Association of changes in expression of HDAC and SIRT genes after drug treatment with cancer cell line sensitivity to kinase inhibitors

References

• Seto E, Yoshida M. Erasers of histone acetylation: the histone deacetylase enzymes. Cold Spring Harb Perspect Biol. 2014;6(4):a018713. doi: 10.1101/cshperspect.a018713
   PubMed Web of Science ®Google Scholar
• Witt O, Deubzer HE, Milde T, et al. HDAC family: what are the cancer relevant targets? Cancer Lett. 2009;277(1):8–29. doi: 10.1016/j.canlet.2008.08.016
   PubMed Web of Science ®Google Scholar
• Roche J, Bertrand P. Inside HDACs with more selective HDAC inhibitors. Eur J Med Chem. 2016;121:451–483. doi: 10.1016/j.ejmech.2016.05.047
   PubMed Web of Science ®Google Scholar
• Milazzo G, Mercatelli D, Di Muzio G, Triboli L, De Rosa P, Perini G, Giorgi FM. Histone deacetylases (HDACs): evolution, specificity, role in transcriptional complexes, and pharmacological actionability. Genes (Basel). 2020;11(5):556. doi: 10.3390/genes11050556
   PubMed Web of Science ®Google Scholar
• Manna S, Mishra J, Baral T, et al. Epigenetic signaling and crosstalk in regulation of gene expression and disease progression. Epigenomics. 2023;15(14):723–740. doi: 10.2217/epi-2023-0235
   PubMed Web of Science ®Google Scholar
• Parbin S, Kar S, Shilpi A, et al. Histone deacetylases: a saga of perturbed acetylation homeostasis in cancer. J Histochem Cytochem. 2014;62(1):11–33. doi: 10.1369/0022155413506582
   PubMed Web of Science ®Google Scholar
• Kyrylenko S, Kyrylenko O, Suuronen T, et al. Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases. Cell Mol Life Sci. 2003;60(9):1990–7. doi: 10.1007/s00018-003-3090-z
   PubMed Web of Science ®Google Scholar
• Peixoto P, Castronovo V, Matheus N, et al. HDAC5 is required for maintenance of pericentric heterochromatin, and controls cell-cycle progression and survival of human cancer cells. Cell Death Differ. 2012;19(7):1239–1252. doi: 10.1038/cdd.2012.3
   PubMed Web of Science ®Google Scholar
• Curry AM, White DS, Donu D, et al. Human sirtuin regulators: the “success” stories. Front Physiol. 2021;12:752117. doi: 10.3389/fphys.2021.752117
   PubMed Web of Science ®Google Scholar
• Fortuny L, Sebastian C. Sirtuins as metabolic regulators of immune cells phenotype and function. Genes (Basel). 2021;12(11):1698. doi: 10.3390/genes12111698
   PubMed Web of Science ®Google Scholar
• Poralla L, Stroh T, Erben U, et al. Histone deacetylase 5 regulates the inflammatory response of macrophages. J Cell Mol Med. 2015;19(9):2162–71. doi: 10.1111/jcmm.12595
   PubMed Web of Science ®Google Scholar
• Kumar J, Kumar S. Sirtuin1 in vascular endothelial function, an overview. Epigenetics. 2022;17(9):953–969. doi: 10.1080/15592294.2021.1975936
   PubMed Web of Science ®Google Scholar
• Zheng M, Hu C, Wu M, et al. Emerging role of SIRT2 in non-small cell lung cancer (review). Oncol Lett. 2021;22(4):731. doi: 10.3892/ol.2021.12992
   PubMed Web of Science ®Google Scholar
• Fajardo-Orduna GR, Ledesma-Martinez E, Aguiniga-Sanchez I, et al. Role of SIRT1 in chemoresistant leukemia. Int J Mol Sci. 2023;24(19):14470. doi: 10.3390/ijms241914470
   PubMed Web of Science ®Google Scholar
• Bronner C. Control of DNMT1 abundance in epigenetic inheritance by acetylation, ubiquitylation, and the histone code. Sci Signal. 2011;4(157):pe3. doi: 10.1126/scisignal.2001764
   PubMed Web of Science ®Google Scholar
• Fuks F, Burgers WA, Brehm A, et al. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat Genet. 2000;24(1):88–91. doi: 10.1038/71750
   PubMed Web of Science ®Google Scholar
