表观遗传甲基化在肾脏疾病中的新作用

Luyckx, V.A.; Tonelli, M.; Stanifer, J.W. The global burden of kidney disease and the sustainable development goals. Bull. World Health Organ., 2018, 96(6), 414-422D.
[http://dx.doi.org/10.2471/BLT.17.206441] [PMID: 29904224]

Petronis, A. Epigenetics as a unifying principle in the aetiology of complex traits and diseases. Nature, 2010, 465(7299), 721-727.
[http://dx.doi.org/10.1038/nature09230] [PMID: 20535201]

Dressler, G.R.; Patel, S.R. Epigenetics in kidney development and renal disease. Transl. Res., 2015, 165(1), 166-176.
[http://dx.doi.org/10.1016/j.trsl.2014.04.007] [PMID: 24958601]

Biswas, S.; Rao, C.M. Epigenetic tools (The Writers, The Readers and The Erasers) and their implications in cancer therapy. Eur. J. Pharmacol., 2018, 837, 8-24.
[http://dx.doi.org/10.1016/j.ejphar.2018.08.021] [PMID: 30125562]

Lee, K.H.; Kim, B.C.; Jeong, S.H.; Jeong, C.W.; Ku, J.H.; Kwak, C.; Kim, H.H. Histone Demethylase LSD1 regulates kidney cancer progression by modulating androgen receptor activity. Int. J. Mol. Sci., 2020, 21(17), 6089.
[http://dx.doi.org/10.3390/ijms21176089] [PMID: 32847068]

Liu, L-M.; Sun, W-Z.; Fan, X-Z.; Xu, Y-L.; Cheng, M-B.; Zhang, Y. Methylation of C/EBPα by PRMT1 inhibits its tumor-suppressive function in breast cancer. Cancer Res., 2019, 79(11), 2865-2877.
[http://dx.doi.org/10.1158/0008-5472.CAN-18-3211] [PMID: 31015230]

Schübeler, D. Function and information content of DNA methylation. Nature, 2015, 517(7534), 321-326.
[http://dx.doi.org/10.1038/nature14192] [PMID: 25592537]

Beckerman, P.; Ko, Y-A.; Susztak, K. Epigenetics: A new way to look at kidney diseases. Nephrol. Dial. Transplant., 2014, 29(10), 1821-1827.
[http://dx.doi.org/10.1093/ndt/gfu026] [PMID: 24675284]

Latham, K.E. X chromosome imprinting and inactivation in the early mammalian embryo. Trends Genet., 1996, 12(4), 134-138.
[http://dx.doi.org/10.1016/0168-9525(96)10017-2] [PMID: 8901417]

Smith, S.S. Maintaining the unmethylated state. Clin. Epigenetics, 2013, 5(1), 17.
[http://dx.doi.org/10.1186/1868-7083-5-17] [PMID: 24079333]

Toyota, M.; Ahuja, N.; Ohe-Toyota, M.; Herman, J.G.; Baylin, S.B.; Issa, J.P. CpG island methylator phenotype in colorectal cancer. Proc. Natl. Acad. Sci. USA, 1999, 96(15), 8681-8686.
[http://dx.doi.org/10.1073/pnas.96.15.8681] [PMID: 10411935]

Zhang, L.; Zhang, Q.; Liu, S.; Chen, Y.; Li, R.; Lin, T.; Yu, C.; Zhang, H.; Huang, Z.; Zhao, X.; Tan, X.; Li, Z.; Ye, Z.; Ma, J.; Zhang, B.; Wang, W.; Shi, W.; Liang, X. DNA methyltransferase 1 may be a therapy target for attenuating diabetic nephropathy and podocyte injury. Kidney Int., 2017, 92(1), 140-153.
[http://dx.doi.org/10.1016/j.kint.2017.01.010] [PMID: 28318634]

Jones, P.A. Functions of DNA methylation: Islands, start sites, gene bodies and beyond. Nat. Rev. Genet., 2012, 13(7), 484-492.
[http://dx.doi.org/10.1038/nrg3230] [PMID: 22641018]

Okano, M.; Xie, S.; Li, E. Dnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cells. Nucleic Acids Res., 1998, 26(11), 2536-2540.
[http://dx.doi.org/10.1093/nar/26.11.2536] [PMID: 9592134]

Goll, M.G.; Kirpekar, F.; Maggert, K.A.; Yoder, J.A.; Hsieh, C-L.; Zhang, X.; Golic, K.G.; Jacobsen, S.E.; Bestor, T.H. Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. Science, 2006, 311(5759), 395-398.
[http://dx.doi.org/10.1126/science.1120976] [PMID: 16424344]

