Please wait a minute...
 Home  About the Journal Editorial Board Aims & Scope Peer Review Policy Subscription Contact us
 
Early Edition  //  Current Issue  //  Open Special Issues  //  Archives  //  Most Read  //  Most Downloaded  //  Most Cited
Aging and disease
Orginal Article |
An updated review of the epigenetic mechanism underlying the pathogenesis of age-related macular degeneration
Xiaohua Li1,2,3,4, Shikun He1,2,3,4,5,*, Mingwei Zhao6,*
1Henan Provincial People’s Hospital, Zhengzhou, China.
2Henan Eye Hospital, Henan Eye Institute, Henan Key Laboratory of Ophthalmology and Visual Science, Zhengzhou, China.
3People’s Hospital of Zhengzhou University, Zhengzhou, China.
4People’s Hospital of Henan University, Zhengzhou, China.
5Departments of Pathology and Ophthalmology, Keck School of Medicine of the University of Southern California, Los Angeles, CA, USA.
6Ophthalmology Optometry Centre, Peking University People’s Hospital, Beijing Key Laboratory of Diagnosis and Therapy of Retinal and Choroid Diseases, Beijing, China.
Download: PDF(786 KB)   HTML
Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks    
Abstract  

Epigenetics has been recognized to play an important role in physiological and pathological processes of the human body. Accumulating evidence has indicated that epigenetic mechanisms contribute to the pathogenesis of age-related macular degeneration (AMD). Although the susceptibility related to genetic variants has been revealed by genome-wide association studies, those genetic variants may predict AMD risk only in certain human populations. Other mechanisms, particularly those involving epigenetic factors, may play an important role in the pathogenesis of AMD. Therefore, we briefly summarize the most recent reports related to such epigenetic mechanisms, including DNA methylation, histone modification, and non-coding RNA, and the interplay of genetic and epigenetic factors in the pathogenesis of AMD.

Keywords age-related macular degeneration      epigenetics      single nucleotide polymorphisms     
Corresponding Authors: Shikun He,Mingwei Zhao   
Just Accepted Date: 05 December 2019  
Service
E-mail this article
E-mail Alert
RSS
Articles by authors
Xiaohua Li
Shikun He
Mingwei Zhao
Cite this article:   
Xiaohua Li,Shikun He,Mingwei Zhao. An updated review of the epigenetic mechanism underlying the pathogenesis of age-related macular degeneration[J]. Aging and disease, 10.14336/AD.2019.1126
URL:  
http://www.aginganddisease.org/EN/10.14336/AD.2019.1126     OR     http://www.aginganddisease.org/EN/Y/V/I/0
Figure 1.  Inhibition of CNV by TSA may involve multiple mechanisms: (1) Suppression of HIF1α and inflammatory cytokines as well as VEGF expression; (2) Inhibition of the phosphorylation of VEGF receptor 2 induced by VEGF; (3) Inhibition of activation of MAPK; (4) Upregulation of the expression of the anti-angiogenesis factor PEDF. CNV, choroidal neovascularization; TSA, trichostatin A.
Figure 2.  Function of SIRT1. Biological functions of Sirt1 are broad, ranging from aging, anti-oxidative protection of cells, inhibition of inflammation, angiogenesis, and fibrosis, and tumorigenesis suppression.
Figure 3.  Resveratrol inhibits experimental CNV.Resveratrol inhibits VEGF receptor 2 phosphorylation (P-VEGF-R2) in mice with a choroidal neovascular (CNV) lesion induced by laser, as showed by immunofluorescence. Green indicates positive staining of P-VEGF-R2 and red is propidium iodide (PI) staining. Yellow represents double labeling. the P-VEGF-R2 staining is considerably reduced in mice with a CNV lesion after resveratrol application (square). Original magnification ×400.
Figure 4.  Relevance of RNA methylation to cellular processes. RNA methylation may impact various cellular processes, including cell differentiation, proliferation, migration metabolism, and regulation of inflammation, the immune response, hypoxia, and tumorigenesis.
