Analysis of Human microRNA Expression Profiling During Diquat-Induced Renal Proximal Tubular Epithelial Cell Injury

References

• Magalhães N, Carvalho F, Dinis-Oliveira RJ. Human and experimental toxicology of diquat poisoning: toxicokinetics, mechanisms of toxicity, clinical features, and treatment. Hum Exp Toxicol. 2018;37(11):1131–1160. doi:10.1177/0960327118765330
   PubMed Web of Science ®Google Scholar
• Oreopoulos DG, McEvoy J. Diquat poisoning. Postgrad Med J. 1969;45(527):635–637. doi:10.1136/pgmj.45.527.635
   PubMed Web of Science ®Google Scholar
• Tsen CM, Yu CW, Chuang WC, et al. A simple approach for the ultrasensitive detection of paraquat residue in adzuki beans by surface-enhanced Raman scattering. Analyst. 2019;144(2):426–438. doi:10.1039/C8AN01845F
   PubMed Web of Science ®Google Scholar
• Wang X, Wang X, Zhu Y, et al. ADME/T-based strategies for paraquat detoxification: transporters and enzymes. Environ Pollut. 2021;291:118137. doi:10.1016/j.envpol.2021.118137
   PubMed Web of Science ®Google Scholar
• Yu G, Cui S, Jian T, et al. Diquat poisoning in a pregnant woman resulting in a miscarriage and maternal death. Clin Toxicol. 2021;59(12):1275–1277. doi:10.1080/15563650.2021.1905164
   PubMed Web of Science ®Google Scholar
• Rogers LK, Bates CM, Welty SE, et al. Diquat induces renal proximal tubule injury in glutathione reductase-deficient mice. Toxicol Appl Pharmacol. 2006;217(3):289–298. doi:10.1016/j.taap.2006.08.012
   PubMed Web of Science ®Google Scholar
• Lock A. The effect of paraquat and diquat on renal function in the rat. Toxicol Appl Pharmacol. 1979;48:321–336. doi:10.1016/0041-008X(79)90039-5
   Web of Science ®Google Scholar
• Chen Y, Chen Y, Zhang H, et al. Pterostilbene as a protective antioxidant attenuates diquat-induced liver injury and oxidative stress in 21-day-old broiler chickens. Poult Sci. 2020;99(6):3158–3167. doi:10.1016/j.psj.2020.01.021
   PubMed Web of Science ®Google Scholar
• Jones GM, Vale JA. Mechanisms of toxicity, clinical features, and management of diquat poisoning: a review. J Toxicol Clin Toxicol. 2000;38(2):123–128. doi:10.1081/CLT-100100926
   PubMed Web of Science ®Google Scholar
• Vanholder R, Colardyn F, De Reuck J, et al. Diquat intoxication. Am J Med. 1981;70(6):1267–1271. doi:10.1016/0002-9343(81)90836-6
   PubMed Web of Science ®Google Scholar
• Huang Y, Zhang R, Meng M, et al. High-dose diquat poisoning: a case report. J Int Med Res. 2021;49(6):1–10. doi:10.1177/03000605211026117
   Web of Science ®Google Scholar
• Nisar R, Hanson PS, He L, et al. Diquat causes caspase-independent cell death in SH-SY5Y cells by production of ROS independently of mitochondria. Arch Toxicol. 2015;89(10):1811–1825. doi:10.1007/s00204-015-1453-5
   PubMed Web of Science ®Google Scholar
• Park A, Koh HC. NF-kappaB/mTOR-mediated autophagy can regulate diquat-induced apoptosis. Arch Toxicol. 2019;93(5):1239–1253. doi:10.1007/s00204-019-02424-7
   PubMed Web of Science ®Google Scholar
• Choi SE, Park YS, Koh HC. NF-kappaB/p53-activated inflammatory response involves in diquat-induced mitochondrial dysfunction and apoptosis. Environ Toxicol. 2018;33(10):1005–1018. doi:10.1002/tox.22552
   PubMed Web of Science ®Google Scholar
• Gupta S, Silveira DA, Mombach JCM. Towards DNA-damage induced autophagy: a Boolean model of p53-induced cell fate mechanisms. DNA Repair. 2020;96:102971. doi:10.1016/j.dnarep.2020.102971
   PubMed Web of Science ®Google Scholar
• Huang J, Liu W, Doycheva DM, et al. Ghrelin attenuates oxidative stress and neuronal apoptosis via GHSR-1alpha/AMPK/Sirt1/PGC-1alpha/UCP2 pathway in a rat model of neonatal HIE. Free Radic Biol Med. 2019;141:322–337. doi:10.1016/j.freeradbiomed.2019.07.001