Tuorto, F.; Herbst, F.; Alerasool, N.; Bender, S.; Popp, O.; Federico, G.; Reitter, S.; Liebers, R.; Stoecklin, G.; Gröne, H.J.; Dittmar, G.; Glimm, H.; Lyko, F. The tRNA methyltransferase Dnmt2 is required for accurate polypeptide synthesis during haematopoiesis. EMBO J., 2015, 34(18), 2350-2362.
[http://dx.doi.org/10.15252/embj.201591382] [PMID: 26271101]

Rassoulzadegan, M.; Grandjean, V.; Gounon, P.; Vincent, S.; Gillot, I.; Cuzin, F. RNA-mediated non-mendelian inheritance of an epigenetic change in the mouse. Nature, 2006, 441(7092), 469-474.
[http://dx.doi.org/10.1038/nature04674] [PMID: 16724059]

Dahl, C.; Guldberg, P. DNA methylation analysis techniques. Biogerontology, 2003, 4(4), 233-250.
[http://dx.doi.org/10.1023/A:1025103319328] [PMID: 14501188]

Guo, C.; Pei, L.; Xiao, X.; Wei, Q.; Chen, J-K.; Ding, H-F.; Huang, S.; Fan, G.; Shi, H.; Dong, Z. DNA methylation protects against cisplatin-induced kidney injury by regulating specific genes, including interferon regulatory factor 8. Kidney Int., 2017, 92(5), 1194-1205.
[http://dx.doi.org/10.1016/j.kint.2017.03.038] [PMID: 28709638]

Wang, J.; Li, H.; Qiu, S.; Dong, Z.; Xiang, X.; Zhang, D. MBD2 upregulates miR-301a-5p to induce kidney cell apoptosis during vancomycin-induced AKI. Cell Death Dis., 2017, 8(10), e3120-e3120.
[http://dx.doi.org/10.1038/cddis.2017.509] [PMID: 29022913]

Castellano, G.; Franzin, R.; Sallustio, F.; Stasi, A.; Banelli, B.; Romani, M.; De Palma, G.; Lucarelli, G.; Divella, C.; Battaglia, M.; Crovace, A.; Staffieri, F.; Grandaliano, G.; Stallone, G.; Ditonno, P.; Cravedi, P.; Cantaluppi, V.; Gesualdo, L. Complement component C5a induces aberrant epigenetic modifications in renal tubular epithelial cells accelerating senescence by Wnt4/βcatenin signaling after ischemia/reperfusion injury. Aging (Albany NY), 2019, 11(13), 4382-4406.
[http://dx.doi.org/10.18632/aging.102059] [PMID: 31284268]

Tampe, B.; Steinle, U.; Tampe, D.; Carstens, J.L.; Korsten, P.; Zeisberg, E.M.; Müller, G.A.; Kalluri, R.; Zeisberg, M. Low-dose hydralazine prevents fibrosis in a murine model of acute kidney injury-to-chronic kidney disease progression. Kidney Int., 2017, 91(1), 157-176.
[http://dx.doi.org/10.1016/j.kint.2016.07.042] [PMID: 27692563]

Singh, N.; Dueñas-González, A.; Lyko, F.; Medina-Franco, J.L. Molecular modeling and molecular dynamics studies of hydralazine with human DNA methyltransferase 1. ChemMedChem, 2009, 4(5), 792-799.
[http://dx.doi.org/10.1002/cmdc.200900017] [PMID: 19322801]

Yin, S.; Zhang, Q.; Yang, J.; Lin, W.; Li, Y.; Chen, F.; Cao, W. TGFβ-incurred epigenetic aberrations of miRNA and DNA methyltransferase suppress Klotho and potentiate renal fibrosis. Biochim. Biophys. Acta Mol. Cell Res., 2017, 1864(7), 1207-1216.
[http://dx.doi.org/10.1016/j.bbamcr.2017.03.002] [PMID: 28285987]

Agha, G.; Mendelson, M.M.; Ward-Caviness, C.K.; Joehanes, R.; Huan, T.; Gondalia, R.; Salfati, E.; Brody, J.A.; Fiorito, G.; Bressler, J.; Chen, B.H.; Ligthart, S.; Guarrera, S.; Colicino, E.; Just, A.C.; Wahl, S.; Gieger, C.; Vandiver, A.R.; Tanaka, T.; Hernandez, D.G.; Pilling, L.C.; Singleton, A.B.; Sacerdote, C.; Krogh, V.; Panico, S.; Tumino, R.; Li, Y.; Zhang, G.; Stewart, J.D.; Floyd, J.S.; Wiggins, K.L.; Rotter, J.I.; Multhaup, M.; Bakulski, K.; Horvath, S.; Tsao, P.S.; Absher, D.M.; Vokonas, P.; Hirschhorn, J.; Fallin, M.D.; Liu, C.; Bandinelli, S.; Boerwinkle, E.; Dehghan, A.; Schwartz, J.D.; Psaty, B.M.; Feinberg, A.P.; Hou, L.; Ferrucci, L.; Sotoodehnia, N.; Matullo, G.; Peters, A.; Fornage, M.; Assimes, T.L.; Whitsel, E.A.; Levy, D.; Baccarelli, A.A. Blood leukocyte DNA methylation predicts risk of future myocardial infarction and coronary heart disease. Circulation, 2019, 140(8), 645-657.
[http://dx.doi.org/10.1161/CIRCULATIONAHA.118.039357] [PMID: 31424985]