Figure 5.  The role of epigenetic factors in the pathogenesis of AMD. Interaction among environmental, genetic, and epigenetic factors may determine initiation of the pathogenesis of AMD. Environmental factors may contribute to the alteration of epigenetic factors, changes in epigenetic mechanisms may induce abnormal gene expression through crosstalk with the genome. On the other hand, genetic alterations, such as single nucleotide polymorphisms, may affect epigenetic factors. Furthermore, there is an interplay among epigenetic regulation pathways, suggesting that AMD is a complex disease. An aberration of genome transcription that is related to AMD is regulated by both genetic and epigenetic factors.
[1] Yonekawa Y, Miller JW, Kim IK (2015). Age-Related Macular Degeneration: Advances in Management and Diagnosis. J Clin Med, 4:343-359.
[2] Meyers KJ, Liu Z, Millen AE, Iyengar SK, Blodi BA, Johnson E, et al. (2015). Joint Associations of Diet, Lifestyle, and Genes with Age-Related Macular Degeneration. Ophthalmology, 122:2286-2294.
[3] van Lookeren Campagne M, LeCouter J, Yaspan BL, Ye W (2014). Mechanisms of age-related macular degeneration and therapeutic opportunities. J Pathol, 232:151-164.
[4] Chen Y, Bedell M, Zhang K (2010). Age-related macular degeneration: genetic and environmental factors of disease. Mol Interv, 10:271-281.
[5] Mousavi M, Armstrong RA (2013). Genetic risk factors and age-related macular degeneration (AMD). Journal of Optometry, 6:176-184.
[6] Miyake M, Yamashiro K, Tamura H, Kumagai K, Saito M, Sugahara-Kuroda M, et al. (2015). The Contribution of Genetic Architecture to the 10-Year Incidence of Age-Related Macular Degeneration in the Fellow Eye. Invest Ophthalmol Vis Sci, 56:5353-5361.
[7] Fritsche LG, Chen W, Schu M, Yaspan BL, Yu Y, Thorleifsson G, et al. (2013). Seven new loci associated with age-related macular degeneration. Nat Genet, 45:433-439, 439e431-432.
[8] Thakkinstian A, Han P, McEvoy M, Smith W, Hoh J, Magnusson K, et al. (2006). Systematic review and meta-analysis of the association between complement factor H Y402H polymorphisms and age-related macular degeneration. Hum Mol Genet, 15:2784-2790.
[9] Yasuma TR, Nakamura M, Nishiguchi KM, Kikuchi M, Kaneko H, Niwa T, et al. (2010). Elevated C-reactive protein levels and ARMS2/HTRA1 gene variants in subjects without age-related macular degeneration. Mol Vis, 16:2923-2930.
[10] Lin MK, Yang J, Hsu CW, Gore A, Bassuk AG, Brown LM, et al. (2018). HTRA1, an age-related macular degeneration protease, processes extracellular matrix proteins EFEMP1 and TSP1. Aging Cell, 17: e12710.
[11] Millen AE, Meyers KJ, Liu Z, Engelman CD, Wallace RB, LeBlanc ES, et al. (2015). Association between vitamin D status and age-related macular degeneration by genetic risk. JAMA Ophthalmol, 133:1171-1179.
[12] Vladan B, Biljana SP, Mandusic V, Zorana M, Zivkovic L (2013). Instability in X chromosome inactivation patterns in AMD: a new risk factor? Med Hypothesis Discov Innov Ophthalmol, 2:74-82.
[13] Yuan D, Yuan D, Liu X, Yuan S, Xie P, Liu Q (2013). Genetic association with response to intravitreal ranibizumab for neovascular age-related macular degeneration in the Han Chinese population. Ophthalmologica, 230:227-232.
[14] Zhang S, Liu Y, Lu S, Cai X (2015). Genetic variants of interleukin 17A are functionally associated with increased risk of age-related macular degeneration. Inflammation, 38:658-663.