• Patra SK, Patra A, Dahiya R. Histone deacetylase and DNA methyltransferase in human prostate cancer. Biochem Biophys Res Commun. 2001;287(3):705–713. doi: 10.1006/bbrc.2001.5639
   PubMed Web of Science ®Google Scholar
• Huang L. Targeting histone deacetylases for the treatment of cancer and inflammatory diseases. J Cell Physiol. 2006;209(3):611–6. doi: 10.1002/jcp.20781
   PubMed Web of Science ®Google Scholar
• Vleeshouwer-Neumann T, Phelps M, Bammler TK, et al. Histone deacetylase inhibitors antagonize distinct pathways to suppress tumorigenesis of embryonal rhabdomyosarcoma. PLoS One. 2015;10(12):e0144320. doi: 10.1371/journal.pone.0144320
   PubMed Web of Science ®Google Scholar
• Kar S, Niharika, Roy A, et al. Overexpression of SOX2 gene by histone modifications: SOX2 enhances human prostate and breast cancer progression by prevention of apoptosis and enhancing cell proliferation. Oncology (Basel). 2023;101(9):591–608. doi: 10.1159/000531195
   PubMed Web of Science ®Google Scholar
• Azad N, Zahnow CA, Rudin CM, et al. The future of epigenetic therapy in solid tumours - lessons from the past. Nat Rev Clin Oncol. 2013;10(5):256–266. doi: 10.1038/nrclinonc.2013.42
   PubMed Web of Science ®Google Scholar
• Oltra SS, Cejalvo JM, Tormo E, et al. HDAC5 inhibitors as a potential treatment in breast cancer affecting very young women. Cancers (Basel). 2020;12(2):412. doi: 10.3390/cancers12020412
   PubMed Web of Science ®Google Scholar
• Li A, Liu Z, Li M, et al. HDAC5, a potential therapeutic target and prognostic biomarker, promotes proliferation, invasion and migration in human breast cancer. Oncotarget. 2016;7(25):37966–37978. doi: 10.18632/oncotarget.9274
   PubMedGoogle Scholar
• Liu Q, Zheng JM, Chen JK, et al. Histone deacetylase 5 promotes the proliferation of glioma cells by upregulation of notch 1. Mol Med Rep. 2014;10(4):2045–50. doi: 10.3892/mmr.2014.2395
   PubMed Web of Science ®Google Scholar
• Li Y, Seto E. HDACs and HDAC inhibitors in cancer development and therapy. Cold Spring Harb Perspect Med. 2016;6(10):a026831. doi: 10.1101/cshperspect.a026831
   PubMed Web of Science ®Google Scholar
• Hanigan CL, van Engeland M, De Bruine AP, et al. An inactivating mutation in HDAC2 leads to dysregulation of apoptosis mediated by APAF1. Gastroenterology. 2008;135(5):1654–1664. doi: 10.1053/j.gastro.2008.07.078
   PubMed Web of Science ®Google Scholar
• Kiweler N, Schwarz H, Nguyen A, et al. The epigenetic modifier HDAC2 and the checkpoint kinase ATM determine the responses of microsatellite instable colorectal cancer cells to 5-fluorouracil. Cell Biol Toxicol. 2023;39(5):2401–2419. doi: 10.1007/s10565-022-09731-3
   PubMed Web of Science ®Google Scholar
• Zhu P, Martin E, Mengwasser J, et al. Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis. Cancer Cell. 2004;5(5):455–463. doi: 10.1016/S1535-6108(04)00114-X
   PubMed Web of Science ®Google Scholar
• Keshelava N, Davicioni E, Wan Z, et al. Histone deacetylase 1 gene expression and sensitization of multidrug-resistant neuroblastoma cell lines to cytotoxic agents by depsipeptide. J Natl Cancer Inst. 2007;99(14):1107–19. doi: 10.1093/jnci/djm044
   PubMedGoogle Scholar
• Bandyopadhyay D, Mishra A, Medrano EE. Overexpression of histone deacetylase 1 confers resistance to sodium butyrate-mediated apoptosis in melanoma cells through a p53-mediated pathway. Cancer Res. 2004;64(21):7706–7710. doi: 10.1158/0008-5472.CAN-03-3897
   PubMed Web of Science ®Google Scholar