Chu, A.Y.; Tin, A.; Schlosser, P.; Ko, Y-A.; Qiu, C.; Yao, C.; Joehanes, R.; Grams, M.E.; Liang, L.; Gluck, C.A.; Liu, C.; Coresh, J.; Hwang, S.J.; Levy, D.; Boerwinkle, E.; Pankow, J.S.; Yang, Q.; Fornage, M.; Fox, C.S.; Susztak, K.; Köttgen, A. Epigenome-wide association studies identify DNA methylation associated with kidney function. Nat. Commun., 2017, 8(1), 1286-1286.
[http://dx.doi.org/10.1038/s41467-017-01297-7] [PMID: 29097680]

Wahl, S.; Drong, A.; Lehne, B.; Loh, M.; Scott, W.R.; Kunze, S.; Tsai, P.C.; Ried, J.S.; Zhang, W.; Yang, Y.; Tan, S.; Fiorito, G.; Franke, L.; Guarrera, S.; Kasela, S.; Kriebel, J.; Richmond, R.C.; Adamo, M.; Afzal, U.; Ala-Korpela, M.; Albetti, B.; Ammerpohl, O.; Apperley, J.F.; Beekman, M.; Bertazzi, P.A.; Black, S.L.; Blancher, C.; Bonder, M.J.; Brosch, M.; Carstensen-Kirberg, M.; de Craen, A.J.; de Lusignan, S.; Dehghan, A.; Elkalaawy, M.; Fischer, K.; Franco, O.H.; Gaunt, T.R.; Hampe, J.; Hashemi, M.; Isaacs, A.; Jenkinson, A.; Jha, S.; Kato, N.; Krogh, V.; Laffan, M.; Meisinger, C.; Meitinger, T.; Mok, Z.Y.; Motta, V.; Ng, H.K.; Nikolakopoulou, Z.; Nteliopoulos, G.; Panico, S.; Pervjakova, N.; Prokisch, H.; Rathmann, W.; Roden, M.; Rota, F.; Rozario, M.A.; Sandling, J.K.; Schafmayer, C.; Schramm, K.; Siebert, R.; Slagboom, P.E.; Soininen, P.; Stolk, L.; Strauch, K.; Tai, E.S.; Tarantini, L.; Thorand, B.; Tigchelaar, E.F.; Tumino, R.; Uitterlinden, A.G.; van Duijn, C.; van Meurs, J.B.; Vineis, P.; Wickremasinghe, A.R.; Wijmenga, C.; Yang, T.P.; Yuan, W.; Zhernakova, A.; Batterham, R.L.; Smith, G.D.; Deloukas, P.; Heijmans, B.T.; Herder, C.; Hofman, A.; Lindgren, C.M.; Milani, L.; van der Harst, P.; Peters, A.; Illig, T.; Relton, C.L.; Waldenberger, M.; Järvelin, M.R.; Bollati, V.; Soong, R.; Spector, T.D.; Scott, J.; McCarthy, M.I.; Elliott, P.; Bell, J.T.; Matullo, G.; Gieger, C.; Kooner, J.S.; Grallert, H.; Chambers, J.C. Epigenome-wide association study of body mass index, and the adverse outcomes of adiposity. Nature, 2017, 541(7635), 81-86.
[http://dx.doi.org/10.1038/nature20784] [PMID: 28002404]

Zawada, A.M.; Schneider, J.S.; Michel, A.I.; Rogacev, K.S.; Hummel, B.; Krezdorn, N.; Müller, S.; Rotter, B.; Winter, P.; Obeid, R.; Geisel, J.; Fliser, D.; Heine, G.H. DNA methylation profiling reveals differences in the 3 human monocyte subsets and identifies uremia to induce DNA methylation changes during differentiation. Epigenetics, 2016, 11(4), 259-272.
[http://dx.doi.org/10.1080/15592294.2016.1158363] [PMID: 27018948]

Hamatani, H.; Sakairi, T.; Ikeuchi, H.; Kaneko, Y.; Maeshima, A.; Nojima, Y.; Hiromura, K. TGF-β1 alters DNA methylation levels in promoter and enhancer regions of the WT1 gene in human podocytes. Nephrology (Carlton), 2019, 24(5), 575-584.
[http://dx.doi.org/10.1111/nep.13411] [PMID: 29851165]

Heylen, L.; Thienpont, B.; Naesens, M.; Lambrechts, D.; Sprangers, B. The emerging role of DNA methylation in kidney transplantation: A perspective. Am. J. Transplant., 2016, 16(4), 1070-1078.
[http://dx.doi.org/10.1111/ajt.13585] [PMID: 26780242]