[15] Liang XY, Lai TY, Liu DT, Fan AH, Chen LJ, Tam PO, et al. (2012). Differentiation of exudative age-related macular degeneration and polypoidal choroidal vasculopathy in the ARMS2/HTRA1 locus. Invest Ophthalmol Vis Sci, 53:3175-3182.
[16] Liang XY, Chen LJ, Ng TK, Tuo J, Gao JL, Tam PO, et al. (2014). FPR1 interacts with CFH, HTRA1 and smoking in exudative age-related macular degeneration and polypoidal choroidal vasculopathy. Eye (Lond), 28:1502-1510.
[17] Liu K, Chen LJ, Tam PO, Shi Y, Lai TY, Liu DT, et al. (2013). Associations of the C2-CFB-RDBP-SKIV2L locus with age-related macular degeneration and polypoidal choroidal vasculopathy. Ophthalmology, 120:837-843.
[18] Zhang X, Li M, Wen F, Zuo C, Chen H, Wu K, et al. (2013). Different impact of high-density lipoprotein-related genetic variants on polypoidal choroidal vasculopathy and neovascular age-related macular degeneration in a Chinese Han population. Exp Eye Res, 108:16-22.
[19] Ji Y, Zhang X, Wu K, Su Y, Li M, Zuo C, et al. (2014). Association of rs6982567 near GDF6 with neovascular age-related macular degeneration and polypoidal choroidal vasculopathy in a Han Chinese cohort. BMC Ophthalmol, 14:140.
[20] Yanagisawa S, Sakurada Y, Miki A, Matsumiya W, Imoto I, Honda S (2015). The association of elastin gene variants with two angiographic subtypes of polypoidal choroidal vasculopathy. PLoS One, 10: e0120643.
[21] SanGiovanni JP, Chew EY (2014). Clinical applications of age-related macular degeneration genetics. Cold Spring Harb Perspect Med, 4.
[22] Suuronen T, Nuutinen T, Ryhanen T, Kaarniranta K, Salminen A (2007). Epigenetic regulation of clusterin/apolipoprotein J expression in retinal pigment epithelial cells. Biochem Biophys Res Commun, 357:397-401.
[23] Seddon JM, Reynolds R, Shah HR, Rosner B (2011). Smoking, dietary betaine, methionine, and vitamin D in monozygotic twins with discordant macular degeneration: epigenetic implications. Ophthalmology, 118:1386-1394.
[24] Hunter A, Spechler PA, Cwanger A, Song Y, Zhang Z, Ying G-s, et al. (2012). DNA Methylation Is Associated with Altered Gene Expression in AMD. Investigative Opthalmology & Visual Science, 53:2089-2105.
[25] Wei L, Liu B, Tuo J, Shen D, Chen P, Li Z, et al. (2012). Hypomethylation of the IL17RC promoter associates with age-related macular degeneration. Cell Rep, 2:1151-1158.
[26] Oliver VF, Jaffe AE, Song J, Wang G, Zhang P, Branham KE, et al. (2015). Differential DNA methylation identified in the blood and retina of AMD patients. Epigenetics, 10:698-707.
[27] Koks G, Uudelepp ML, Limbach M, Peterson P, Reimann E, Koks S (2015). Smoking-induced expression of the GPR15 gene indicates its potential role in chronic inflammatory pathologies. Am J Pathol, 185:2898-2906.
[28] Arjamaa O, Nikinmaa M, Salminen A, Kaarniranta K (2009). Regulatory role of HIF-1alpha in the pathogenesis of age-related macular degeneration (AMD). Ageing Res Rev, 8:349-358.
[29] Cascella R, Strafella C, Caputo V, Errichiello V, Zampatti S, Milano F, et al. (2018). Towards the application of precision medicine in Age-Related Macular Degeneration. Prog Retin Eye Res, 63:132-146.