• Karwaciak I, Salkowska A, Karas K, et al. SIRT2 contributes to the resistance of melanoma cells to the multikinase inhibitor dasatinib. Cancers (Basel). 2019;11(5):673. doi: 10.3390/cancers11050673
   PubMed Web of Science ®Google Scholar
• Ceballos MP, Quiroga AD, Palma NF. Role of sirtuins in hepatocellular carcinoma progression and multidrug resistance: mechanistical and pharmacological perspectives. Biochem Pharmacol. 2023;212:115573. doi: 10.1016/j.bcp.2023.115573
   PubMed Web of Science ®Google Scholar
• Monks A, Zhao Y, Hose C, et al. The NCI transcriptional pharmacodynamics workbench: a tool to examine dynamic expression profiling of therapeutic response in the NCI-60 cell line panel. Cancer Res. 2018;78(24):6807–6817. doi: 10.1158/0008-5472.CAN-18-0989
   PubMed Web of Science ®Google Scholar
• Krushkal J, Zhao Y, Hose C, et al. Concerted changes in transcriptional regulation of genes involved in DNA methylation, demethylation, and folate-mediated one-carbon metabolism pathways in the NCI-60 cancer cell line panel in response to cancer drug treatment. Clin Epigenetics. 2016;8(1):73. doi: 10.1186/s13148-016-0240-3
   PubMedGoogle Scholar
• Krushkal J, Zhao Y, Hose C, et al. Longitudinal transcriptional response of glycosylation-related genes, regulators, and targets in cancer cell lines treated with 11 antitumor agents. Cancer Inform. 2017;16. doi: 10.1177/1176935117747259
   PubMedGoogle Scholar
• Pleyer L, Greil R. Digging deep into “dirty” drugs – modulation of the methylation machinery. Drug Metab Rev. 2015;47(2):252–279. doi: 10.3109/03602532.2014.995379
   PubMed Web of Science ®Google Scholar
• Lamb J, Crawford ED, Peck D, et al. The connectivity map: using gene-expression signatures to connect small molecules, genes, and disease. Science. 2006;313(5795):1929–35. doi: 10.1126/science.1132939
   PubMed Web of Science ®Google Scholar
• Holbeck SL, Collins JM, Doroshow JH. Analysis of Food and Drug Administration-approved anticancer agents in the NCI60 panel of human tumor cell lines. Mol Cancer Ther. 2010;9(5):1451–1460. doi: 10.1158/1535-7163.MCT-10-0106
   PubMed Web of Science ®Google Scholar
• Irizarry RA, Hobbs B, Collin F, et al. Exploration, normalization, and summaries of high density oligonucleotide array probe level data. Biostatistics. 2003;4(2):249–264. doi: 10.1093/biostatistics/4.2.249
   PubMed Web of Science ®Google Scholar
• Benjamini Y, Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J R Statist Soc. 1995;57(1):289–300. doi: 10.1111/j.2517-6161.1995.tb02031.x
   Google Scholar
• Zhang P, Palmisano A, Kumar R, et al. TPWshiny: an interactive R/Shiny app to explore cell line transcriptional responses to anti-cancer drugs. Bioinformatics. 2022;38(2):570–572. doi: 10.1093/bioinformatics/btab619
   PubMed Web of Science ®Google Scholar
• Zhu X, Liu X, Cheng Z, et al. Quantitative analysis of global proteome and lysine acetylome reveal the differential impacts of VPA and SAHA on HL60 cells. Sci Rep. 2016;6(1):19926. doi: 10.1038/srep19926
   PubMedGoogle Scholar
• Subramanian K, Rauniyar N, Lavallee-Adam M, et al. Quantitative analysis of the proteome response to the histone deacetylase inhibitor (HDACi) vorinostat in Niemann-Pick type C1 disease. Mol & Cell Proteomics. 2017;16(11):1938–1957. doi: 10.1074/mcp.M116.064949
   PubMed Web of Science ®Google Scholar
• Asmussen J, Lasater EA, Tajon C, et al. MEK-dependent negative feedback underlies BCR-ABL-mediated oncogene addiction. Cancer Discov. 2014;4(2):200–215. doi: 10.1158/2159-8290.CD-13-0235
   PubMed Web of Science ®Google Scholar