Chen, G.; Chen, H.; Ren, S.; Xia, M.; Zhu, J.; Liu, Y.; Zhang, L.; Tang, L.; Sun, L.; Liu, H.; Dong, Z. Aberrant DNA methylation of mTOR pathway genes promotes inflammatory activation of immune cells in diabetic kidney disease. Kidney Int., 2019, 96(2), 409-420.
[http://dx.doi.org/10.1016/j.kint.2019.02.020] [PMID: 31101365]

Hotamisligil, G.S. Inflammation, metaflammation and immunometabolic disorders. Nature, 2017, 542(7640), 177-185.
[http://dx.doi.org/10.1038/nature21363] [PMID: 28179656]

Bansal, A.; Balasubramanian, S.; Dhawan, S.; Leung, A.; Chen, Z.; Natarajan, R. Integrative omics analyses reveal epigenetic memory in diabetic renal cells regulating genes associated with kidney dysfunction. Diabetes, 2020, 69(11), 2490-2502.
[http://dx.doi.org/10.2337/db20-0382] [PMID: 32747424]

Watanabe, A.; Marumo, T.; Kawarazaki, W.; Nishimoto, M.; Ayuzawa, N.; Ueda, K.; Hirohama, D.; Tanaka, T.; Yagi, S.; Ota, S.; Nagae, G.; Aburatani, H.; Kumagai, H.; Fujita, T. Aberrant DNA methylation of pregnane X receptor underlies metabolic gene alterations in the diabetic kidney. Am. J. Physiol. Renal Physiol., 2018, 314(4), F551-F560.
[http://dx.doi.org/10.1152/ajprenal.00390.2017] [PMID: 29212764]

Smyth, L.J.; Patterson, C.C.; Swan, E.J.; Maxwell, A.P.; McKnight, A.J. DNA methylation associated with diabetic kidney disease in blood-derived DNA. Front. Cell Dev. Biol., 2020, 8561907
[http://dx.doi.org/10.3389/fcell.2020.561907] [PMID: 33178681]

Oba, S.; Ayuzawa, N.; Nishimoto, M.; Kawarazaki, W.; Ueda, K.; Hirohama, D.; Kawakami-Mori, F.; Shimosawa, T.; Marumo, T.; Fujita, T. Aberrant DNA methylation of Tgfb1 in diabetic kidney mesangial cells. Sci. Rep., 2018, 8(1), 16338.
[http://dx.doi.org/10.1038/s41598-018-34612-3] [PMID: 30397232]

Chen, W.; Zhuang, J.; Wang, P.P.; Jiang, J.; Lin, C.; Zeng, P.; Liang, Y.; Zhang, X.; Dai, Y.; Diao, H. DNA methylation-based classification and identification of renal cell carcinoma prognosis-subgroups. Cancer Cell Int., 2019, 19(1), 185.
[http://dx.doi.org/10.1186/s12935-019-0900-4] [PMID: 31346320]

Miao, Y.; Cao, F.; Li, P.; Liu, P. DNA methylation of Hugl-2 is a prognostic biomarker in kidney renal clear cell carcinoma. Clin. Exp. Pharmacol. Physiol., 2020, 48(1), 44-53.
[http://dx.doi.org/10.1111/1440-1681.13390] [PMID: 32754907]

Heylen, L.; Thienpont, B.; Busschaert, P.; Sprangers, B.; Kuypers, D.; Moisse, M.; Lerut, E.; Lambrechts, D.; Naesens, M. Age-related changes in DNA methylation affect renal histology and post-transplant fibrosis. Kidney Int., 2019, 96(5), 1195-1204.
[http://dx.doi.org/10.1016/j.kint.2019.06.018] [PMID: 31530476]

Yang, Q.; Chen, H-Y.; Wang, J-N.; Han, H-Q.; Jiang, L.; Wu, W-F.; Wei, B.; Gao, L.; Ma, Q.Y.; Liu, X.Q.; Chen, Q.; Wen, J.G.; Jin, J.; Huang, Y.; Ni, W.J.; Ma, T.T.; Li, J.; Meng, X.M. Alcohol promotes renal fibrosis by activating Nox2/4-mediated DNA methylation of Smad7. Clin. Sci. (Lond.), 2020, 134(2), 103-122.
[http://dx.doi.org/10.1042/CS20191047] [PMID: 31898747]

Chang, Y.W.; Singh, K.P. Arsenic induces fibrogenic changes in human kidney epithelial cells potentially through epigenetic alterations in DNA methylation. J. Cell. Physiol., 2019, 234(4), 4713-4725.
[http://dx.doi.org/10.1002/jcp.27244] [PMID: 30191986]