[30] Porter LF, Saptarshi N, Fang Y, Rathi S, den Hollander AI, de Jong EK, et al. (2019). Whole-genome methylation profiling of the retinal pigment epithelium of individuals with age-related macular degeneration reveals differential methylation of the SKI, GTF2H4, and TNXB genes. Clin Epigenetics, 11:6.2-14
[31] Kim MS, Kwon HJ, Lee YM, Baek JH, Jang JE, Lee SW, et al. (2001). Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. Nat Med, 7:437-443.
[32] Ponnaluri VK, Vadlapatla RK, Vavilala DT, Pal D, Mitra AK, Mukherji M (2011). Hypoxia induced expression of histone lysine demethylases: implications in oxygen-dependent retinal neovascular diseases. Biochem Biophys Res Commun, 415:373-377.
[33] To M, Yamamura S, Akashi K, Charron CE, Haruki K, Barnes PJ, et al. (2012). Defect of adaptation to hypoxia in patients with COPD due to reduction of histone deacetylase 7. Chest, 141:1233-1242.
[34] Wang S, Li X, Parra M, Verdin E, Bassel-Duby R, Olson EN (2008). Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7. Proc Natl Acad Sci U S A, 105:7738-7743.
[35] Hsing CH, Hung SK, Chen YC, Wei TS, Sun DP, Wang JJ, et al. (2015). Histone Deacetylase Inhibitor Trichostatin A Ameliorated Endotoxin-Induced Neuroinflammation and Cognitive Dysfunction. Mediators Inflamm, 2015:163140.
[36] Deroanne CF, Bonjean K, Servotte S, Devy L, Colige A, Clausse N, et al. (2002). Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. Oncogene, 21:427-436.
[37] Hrgovic I, Doll M, Pinter A, Kaufmann R, Kippenberger S, Meissner M (2017). Histone deacetylase inhibitors interfere with angiogenesis by decreasing endothelial VEGFR-2 protein half-life in part via a VE-cadherin-dependent mechanism. Exp Dermatol, 26:194-201.
[38] Xing Y, Tu J, Zhang L, Guo L, Xi T (2015). Anti-angiogenic effect of tanshinone IIA involves inhibition of the VEGF/VEGFR2 pathway in vascular endothelial cells. Oncol Rep, 33:163-170.
[39] https://patents.google.com/patent/WO2004043352A2 #patentCitations MXPA05004485A *2002-11-122005-1123- Alcon Inc. Histone deacetylase inhibitors for the treatment of ocular neovascular or edematous disorders and diseases.
[40] Gnana-Prakasam JP, Veeranan-Karmegam R, Coothankandaswamy V, Reddy SK, Martin PM, Thangaraju M, et al. (2013). Loss of Hfe leads to progression of tumor phenotype in primary retinal pigment epithelial cells. Invest Ophthalmol Vis Sci, 54:63-71.
[41] Chan N, He S, Spee CK, Ishikawa K, Hinton DR (2015). Attenuation of choroidal neovascularization by histone deacetylase inhibitor. PLoS One, 10:e0120587.
[42] Crosson CE, Mani SK, Husain S, Alsarraf O, Menick DR (2010). Inhibition of histone deacetylase protects the retina from ischemic injury. Invest Ophthalmol Vis Sci, 51:3639-3645.
[43] Poulose N, Raju R (2015). Sirtuin regulation in aging and injury. Biochim Biophys Acta, 1852:2442-2455.
[44] Tucci P (2012). Caloric restriction: is mammalian life extension linked to p53? Aging (Albany NY), 4:525-534.
[45] Kojiro Nakamura, Min Zhang, Shoichi Kageyama, et al. (2017). Macrophage heme oxygenase-1-SIRT1-p53 axis regulates sterile inflammation in liver ischemia-reperfusion injury. J Hepatol, 67(6): 1232-1242.