• Peng S, Sen B, Mazumdar T, et al. Dasatinib induces DNA damage and activates DNA repair pathways leading to senescence in non-small cell lung cancer cell lines with kinase-inactivating BRAF mutations. Oncotarget. 2016;7(1):565–79. doi: 10.18632/oncotarget.6376
   PubMedGoogle Scholar
• Malone CF, Emerson C, Ingraham R, et al. mTOR and HDAC inhibitors converge on the TXNIP/thioredoxin pathway to cause catastrophic oxidative stress and regression of RAS-driven tumors. Cancer Discov. 2017;7(12):1450–1463. doi: 10.1158/2159-8290.CD-17-0177
   PubMed Web of Science ®Google Scholar
• Bolden JE, Shi W, Jankowski K, et al. HDAC inhibitors induce tumor-cell-selective pro-apoptotic transcriptional responses. Cell Death Dis. 2013;4(2):e519. doi: 10.1038/cddis.2013.9
   PubMedGoogle Scholar
• Holbeck SL, Camalier R, Crowell JA, et al. The National Cancer Institute ALMANAC: a comprehensive screening resource for the detection of anticancer drug pairs with enhanced therapeutic activity. Cancer Res. 2017;77(13):3564–3576. doi: 10.1158/0008-5472.CAN-17-0489
   PubMed Web of Science ®Google Scholar
• Abaan OD, Polley EC, Davis SR, et al. The exomes of the NCI-60 panel: a genomic resource for cancer biology and systems pharmacology. Cancer Res. 2013;73(14):4372–82. doi: 10.1158/0008-5472.CAN-12-3342
   PubMed Web of Science ®Google Scholar
• Reinhold WC, Sunshine M, Liu H, et al. CellMiner: a web-based suite of genomic and pharmacologic tools to explore transcript and drug patterns in the NCI-60 cell line set. Cancer Res. 2012;72(14):3499–511. doi: 10.1158/0008-5472.CAN-12-1370
   PubMed Web of Science ®Google Scholar
• Yang J, Gong CJ, Ke QJ, et al. Insights into the function and clinical application of HDAC5 in cancer management. Front Oncol. 2021;11:11. doi: 10.3389/fonc.2021.661620
   Web of Science ®Google Scholar
• Liu CH, Lv DS, Li M, et al. Hypermethylation of miRNA-589 promoter leads to upregulation of HDAC5 which promotes malignancy in non-small cell lung cancer. Int J Oncol. 2017;50(6):2079–2090. doi: 10.3892/ijo.2017.3967
   PubMed Web of Science ®Google Scholar
• Gu X, Fu CC, Lin LF, et al. miR-124 and miR-9 mediated downregulation of HDAC5 promotes neurite development through activating MEF2C-GPM6A pathway. J Cell Physiol. 2018;233(1):673–687. doi: 10.1002/jcp.25927
   PubMed Web of Science ®Google Scholar
• Hsieh TH, Hsu CY, Tsai CF, et al. HDAC inhibitors target HDAC5, upregulate microRNA-125a-5p, and induce apoptosis in breast cancer cells. Mol Ther. 2015;23(4):656–66. doi: 10.1038/mt.2014.247
   PubMed Web of Science ®Google Scholar
• Li H, Xie H, Liu W, et al. A novel microRNA targeting HDAC5 regulates osteoblast differentiation in mice and contributes to primary osteoporosis in humans. J Clin Invest. 2009;119(12):3666–3677. doi: 10.1172/JCI39832
   PubMed Web of Science ®Google Scholar
• Roccaro AM, Sacco A, Jia X, et al. microRNA-dependent modulation of histone acetylation in Waldenström macroglobulinemia. Blood. 2010;116(9):1506–14. doi: 10.1182/blood-2010-01-265686
   PubMed Web of Science ®Google Scholar
• Dong N, Xu B, Shi H, et al. Baicalein inhibits amadori-glycated albumin-induced MCP-1 expression in retinal ganglion cells via a microRNA-124-dependent mechanism. Invest Ophthalmol Vis Sci. 2015;56(10):5844–5853. doi: 10.1167/iovs.15-17444
   PubMed Web of Science ®Google Scholar
• Shi L, Tian Z, Fu Q, et al. miR-217-regulated MEF2D-HDAC5/ND6 signaling pathway participates in the oxidative stress and inflammatory response after cerebral ischemia. Brain Res. 2020;1739:146835. doi: 10.1016/j.brainres.2020.146835
   PubMed Web of Science ®Google Scholar