Li, H.; Zhang, W.; Zhong, F.; Das, G.C.; Xie, Y.; Li, Z.; Cai, W.; Jiang, G.; Choi, J.; Sidani, M.; Hyink, D.P.; Lee, K.; Klotman, P.E.; He, J.C. Epigenetic regulation of RCAN1 expression in kidney disease and its role in podocyte injury. Kidney Int., 2018, 94(6), 1160-1176.
[http://dx.doi.org/10.1016/j.kint.2018.07.023] [PMID: 30366682]

Zinellu, A.; Sotgia, S.; Sotgiu, E.; Assaretti, S.; Baralla, A.; Mangoni, A.A.; Satta, A.E.; Carru, C. Cholesterol lowering treatment restores blood global DNA methylation in chronic kidney disease (CKD) patients. Nutr. Metab. Cardiovasc. Dis., 2017, 27(9), 822-829.
[http://dx.doi.org/10.1016/j.numecd.2017.06.011] [PMID: 28755807]

Hayashi, K.; Hishikawa, A.; Hashiguchi, A.; Azegami, T.; Yoshimoto, N.; Nakamichi, R.; Tokuyama, H.; Itoh, H. Association of glomerular DNA damage and DNA methylation with one-year eGFR decline in IgA nephropathy. Sci. Rep., 2020, 10(1), 237.
[http://dx.doi.org/10.1038/s41598-019-57140-0] [PMID: 31937846]

Smyth, L.J.; Duffy, S.; Maxwell, A.P.; McKnight, A.J. Genetic and epigenetic factors influencing chronic kidney disease. Am. J. Physiol. Renal Physiol., 2014, 307(7), F757-F776.
[http://dx.doi.org/10.1152/ajprenal.00306.2014] [PMID: 25080522]

Hishikawa, A.; Hayashi, K.; Abe, T.; Kaneko, M.; Yokoi, H.; Azegami, T.; Nakamura, M.; Yoshimoto, N.; Kanda, T.; Sakamaki, Y.; Itoh, H. Decreased KAT5 expression impairs DNA repair and induces altered DNA methylation in kidney podocytes. Cell Rep., 2019, 26(5), 1318-1332.e4.
[http://dx.doi.org/10.1016/j.celrep.2019.01.005] [PMID: 30699357]

Hishikawa, A.; Hayashi, K.; Yoshimoto, N.; Nakamichi, R.; Homma, K.; Itoh, H. DNA damage and expression of DNA methylation modulators in urine-derived cells of patients with hypertension and diabetes. Sci. Rep., 2020, 10(1), 3377.
[http://dx.doi.org/10.1038/s41598-020-60420-9] [PMID: 32099032]

Cann, K.L.; Dellaire, G. Heterochromatin and the DNA damage response: The need to relax. Biochem. Cell Biol., 2011, 89(1), 45-60.
[http://dx.doi.org/10.1139/O10-113] [PMID: 21326362]

Ito, S.; Shen, L.; Dai, Q.; Wu, S.C.; Collins, L.B.; Swenberg, J.A.; He, C.; Zhang, Y. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science, 2011, 333(6047), 1300-1303.
[http://dx.doi.org/10.1126/science.1210597] [PMID: 21778364]

Ito, S.; D’Alessio, A.C.; Taranova, O.V.; Hong, K.; Sowers, L.C.; Zhang, Y. Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification. Nature, 2010, 466(7310), 1129-1133.
[http://dx.doi.org/10.1038/nature09303] [PMID: 20639862]

Huang, N.; Tan, L.; Xue, Z.; Cang, J.; Wang, H. Reduction of DNA hydroxymethylation in the mouse kidney insulted by ischemia reperfusion. Biochem. Biophys. Res. Commun., 2012, 422(4), 697-702.
[http://dx.doi.org/10.1016/j.bbrc.2012.05.061] [PMID: 22627137]

Williams, K.; Christensen, J.; Pedersen, M.T.; Johansen, J.V.; Cloos, P.A.; Rappsilber, J.; Helin, K. TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity. Nature, 2011, 473(7347), 343-348.
[http://dx.doi.org/10.1038/nature10066] [PMID: 21490601]

Tahiliani, M.; Koh, K.P.; Shen, Y.; Pastor, W.A.; Bandukwala, H.; Brudno, Y.; Agarwal, S.; Iyer, L.M.; Liu, D.R.; Aravind, L.; Rao, A. Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science, 2009, 324(5929), 930-935.
[http://dx.doi.org/10.1126/science.1170116] [PMID: 19372391]

Watson, C.J.; Collier, P.; Tea, I.; Neary, R.; Watson, J.A.; Robinson, C.; Phelan, D.; Ledwidge, M.T.; McDonald, K.M.; McCann, A.; Sharaf, O.; Baugh, J.A. Hypoxia-induced epigenetic modifications are associated with cardiac tissue fibrosis and the development of a myofibroblast-like phenotype. Hum. Mol. Genet., 2014, 23(8), 2176-2188.
[http://dx.doi.org/10.1093/hmg/ddt614] [PMID: 24301681]