[46] Seo JS, Moon MH, Jeong JK, Seol JW, Lee YJ, Park BH, et al. (2012). SIRT1, a histone deacetylase, regulates prion protein-induced neuronal cell death. Neurobiol Aging, 33:1110-1120.
[47] Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, Pandita TK, et al. (2001). hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell, 107:149-159.
[48] Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, Lin Y, et al. (2004). Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science, 303:2011-2015.
[49] Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye RA, et al. (2004). Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. Embo J, 23:2369-2380.
[50] Wang C, Chen L, Hou X, Li Z, Kabra N, Ma Y, et al. (2006). Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol, 8:1025-1031.
[51] Tan L, Yu JT, Guan HS (2008). Resveratrol exerts pharmacological preconditioning by activating PGC-1alpha. Med Hypotheses, 71:664-667.
[52] Lim JH, Lee YM, Chun YS, Chen J, Kim JE, Park JW (2010). Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol Cell, 38:864-878.
[53] Dioum EM, Chen R, Alexander MS, Zhang Q, Hogg RT, Gerard RD, et al. (2009). Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science, 324:1289-1293.
[54] Peng CH, Cherng JY, Chiou GY, Chen YC, Chien CH, Kao CL, et al. (2011). Delivery of Oct4 and SirT1 with cationic polyurethanes-short branch PEI to aged retinal pigment epithelium. Biomaterials, 32:9077-9088.
[55] Maloney SC, Antecka E, Granner T, Fernandes B, Lim LA, Orellana ME, et al. (2013). Expression of SIRT1 in choroidal neovascular membranes. Retina, 33:862-866.
[56] Zhuge CC, Xu JY, Zhang J, Li W, Li P, Li Z, et al. (2014). Fullerenol protects retinal pigment epithelial cells from oxidative stress-induced premature senescence via activating SIRT1. Invest Ophthalmol Vis Sci, 55:4628-4638.
[57] Wei W, Li L, Zhang Y, Geriletu, Yang J, Zhang Y, et al. (2014). Vitamin C protected human retinal pigmented epithelium from oxidant injury depending on regulating SIRT1. Scientific World Journal, 2014:750634.
[58] Li L, Wei W, Zhang Y, Tu G, Zhang Y, Yang J, et al. (2015). SirT1 and STAT3 protect retinal pigmented epithelium cells against oxidative stress. Mol Med Rep, 12:2231-2238.
[59] Richer S, Patel S, Sockanathan S, Ulanski LJ, 2nd, Miller L, Podella C (2014). Resveratrol based oral nutritional supplement produces long-term beneficial effects on structure and visual function in human patients. Nutrients, 6:4404-4420.
[60] Turner RS, Thomas RG, Craft S, van Dyck CH, Mintzer J, Reynolds BA, et al. (2015). A randomized, double-blind, placebo-controlled trial of resveratrol for Alzheimer disease. Neurology, 85:1383-1391.
[61] Zhang H, He S, Spee C, Ishikawa K, Hinton DR (2015). SIRT1 mediated inhibition of VEGF/VEGFR2 signaling by Resveratrol and its relevance to choroidal neovascularization. Cytokine, 76:549-552.
[62] Karali M, Persico M, Mutarelli M, Carissimo A, Pizzo M, Singh Marwah V, et al. (2016). High-resolution analysis of the human retina miRNome reveals isomiR variations and novel microRNAs. Nucleic Acids Res, 44:1525-1540.
[63] Li Y, Mao L, Gao Y, Baral S, Zhou Y, Hu B (2015). MicroRNA-107 contributes to post-stroke angiogenesis by targeting Dicer-1. Sci Rep, 5:13316.
[64] Askou AL, Alsing S, Holmgaard A, Bek T, Corydon TJ (2018). Dissecting microRNA dysregulation in age-related macular degeneration: new targets for eye gene therapy. Acta Ophthalmol, 96:9-23.