• Dell’Aversana C, Giorgio C, D’Amato L, et al. miR-194-5p/BCLAF1 deregulation in AML tumorigenesis. Leukemia. 2017;31(11):2315–2325. doi: 10.1038/leu.2017.64
   PubMed Web of Science ®Google Scholar
• Sweeney BA, Petrov AI, Ribas CE, et al. RNA central 2021: secondary structure integration, improved sequence search and new member databases. Nucleic Acids Res. 2021;49(D1):D212–D220. doi: 10.1093/nar/gkaa921
   PubMed Web of Science ®Google Scholar
• Kozomara A, Birgaoanu M, Griffiths-Jones S. miRBase: from microRNA sequences to function. Nucleic Acids Res. 2019;47(D1):D155–D162. doi: 10.1093/nar/gky1141
   PubMed Web of Science ®Google Scholar
• Simon R, Lam A, Li MC, et al. Analysis of gene expression data using BRB-ArrayTools. Cancer Inform. 2007;3:11–7. doi: 10.1177/117693510700300022
   PubMedGoogle Scholar
• Xu X, Zhao Y, Simon R. Gene set expression comparison kit for BRB-ArrayTools. Bioinformatics. 2008;24(1):137–9. doi: 10.1093/bioinformatics/btm541
   PubMed Web of Science ®Google Scholar
• Huang HY, Lin YC, Li J, et al. miRtarbase 2020: updates to the experimentally validated microRNA-target interaction database. Nucleic Acids Res. 2020;48(D1):D148–D154. doi: 10.1093/nar/gkz896
   PubMed Web of Science ®Google Scholar
• Hsu SD, Lin FM, Wu WY, et al. miRTarBase: a database curates experimentally validated microRNA–target interactions. Nucleic Acids Res. 2011;39(suppl_1):D163–D169. doi: 10.1093/nar/gkq1107
   PubMed Web of Science ®Google Scholar
• Yang H, Sun B, Xu K, et al. Pharmaco-transcriptomic correlation analysis reveals novel responsive signatures to HDAC inhibitors and identifies Dasatinib as a synergistic interactor in small-cell lung cancer. EBioMedicine. 2021;69:103457. doi: 10.1016/j.ebiom.2021.103457
   PubMed Web of Science ®Google Scholar
• Rix U, Hantschel O, Durnberger G, et al. Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets. Blood. 2007;110(12):4055–63. doi: 10.1182/blood-2007-07-102061
   PubMed Web of Science ®Google Scholar
• Wishart DS, Feunang YD, Guo AC, et al. DrugBank 5.0: a major update to the DrugBank database for 2018. Nucleic Acids Res. 2018;46(D1):D1074–D1082. doi: 10.1093/nar/gkx1037
   PubMed Web of Science ®Google Scholar
• Chang Q, Jorgensen C, Pawson T, et al. Effects of dasatinib on EphA2 receptor tyrosine kinase activity and downstream signalling in pancreatic cancer. Br J Cancer. 2008;99(7):1074–82. doi: 10.1038/sj.bjc.6604676
   PubMed Web of Science ®Google Scholar
• Konecny GE, Glas R, Dering J, et al. Activity of the multikinase inhibitor dasatinib against ovarian cancer cells. Br J Cancer. 2009;101(10):1699–708. doi: 10.1038/sj.bjc.6605381
   PubMed Web of Science ®Google Scholar
• Sen B, Peng S, Tang X, et al. Kinase-impaired BRAF mutations in lung cancer confer sensitivity to dasatinib. Sci Transl Med. 2012;4(136):136ra70. doi: 10.1126/scitranslmed.3003513
   PubMed Web of Science ®Google Scholar
• Wong JP, Todd JR, Finetti MA, et al. Dual targeting of PDGFR⍺ and FGFR1 displays synergistic efficacy in malignant rhabdoid tumors. Cell Rep. 2016;17(5):1265–1275. doi: 10.1016/j.celrep.2016.10.005
   PubMed Web of Science ®Google Scholar
• Rodriguez-Agustin A, Casanova V, Grau-Exposito J, et al. Immunomodulatory activity of the tyrosine kinase inhibitor dasatinib to elicit NK cytotoxicity against cancer, HIV infection and aging. Pharmaceutics. 2023;15(3):917. doi: 10.3390/pharmaceutics15030917
   PubMed Web of Science ®Google Scholar
• Lee J, Huang S. Cancer epigenetics: mechanisms and crosstalk of a HDAC inhibitor, vorinostat. Chemotherapy. 2013;2(111):14934. doi: 10.4172/2167-7700.1000111