   PubMed Web of Science ®Google Scholar
• Jahan N, Chowdhury A, Li T, et al. Neferine improves oxidative stress and apoptosis in benign prostate hyperplasia via Nrf2-ARE pathway. Redox Rep. 2021;26(1):1–9. doi:10.1080/13510002.2021.1871814
   PubMed Web of Science ®Google Scholar
• Bartel DP. MicroRNAs: genomics, biogenesis, mechanism, and function. Cell. 2004;116:281–297. doi:10.1016/S0092-8674(04)00045-5
   PubMed Web of Science ®Google Scholar
• Michlewski G, Cáceres JF. Post-transcriptional control of miRNA biogenesis. RNA. 2019;25(1):1–16. doi:10.1261/rna.068692.118
   PubMed Web of Science ®Google Scholar
• Han S, Lin F, Ruan Y, et al. miR-132-3p promotes the cisplatin-induced apoptosis and inflammatory response of renal tubular epithelial cells by targeting SIRT1 via the NF-kappaB pathway. Int Immunopharmacol. 2021;99:108022. doi:10.1016/j.intimp.2021.108022
   PubMed Web of Science ®Google Scholar
• Jing H, Zhang Q, Li S, et al. Pb exposure triggers MAPK-dependent inflammation by activating oxidative stress and miRNA-155 expression in carp head kidney. Fish Shellfish Immunol. 2020;106:219–227. doi:10.1016/j.fsi.2020.08.015
   PubMed Web of Science ®Google Scholar
• Wu J, Zheng C, Wang Y, et al. LncRNA APCDD1L-AS1 induces icotinib resistance by inhibition of EGFR autophagic degradation via the miR-1322/miR-1972/miR-324-3p-SIRT5 axis in lung adenocarcinoma. Biomark Res. 2021;9(1):9. doi:10.1186/s40364-021-00262-3
   PubMed Web of Science ®Google Scholar
• Zhan Y, Guo Z, Zheng F, et al. Reactive oxygen species regulate miR-17-5p expression via DNA methylation in paraquat-induced nerve cell damage. Environ Toxicol. 2020;35(12):1364–1373. doi:10.1002/tox.23001
   PubMed Web of Science ®Google Scholar
• Ryan MJ, Johnson G, Kirk J, et al. HK-2: an immortalized proximal tubule epithelial cell line from normal adult human kidney. Kidney Int. 1994;45:48–57. doi:10.1038/ki.1994.6
   PubMed Web of Science ®Google Scholar
• Zhang JQ, Gao BW, Wang J, et al. Chronic exposure to diquat causes reproductive toxicity in female mice. PLoS One. 2016;11(1):e0147075. doi:10.1371/journal.pone.0147075
   PubMed Web of Science ®Google Scholar
• Chen J, Su Y, Lin R, et al. Effects of acute diquat poisoning on liver mitochondrial apoptosis and autophagy in ducks. Front Vet Sci. 2021;8:727–766. doi:10.3389/fvets.2021.727766
   Web of Science ®Google Scholar
• Hao L, Cheng Y, Su W, et al. Pediococcus pentosaceus ZJUAF-4 relieves oxidative stress and restores the gut microbiota in diquat-induced intestinal injury. Appl Microbiol Biotechnol. 2021;105(4):1657–1668. doi:10.1007/s00253-021-11111-6
   PubMed Web of Science ®Google Scholar
• Liang H, Ran Q, Jang YC, et al. Glutathione peroxidase 4 differentially regulates the release of apoptogenic proteins from mitochondria. Free Radic Biol Med. 2009;47(3):312–320. doi:10.1016/j.freeradbiomed.2009.05.012
   PubMed Web of Science ®Google Scholar
• Wang B, Mao JH, Wang BY, et al. Exosomal miR-1910-3p promotes proliferation, metastasis, and autophagy of breast cancer cells by targeting MTMR3 and activating the NF-kappaB signaling pathway. Cancer Lett. 2020;489:87–99. doi:10.1016/j.canlet.2020.05.038
   PubMed Web of Science ®Google Scholar
• Lu Q, Wu R, Zhao M, et al. miRNAs as therapeutic targets in inflammatory disease. Trends Pharmacol Sci. 2019;40(11):853–865. doi:10.1016/j.tips.2019.09.007
   PubMed Web of Science ®Google Scholar
• Liu F, Zhang Q, Liang Y. MicroRNA-598 acts as an inhibitor in retinoblastoma through targeting E2F1 and regulating AKT pathway. J Cell Biochem. 2020;121(3):2294–2302. doi:10.1002/jcb.29453
   PubMed Web of Science ®Google Scholar