Singh, V.; Sharma, P.; Capalash, N. DNA methyltransferase-1 inhibitors as epigenetic therapy for cancer. Curr. Cancer Drug Targets, 2013, 13(4), 379-399.
[http://dx.doi.org/10.2174/15680096113139990077] [PMID: 23517596]

Liu, B.; Du, Q.; Chen, L.; Fu, G.; Li, S.; Fu, L.; Zhang, X.; Ma, C.; Bin, C. CpG methylation patterns of human mitochondrial DNA. Sci. Rep., 2016, 6(1), 23421.
[http://dx.doi.org/10.1038/srep23421] [PMID: 26996456]

Mau, T.; Yung, R. Potential of epigenetic therapies in non-cancerous conditions. Front. Genet., 2014, 5, 438.
[http://dx.doi.org/10.3389/fgene.2014.00438] [PMID: 25566322]

Greer, E.L.; Shi, Y. Histone methylation: A dynamic mark in health, disease and inheritance. Nat. Rev. Genet., 2012, 13(5), 343-357.
[http://dx.doi.org/10.1038/nrg3173] [PMID: 22473383]

Nguyen, A.T.; Zhang, Y. The diverse functions of Dot1 and H3K79 methylation. Genes Dev., 2011, 25(13), 1345-1358.
[http://dx.doi.org/10.1101/gad.2057811] [PMID: 21724828]

Zhang, A.S.; Xu, Y.P.; Sui, X.L.; Zhang, Y.Z.; Gu, F.J.; Chen, J.H. Correlation between histone H3K4 trimethylation and DNA methylation and evaluation of the metabolomic features in acute rejection after kidney transplantation. Am. J. Transl. Res., 2020, 12(11), 7565-7580.
[PMID: 33312389]

Lin, S-H.; Ho, W-T.; Wang, Y-T.; Chuang, C-T.; Chuang, L-Y.; Guh, J-Y. Histone methyltransferase Suv39h1 attenuates high glucose-induced fibronectin and p21(WAF1) in mesangial cells. Int. J. Biochem. Cell Biol., 2016, 78, 96-105.
[http://dx.doi.org/10.1016/j.biocel.2016.06.021] [PMID: 27373678]

Sasaki, K.; Doi, S.; Nakashima, A.; Irifuku, T.; Yamada, K.; Kokoroishi, K.; Ueno, T.; Doi, T.; Hida, E.; Arihiro, K.; Kohno, N.; Masaki, T. Inhibition of SET domain-containing lysine methyltransferase 7/9 ameliorates renal fibrosis. J. Am. Soc. Nephrol., 2016, 27(1), 203-215.
[http://dx.doi.org/10.1681/ASN.2014090850] [PMID: 26045091]

Irifuku, T.; Doi, S.; Sasaki, K.; Doi, T.; Nakashima, A.; Ueno, T.; Yamada, K.; Arihiro, K.; Kohno, N.; Masaki, T. Inhibition of H3K9 histone methyltransferase G9a attenuates renal fibrosis and retains klotho expression. Kidney Int., 2016, 89(1), 147-157.
[http://dx.doi.org/10.1038/ki.2015.291] [PMID: 26444031]

Sharma, N.; Sankrityayan, H.; Kale, A.; Gaikwad, A.B. Role of SET7/9 in the progression of ischemic renal injury in diabetic and non-diabetic rats. Biochem. Biophys. Res. Commun., 2020, 528(1), 14-20.
[http://dx.doi.org/10.1016/j.bbrc.2020.05.075] [PMID: 32448511]

Chen, J.; Gu, Y.; Zhang, H.; Ning, Y.; Song, N.; Hu, J.; Cai, J.; Shi, Y.; Ding, X.; Zhang, X. Amelioration of uremic toxin indoxyl sulfate-induced osteoblastic calcification by SET domain containing lysine methyltransferase 7/9 protein. Nephron, 2019, 141(4), 287-294.
[http://dx.doi.org/10.1159/000495885] [PMID: 30783062]

Jia, Y.; Reddy, M.A.; Das, S.; Oh, H.J.; Abdollahi, M.; Yuan, H.; Zhang, E.; Lanting, L.; Wang, M.; Natarajan, R. Dysregulation of histone H3 lysine 27 trimethylation in transforming growth factor-β1-induced gene expression in mesangial cells and diabetic kidney. J. Biol. Chem., 2019, 294(34), 12695-12707.
[http://dx.doi.org/10.1074/jbc.RA119.007575] [PMID: 31266808]

Soofi, A.; Kutschat, A.P.; Azam, M.; Laszczyk, A.M.; Dressler, G.R. Regeneration after acute kidney injury requires PTIP-mediated epigenetic modifications. JCI Insight, 2020, 5(3)e130204
[http://dx.doi.org/10.1172/jci.insight.130204] [PMID: 31917689]