   PubMedGoogle Scholar
• Bhatla T, Wang J, Morrison DJ, et al. Epigenetic reprogramming reverses the relapse-specific gene expression signature and restores chemosensitivity in childhood B-lymphoblastic leukemia. Blood. 2012;119(22):5201–10. doi: 10.1182/blood-2012-01-401687
   PubMed Web of Science ®Google Scholar
• LaBonte MJ, Wilson PM, Fazzone W, et al. DNA microarray profiling of genes differentially regulated by the histone deacetylase inhibitors vorinostat and LBH589 in colon cancer cell lines. BMC Med Genomics. 2009;2(1):67. doi: 10.1186/1755-8794-2-67
   PubMedGoogle Scholar
• Li CT, Hsiao YM, Wu TC, et al. Vorinostat, SAHA, represses telomerase activity via epigenetic regulation of telomerase reverse transcriptase in non-small cell lung cancer cells. J Cell Biochem. 2011;112(10):3044–3053. doi: 10.1002/jcb.23229
   PubMed Web of Science ®Google Scholar
• Abril YLN, Fernandez IR, Hong JY, et al. Pharmacological and genetic perturbation establish SIRT5 as a promising target in breast cancer. Oncogene. 2021;40(9):1644–1658. doi: 10.1038/s41388-020-01637-w
   PubMed Web of Science ®Google Scholar
• Yousafzai NA, Jin H, Ullah M, et al. Recent advances of SIRT1 and implications in chemotherapeutics resistance in cancer. Am J Cancer Res. 2021;11(11):5233–5248.
   PubMed Web of Science ®Google Scholar
• Pichot CS, Hartig SM, Xia L, et al. Dasatinib synergizes with doxorubicin to block growth, migration, and invasion of breast cancer cells. Br J Cancer. 2009;101(1):38–47. doi: 10.1038/sj.bjc.6605101
   PubMed Web of Science ®Google Scholar
• Lehmann BD, Bauer JA, Chen X, et al. Identification of human triple-negative breast cancer subtypes and preclinical models for selection of targeted therapies. J Clin Invest. 2011;121(7):2750–67. doi: 10.1172/JCI45014
   PubMed Web of Science ®Google Scholar
• Huang F, Reeves K, Han X, et al. Identification of candidate molecular markers predicting sensitivity in solid tumors to dasatinib: rationale for patient selection. Cancer Res. 2007;67(5):2226–38. doi: 10.1158/0008-5472.CAN-06-3633
   PubMed Web of Science ®Google Scholar
• Finn RS, Dering J, Ginther C, et al. Dasatinib, an orally active small molecule inhibitor of both the src and abl kinases, selectively inhibits growth of basal-type/“triple-negative’’ breast cancer cell lines growing in vitro. Breast Cancer Res Tr. 2007;105(3):319–326. doi: 10.1007/s10549-006-9463-x
   PubMed Web of Science ®Google Scholar
• Cao C, Vasilatos SN, Bhargava R, et al. Functional interaction of histone deacetylase 5 (HDAC5) and lysine-specific demethylase 1 (LSD1) promotes breast cancer progression. Oncogene. 2017;36(1):133–145. doi: 10.1038/onc.2016.186
   PubMed Web of Science ®Google Scholar
• Cao C, Wu H, Vasilatos SN, et al. HDAC5-LSD1 axis regulates antineoplastic effect of natural HDAC inhibitor sulforaphane in human breast cancer cells. Int J Cancer. 2018;143(6):1388–1401. doi: 10.1002/ijc.31419
   PubMed Web of Science ®Google Scholar
• Xue Y, Lian WW, Zhi JQ, et al. HDAC5-mediated deacetylation and nuclear localisation of SOX9 is critical for tamoxifen resistance in breast cancer. Br J Cancer. 2019;121(12):1039–1049. doi: 10.1038/s41416-019-0625-0
   PubMed Web of Science ®Google Scholar
• Zhou Q, Chaerkady R, Shaw PG, et al. Screening for therapeutic targets of vorinostat by SILAC-based proteomic analysis in human breast cancer cells. Proteomics. 2010;10(5):1029–39. doi: 10.1002/pmic.200900602
   PubMed Web of Science ®Google Scholar