• Wang S, Qiu J, Wang L, et al. Long non-coding RNA LINC01207 promotes prostate cancer progression by downregulating microRNA-1972 and upregulating LIM and SH3 protein 1. IUBMB Life. 2020;72(9):1960–1975. doi:10.1002/iub.2327
   PubMed Web of Science ®Google Scholar
• Li S, Lu G, Wang D, et al. MicroRNA-4443 regulates monocyte activation by targeting tumor necrosis factor receptor associated factor 4 in stroke-induced immunosuppression. Eur J Neurol. 2020;27(8):1625–1637. doi:10.1111/ene.14282
   PubMed Web of Science ®Google Scholar
• Qi Y, Zhou Y, Chen X, et al. MicroRNA-4443 causes CD4+ T cells dysfunction by targeting TNFR-associated factor 4 in graves’ disease. Front Immunol. 2017;8:1440. doi:10.3389/fimmu.2017.01440
   PubMed Web of Science ®Google Scholar
• Zhang C, Wang C, Tang S, et al. TNFR1/TNF-α and mitochondria interrelated signaling pathway mediates quinocetone-induced apoptosis in HepG2 cells. Food Chem Toxicol. 2013;62:825–838. doi:10.1016/j.fct.2013.10.022
   PubMed Web of Science ®Google Scholar
• Strasser A, Jost PJ, Nagata S. The many roles of FAS receptor signaling in the immune system. Immunity. 2009;30(2):180–192. doi:10.1016/j.immuni.2009.01.001
   PubMed Web of Science ®Google Scholar
• Li X, Li F, Zhang X, et al. Caspase-8 auto-cleavage regulates programmed cell death and collaborates with RIPK3/MLKL to prevent lymphopenia. Cell Death Differ. 2022;29(8):1500–1512. doi:10.1038/s41418-022-00938-9
   PubMed Web of Science ®Google Scholar
• Miano M, Cappelli E, Pezzulla A, et al. FAS-mediated apoptosis impairment in patients with Alps/Alps-like phenotype carrying variants on CASP10 gene. Br J Haematol. 2019;187(4):502–508. doi:10.1111/bjh.16098
   PubMed Web of Science ®Google Scholar
• McGrath EE, Marriott HM, Lawrie A, et al. TNF-related apoptosis-inducing ligand (TRAIL) regulates inflammatory neutrophil apoptosis and enhances resolution of inflammation. J Leukoc Biol. 2011;90(5):855–865. doi:10.1189/jlb.0211062
   PubMed Web of Science ®Google Scholar
• Tan S, Liu X, Chen L, et al. Fas/FasL mediates NF-κBp65/PUMA-modulated hepatocytes apoptosis via autophagy to drive liver fibrosis. Cell Death Dis. 2021;12(5):474. doi:10.1038/s41419-021-03749-x
   PubMed Web of Science ®Google Scholar
• Liao X, Wang X, Gu Y, et al. Involvement of death receptor signaling in mechanical stretch-induced cardiomyocyte apoptosis. Life Sci. 2005;77(2):160–174. doi:10.1016/j.lfs.2004.11.029
   PubMed Web of Science ®Google Scholar
• Fritsch M, Günther SD, Schwarzer R, et al. Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis. Nature. 2019;575(7784):683–687. doi:10.1038/s41586-019-1770-6
   PubMed Web of Science ®Google Scholar
• Saggioro FP, Neder L, Stávale JN, et al. Fas, FasL, and cleaved caspases 8 and 3 in glioblastomas: a tissue microarray-based study. Pathol Res Pract. 2014;210(5):267–273. doi:10.1016/j.prp.2013.12.012
   PubMed Web of Science ®Google Scholar
• Gu L, Surolia R, Larson-Casey JL, et al. Targeting Cpt1a-Bcl-2 interaction modulates apoptosis resistance and fibrotic remodeling. Cell Death Differ. 2022;29(1):118–132. doi:10.1038/s41418-021-00840-w
   PubMed Web of Science ®Google Scholar
• Hu H, Sun SC. Ubiquitin signaling in immune responses. Cell Res. 2016;26(4):457–483. doi:10.1038/cr.2016.40
   PubMed Web of Science ®Google Scholar
• Cruz Walma DA, Chen Z, Bullock AN, et al. Ubiquitin ligases: guardians of mammalian development. Nat Rev Mol Cell Biol. 2022;23(5):350–367. doi:10.1038/s41580-021-00448-5
   PubMed Web of Science ®Google Scholar
• Narayanan S, Cai CY, Assaraf YG, et al. Targeting the ubiquitin-proteasome pathway to overcome anti-cancer drug resistance. Drug Resist Updat. 2020;48:100663. doi:10.1016/j.drup.2019.100663
   PubMed Web of Science ®Google Scholar