Morera, L.; Lübbert, M.; Jung, M. Targeting histone methyltransferases and demethylases in clinical trials for cancer therapy. Clin. Epigenetics, 2016, 8(1), 57.
[http://dx.doi.org/10.1186/s13148-016-0223-4] [PMID: 27222667]

Liu, Y.; Yu, Y.; Zhang, J.; Wang, C. The therapeutic effect of dexmedetomidine on protection from renal failure via inhibiting KDM5A in lipopolysaccharide-induced sepsis of mice. Life Sci., 2019, 239(239)116868
[http://dx.doi.org/10.1016/j.lfs.2019.116868] [PMID: 31682847]

Chen, H.; Huang, Y.; Zhu, X.; Liu, C.; Yuan, Y.; Su, H.; Zhang, C.; Liu, C.; Xiong, M.; Qu, Y.; Yun, P.; Zheng, L.; Huang, K. Histone demethylase UTX is a therapeutic target for diabetic kidney disease. J. Physiol., 2019, 597(6), 1643-1660.
[http://dx.doi.org/10.1113/JP277367] [PMID: 30516825]

Guo, Y.; Xiong, Z.; Guo, X. Histone demethylase KDM6B regulates human podocyte differentiation in vitro. Biochem. J., 2019, 476(12), 1741-1751.
[http://dx.doi.org/10.1042/BCJ20180968] [PMID: 31138771]

Deng, X.; Hamamoto, R.; Vougiouklakis, T.; Wang, R.; Yoshioka, Y.; Suzuki, T.; Dohmae, N.; Matsuo, Y.; Park, J.H.; Nakamura, Y. Critical roles of SMYD2-mediated β-catenin methylation for nuclear translocation and activation of Wnt signaling. Oncotarget, 2017, 8(34), 55837-55847.
[http://dx.doi.org/10.18632/oncotarget.19646] [PMID: 28915556]

Li, L.X.; Fan, L.X.; Zhou, J.X.; Grantham, J.J.; Calvet, J.P.; Sage, J.; Li, X. Lysine methyltransferase SMYD2 promotes cyst growth in autosomal dominant polycystic kidney disease. J. Clin. Invest., 2017, 127(7), 2751-2764.
[http://dx.doi.org/10.1172/JCI90921] [PMID: 28604386]

Ea, C-K.; Baltimore, D. Regulation of NF-kappaB activity through lysine monomethylation of p65. Proc. Natl. Acad. Sci. USA, 2009, 106(45), 18972-18977.
[http://dx.doi.org/10.1073/pnas.0910439106] [PMID: 19864627]

Roworth, A.P.; Carr, S.M.; Liu, G.; Barczak, W.; Miller, R.L.; Munro, S.; Kanapin, A.; Samsonova, A.; La Thangue, N.B. Arginine methylation expands the regulatory mechanisms and extends the genomic landscape under E2F control. Sci. Adv., 2019, 5(6)eaaw4640
[http://dx.doi.org/10.1126/sciadv.aaw4640] [PMID: 31249870]

Huang, L.; Wang, Z.; Narayanan, N.; Yang, Y. Arginine methylation of the C-terminus RGG motif promotes TOP3B topoisomerase activity and stress granule localization. Nucleic Acids Res., 2018, 46(6), 3061-3074.
[http://dx.doi.org/10.1093/nar/gky103] [PMID: 29471495]

Zhu, Y.; He, X.; Lin, Y.C.; Dong, H.; Zhang, L.; Chen, X.; Wang, Z.; Shen, Y.; Li, M.; Wang, H.; Sun, J.; Nguyen, L.X.; Zhang, H.; Jiang, W.; Yang, Y.; Chen, J.; Müschen, M.; Chen, C.W.; Konopleva, M.Y.; Sun, W.; Jin, J.; Carlesso, N.; Marcucci, G.; Luo, Y.; Li, L. Targeting PRMT1-mediated FLT3 methylation disrupts maintenance of MLL-rearranged acute lymphoblastic leukemia. Blood, 2019, 134(15), 1257-1268.
[http://dx.doi.org/10.1182/blood.2019002457] [PMID: 31395602]

Boisvert, F-M.; Rhie, A.; Richard, S.; Doherty, A.J. The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell Cycle, 2005, 4(12), 1834-1841.
[http://dx.doi.org/10.4161/cc.4.12.2250] [PMID: 16294045]

Boisvert, F.M.; Déry, U.; Masson, J.Y.; Richard, S. Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev., 2005, 19(6), 671-676.
[http://dx.doi.org/10.1101/gad.1279805] [PMID: 15741314]

Choi, H-J.; Weis, W.I. Purification and Structural Analysis of Desmoplakin.In: Methods in Enzymology; Wilson, K.L.; Sonnenberg, A., Eds.; Academic Press, USA, , 2016; 569, pp. (Ch. 11)197-213.