• Vasudevan AAJ, Hoffmann MJ, Beck MLC, et al. HDAC5 expression in urothelial carcinoma cell lines inhibits long-term proliferation but can promote epithelial-to-mesenchymal transition. Int J Mol Sci. 2019;20(9):2135. doi: 10.3390/ijms20092135
   PubMed Web of Science ®Google Scholar
• Barbarin A, Abdallah M, Lefèvre L, et al. Innate T-αβ lymphocytes as new immunological components of anti-tumoral “off-target” effects of the tyrosine kinase inhibitor dasatinib. Sci Rep-UK. 2020;10(1). doi: 10.1038/s41598-020-60195-z
   PubMed Web of Science ®Google Scholar
• Wang XD, Reeves K, Luo FR, et al. Identification of candidate predictive and surrogate molecular markers for dasatinib in prostate cancer: rationale for patient selection and efficacy monitoring. Genome Biol. 2007;8(11):R255. doi: 10.1186/gb-2007-8-11-r255
   PubMed Web of Science ®Google Scholar
• Roy S, Shor AC, Bagui TK, et al. Histone deacetylase 5 represses the transcription of cyclin D3. J Cell Biochem. 2008;104(6):2143–54. doi: 10.1002/jcb.21771
   PubMed Web of Science ®Google Scholar
• Sharma S, Tyagi W, Tamang R, et al. HDAC5 modulates SATB1 transcriptional activity to promote lung adenocarcinoma. Br J Cancer. 2023;129(4):586–600. doi: 10.1038/s41416-023-02341-8
   PubMed Web of Science ®Google Scholar
• Zhong L, Sun S, Yao S, et al. Histone deacetylase 5 promotes the proliferation and invasion of lung cancer cells. Oncol Rep. 2018;40(4):2224–2232. doi: 10.3892/or.2018.6591
   PubMed Web of Science ®Google Scholar
• Ye M, Fang Z, Gu H, et al. Histone deacetylase 5 promotes the migration and invasion of hepatocellular carcinoma via increasing the transcription of hypoxia-inducible factor-1⍺ under hypoxia condition. Tumor Biol. 2017;39(6):1010428317705034. doi: 10.1177/1010428317705034
   Google Scholar
• Liu JQ, Gu JY, Feng ZH, et al. Both HDAC5 and HDAC6 are required for the proliferation and metastasis of melanoma cells. J Transl Med. 2016;14(1). doi: 10.1186/s12967-015-0753-0
   Google Scholar
• Delcuve GP, Khan DH, Davie JR. Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors. Clin Epigenetics. 2012;4(1):5. doi: 10.1186/1868-7083-4-5
   PubMed Web of Science ®Google Scholar
• Zhao B, Wang YC, Zhao X, et al. SIRT1 enhances oxaliplatin resistance in colorectal cancer through microRNA-20b-3p/DEPDC1 axis. Cell Biol Int. 2022;46(12):2107–2117. doi: 10.1002/cbin.11905
   PubMed Web of Science ®Google Scholar
• Li WB, Sun Z. Mechanism of action for HDAC inhibitors—insights from omics approaches. Int J Mol Sci. 2019;20(7):1616. doi: 10.3390/ijms20071616
   PubMed Web of Science ®Google Scholar
• Claerhout S, Lim JY, Choi W, et al. Gene expression signature analysis identifies vorinostat as a candidate therapy for gastric cancer. PLoS One. 2011;6(9):e24662. doi: 10.1371/journal.pone.0024662
   PubMed Web of Science ®Google Scholar
• Balch C, Naegeli K, Nam S, et al. A unique histone deacetylase inhibitor alters microRNA expression and signal transduction in chemoresistant ovarian cancer cells. Cancer Biol Ther. 2012;13(8):681–693. doi: 10.4161/cbt.20086
   PubMed Web of Science ®Google Scholar
• Huang WT, Tsai YH, Chen SH, et al. HDAC2 and HDAC5 up-regulations modulate survivin and miR-125a-5p expressions and promote hormone therapy resistance in estrogen receptor positive breast cancer cells. Front Pharmacol. 2017;8:902. doi: 10.3389/fphar.2017.00902
   PubMed Web of Science ®Google Scholar
• Yanagisawa S, Baker JR, Vuppusetty C, et al. The dynamic shuttling of SIRT1 between cytoplasm and nuclei in bronchial epithelial cells by single and repeated cigarette smoke exposure. PLoS One. 2018;13(3):e0193921. doi: 10.1371/journal.pone.0193921
