/jnci/djy230. doi:10.1093/jnci/djy230
[29]	Koppula P, Zhang Y, Zhuang L, et al. Amino acid transporter SLC7A11/xCT at the crossroads of regulating redox homeostasis and nutrient dependency of cancer[J]. Cancer Commun (Lond), 2018, 38(1): 12. DOI: 10.1186/s40880-018-0288-x. doi:10.1186/s40880-018-0288-x
[30]	Dąbrowska K, Skowrońska K, Popek M, et al. The role of Nrf2 transcription factor and Sp1-Nrf2 protein complex in glutamine transporter SN1 regulation in mouse cortical astrocytes exposed to ammonia[J]. Int J Mol Sci, 2021, 22(20): 11233. DOI: 10.3390/ijms222011233. doi:10.3390/ijms222011233
[31]	Yu D, Liu Y, Zhou Y, et al. Triptolide suppresses IDH1-mutated malignancy via Nrf2-driven glutathione metabolism[J]. Proc Natl Acad Sci U S A, 2020, 117(18): 9964-9972. DOI: 10.1073/pnas.1913633117. doi:10.1073/pnas.1913633117
[32]	Lei G, Zhang Y, Koppula P, et al. The role of ferroptosis in ionizing radiation-induced cell death and tumor suppression[J]. Cell Res, 2020, 30(2): 146-162. DOI: 10.1038/s41422-019-0263-3. doi:10.1038/s41422-019-0263-3
[33]	Garcia CG, Kahn SA, Geraldo LHM, et al. combination therapy with sulfasalazine and valproic acid promotes human glioblastoma cell death through imbalance of the intracellular oxidative response[J]. Mol Neurobiol, 2018, 55(8): 6816-6833. DOI: 10.1007/s12035-018-0895-1. doi:10.1007/s12035-018-0895-1
[34]	Toraih EA, El-Wazir A, Abdallah HY, et al. Deregulated microRNA signature following glioblastoma irradiation[J]. Cancer Control, 2019, 26(1): 1073274819847226. DOI: 10.1177/1073274819847226. doi:10.1177/1073274819847226
[35]	Xu Z, Zeng X, Li M, et al. MicroRNA-383 promotes reactive oxygen species-induced autophagy via downregulating peroxiredoxin 3 in human glioma U87 cells[J]. Exp Ther Med, 2021, 21(5): 439. DOI: 10.3892/etm.2021.9870. doi:10.3892/etm.2021.9870
[36]	Yang W, Shen Y, Wei J, et al. MicroRNA-153/Nrf-2/GPx1 pathway regulates radiosensitivity and stemness of glioma stem cells via reactive oxygen species[J]. Oncotarget, 2015, 6(26): 22006-22027. DOI: 10.18632/oncotarget.4292. doi:10.18632/oncotarget.4292pmid:26124081
[37]	Chang M, Qiao L, Li B, et al. Suppression of SIRT6 by miR-33a facilitates tumor growth of glioma through apoptosis and oxidative stress resistance[J]. Oncol Rep, 2017, 38(2): 1251-1258. DOI: 10.3892/or.2017.5780. doi:10.3892/or.2017.5780