Yoshimoto, T.; Boehm, M.; Olive, M.; Crook, M.F.; San, H.; Langenickel, T.; Nabel, E.G. The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Exp. Cell Res., 2006, 312(11), 2040-2053.
[http://dx.doi.org/10.1016/j.yexcr.2006.03.001] [PMID: 16616919]

Marjon, K.; Cameron, M.J.; Quang, P.; Clasquin, M.F.; Mandley, E.; Kunii, K.; McVay, M.; Choe, S.; Kernytsky, A.; Gross, S.; Konteatis, Z.; Murtie, J.; Blake, M.L.; Travins, J.; Dorsch, M.; Biller, S.A.; Marks, K.M. MTAP Deletions in cancer create vulnerability to targeting of the MAT2A/PRMT5/RIOK1 axis. Cell Rep., 2016, 15(3), 574-587.
[http://dx.doi.org/10.1016/j.celrep.2016.03.043] [PMID: 27068473]

Hsu, M-C.; Pan, M-R.; Chu, P-Y.; Tsai, Y-L.; Tsai, C-H.; Shan, Y-S.; Chen, L.T.; Hung, W.C. Protein Arginine methyltransferase 3 enhances chemoresistance in pancreatic cancer by methylating hnRNPA1 to increase ABCG2 expression. Cancers (Basel), 2018, 11(1), 8.
[http://dx.doi.org/10.3390/cancers11010008] [PMID: 30577570]

Cheng, D.; Vemulapalli, V.; Lu, Y.; Shen, J.; Aoyagi, S.; Fry, C.J.; Yang, Y.; Foulds, C.E.; Stossi, F.; Treviño, L.S.; Mancini, M.A.; O’Malley, B.W.; Walker, C.L.; Boyer, T.G.; Bedford, M.T. CARM1 methylates MED12 to regulate its RNA-binding ability. Life Sci. Alliance, 2018, 1(5)e201800117
[http://dx.doi.org/10.26508/lsa.201800117] [PMID: 30456381]

Waldmann, T.; Izzo, A.; Kamieniarz, K.; Richter, F.; Vogler, C.; Sarg, B.; Lindner, H.; Young, N.L.; Mittler, G.; Garcia, B.A.; Schneider, R. Methylation of H2AR29 is a novel repressive PRMT6 target. Epigenetics Chromatin, 2011, 4(1), 11.
[http://dx.doi.org/10.1186/1756-8935-4-11] [PMID: 21774791]

Li, M.; An, W.; Xu, L.; Lin, Y.; Su, L.; Liu, X. The arginine methyltransferase PRMT5 and PRMT1 distinctly regulate the degradation of anti-apoptotic protein CFLARL in human lung cancer cells. J. Exp. Clin. Cancer Res., 2019, 38(1), 64.
[http://dx.doi.org/10.1186/s13046-019-1064-8] [PMID: 30736843]

Mersaoui, S.Y.; Yu, Z.; Coulombe, Y.; Karam, M.; Busatto, F.F.; Masson, J-Y.; Richard, S. Arginine methylation of the DDX5 helicase RGG/RG motif by PRMT5 regulates resolution of RNA:DNA hybrids. EMBO J., 2019, 38(15)e100986
[http://dx.doi.org/10.15252/embj.2018100986] [PMID: 31267554]

Yang, Y.; Hadjikyriacou, A.; Xia, Z.; Gayatri, S.; Kim, D.; Zurita-Lopez, C.; Kelly, R.; Guo, A.; Li, W.; Clarke, S.G.; Bedford, M.T. PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145. Nat. Commun., 2015, 6(1), 6428.
[http://dx.doi.org/10.1038/ncomms7428] [PMID: 25737013]

Jeong, H-J.; Lee, S-J.; Lee, H-J.; Kim, H-B.; Anh Vuong, T.; Cho, H.; Bae, G.U.; Kang, J.S. PRMT7 Promotes Myoblast Differentiation Via Methylation Of P38mapk On Arginine Residue 70. Cell Death Differ., 2020, 27(2), 573-586.
[http://dx.doi.org/10.1038/s41418-019-0373-y] [PMID: 31243342]

Haghandish, N.; Baldwin, R.M.; Morettin, A.; Dawit, H.T.; Adhikary, H.; Masson, J-Y.; Mazroui, R.; Trinkle-Mulcahy, L.; Côté, J. PRMT7 methylates eukaryotic translation initiation factor 2α and regulates its role in stress granule formation. Mol. Biol. Cell, 2019, 30(6), 778-793.
[http://dx.doi.org/10.1091/mbc.E18-05-0330] [PMID: 30699057]

Baldwin, R.M.; Haghandish, N.; Daneshmand, M.; Amin, S.; Paris, G.; Falls, T.J.; Bell, J.C.; Islam, S.; Côté, J. Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression. Oncotarget, 2015, 6(5), 3013-3032.
[http://dx.doi.org/10.18632/oncotarget.3072] [PMID: 25605249]