   PubMed Web of Science ®Google Scholar
• Kong Y, Jung M, Wang K, et al. Histone deacetylase cytoplasmic trapping by a novel fluorescent HDAC inhibitor. Mol Cancer Ther. 2011;10(9):1591–9. doi: 10.1158/1535-7163.MCT-10-0779
   PubMed Web of Science ®Google Scholar
• Bergmann L, Lang AD, Bross C, et al. Subcellular localization and mitotic interactome analyses identify SIRT4 as a centrosomally localized and microtubule associated protein. Cells (Basel). 2020;9(9):1950. doi: 10.3390/cells9091950
   Google Scholar
• Nieto-Sampedro M, Valle-Argos B, Gómez-Nicola D, et al. Inhibitors of glioma growth that reveal the tumour to the immune system. Clin Med Insights-On. 2011;5:265–314. doi: 10.4137/CMO.S7685
   PubMedGoogle Scholar
• Krushkal J, Negi S, Yee LM, et al. Molecular genomic features associated with in vitro response of the NCI-60 cancer cell line panel to natural products. Mol Oncol. 2021;15(2):381–406. doi: 10.1002/1878-0261.12849
   PubMed Web of Science ®Google Scholar
• Muselli F, Peyron JF, Mary D. Druggable biochemical pathways and potential therapeutic alternatives to target leukemic stem cells and eliminate the residual disease in chronic myeloid leukemia. Int J Mol Sci. 2019;20(22):5616. doi: 10.3390/ijms20225616
   PubMed Web of Science ®Google Scholar
• Nebbioso A, Carafa V, Benedetti R, et al. Trials with ‘epigenetic’ drugs: an update. Mol Oncol. 2012;6(6):657–82. doi: 10.1016/j.molonc.2012.09.004
   PubMed Web of Science ®Google Scholar
• Massimino M, Stella S, Tirro E, et al. Non ABL-directed inhibitors as alternative treatment strategies for chronic myeloid leukemia. Mol Cancer. 2018;17(1):56. doi: 10.1186/s12943-018-0805-1
   PubMedGoogle Scholar
• Chien W, Sudo M, Ding LW, et al. Functional genome-wide screening identifies targets and pathways sensitizing pancreatic cancer cells to dasatinib. J Cancer. 2018;9(24):4762–4773. doi: 10.7150/jca.25138
   PubMed Web of Science ®Google Scholar
• Fiskus W, Pranpat M, Balasis M, et al. Cotreatment with vorinostat (suberoylanilide hydroxamic acid) enhances activity of dasatinib (BMS-354825) against imatinib mesylate-sensitive or imatinib mesylate-resistant chronic myelogenous leukemia cells. Clin Cancer Res. 2006;12(19):5869–5878. doi: 10.1158/1078-0432.CCR-06-0980
   PubMed Web of Science ®Google Scholar
• Wu YS, Quan Y, Zhang DX, et al. Synergistic inhibition of breast cancer cell growth by an epigenome-targeting drug and a tyrosine kinase inhibitor. Biol Pharm Bull. 2017;40(10):1747–1753. doi: 10.1248/bpb.b17-00360
   PubMed Web of Science ®Google Scholar
• Mahendrarajah N, Paulus R, Kramer OH. Histone deacetylase inhibitors induce proteolysis of activated CDC42-associated kinase-1 in leukemic cells. J Cancer Res Clin Oncol. 2016;142(11):2263–73. doi: 10.1007/s00432-016-2229-x
   PubMed Web of Science ®Google Scholar
• Chan D, Zheng Y, Tyner JW, et al. Belinostat and panobinostat (HDACI): in vitro and in vivo studies in thyroid cancer. J Cancer Res Clin Oncol. 2013;139(9):1507–14. doi: 10.1007/s00432-013-1465-6
   PubMed Web of Science ®Google Scholar
• Heo SK, Noh EK, Yoon DJ, et al. Dasatinib accelerates valproic acid-induced acute myeloid leukemia cell death by regulation of differentiation capacity. PLoS One. 2014;9(2):e98859. doi: 10.1371/journal.pone.0098859
   PubMedGoogle Scholar
• Zhang J, Chen Y, He QY. Distinct characteristics of dasatinib-induced pyroptosis in gasdermin E-expressing human lung cancer A549 cells and neuroblastoma SH-SY5Y cells. Oncol Lett. 2020;20(1):145–154. doi: 10.3892/ol.2020.12406
   Web of Science ®Google Scholar