[65] Lin H, Qian J, Castillo AC, Long B, Keyes KT, Chen G, et al. (2011). Effect of miR-23 on oxidant-induced injury in human retinal pigment epithelial cells. Invest Ophthalmol Vis Sci, 52:6308-6314.
[66] Lukiw WJ, Surjyadipta B, Dua P, Alexandrov PN (2012). Common micro RNAs (miRNAs) target complement factor H (CFH) regulation in Alzheimer's disease (AD) and in age-related macular degeneration (AMD). Int J Biochem Mol Biol, 3:105-116.
[67] Sabatel C, Malvaux L, Bovy N, Deroanne C, Lambert V, Gonzalez ML, et al. (2011). MicroRNA-21 exhibits antiangiogenic function by targeting RhoB expression in endothelial cells. PLoS One, 6:e16979.
[68] Kaneko H, Dridi S, Tarallo V, Gelfand BD, Fowler BJ, Cho WG, et al. (2011). DICER1 deficit induces Alu RNA toxicity in age-related macular degeneration. Nature, 471:325-330.
[69] Saxena K, Rutar MV, Provis JM, Natoli RC (2015). Identification of miRNAs in a Model of Retinal Degenerations. Invest Ophthalmol Vis Sci, 56:1820-1829.
[70] Strafella C, Errichiello V, Caputo V, Aloe G, Ricci F, Cusumano A, et al. (2019). The Interplay between miRNA-Related Variants and Age-Related Macular Degeneration: EVIDENCE of Association of MIR146A and MIR27A. Int J Mol Sci, 20: pii: E1578
[71] Lasser C (2012). Exosomal RNA as biomarkers and the therapeutic potential of exosome vectors. Expert Opin Biol Ther, 12 Suppl 1:S189-197.
[72] Grassmann F, Schoenberger PG, Brandl C, Schick T, Hasler D, Meister G, et al. (2014). A circulating microrna profile is associated with late-stage neovascular age-related macular degeneration. PLoS One, 9:e107461.
[73] Szemraj M, Bielecka-Kowalska A, Oszajca K, Krajewska M, Gos R, Jurowski P, et al. (2015). Serum MicroRNAs as Potential Biomarkers of AMD. Med Sci Monit, 21:2734-2742.
[74] Ren C, Liu Q, Wei Q, Cai W, He M, Du Y, et al. (2017). Circulating miRNAs as Potential Biomarkers of Age-Related Macular Degeneration. Cell Physiol Biochem, 41:1413-1423.
[75] Menard C, Rezende FA, Miloudi K, Wilson A, Tetreault N, Hardy P, et al. (2016). MicroRNA signatures in vitreous humour and plasma of patients with exudative AMD. Oncotarget, 7:19171-19184.
[76] Zhu W, Meng YF, Xing Q, Tao JJ, Lu J, Wu Y (2017). Identification of lncRNAs involved in biological regulation in early age-related macular degeneration. Int J Nanomedicine, 12:7589-7602.
[77] Chen X, Jiang C, Qin B, Liu G, Ji J, Sun X, et al. (2017). LncRNA ZNF503-AS1 promotes RPE differentiation by downregulating ZNF503 expression. Cell Death Dis, 8:e3046.
[78] Sivagurunathan S, Srikakulam N, Arunachalam JP, Pandi G, Chidambaram S (2018). In silico analysis of piRNAs in retina reveals potential targets in intracellular transport and retinal degeneration. bioRxiv:305144.
[79] Yang Y, Hsu PJ, Chen YS, Yang YG (2018). Dynamic transcriptomic m(6)A decoration: writers, erasers, readers and functions in RNA metabolism. Cell Res, 28:616-624.
[80] Vu LP, Cheng Y, Kharas MG (2019). The Biology of m(6)A RNA Methylation in Normal and Malignant Hematopoiesis. Cancer Discov, 9:25-33.
[81] Min KW, Zealy RW, Davila S, Fomin M, Cummings JC, Makowsky D, et al. (2018). Profiling of m6A RNA modifications identified an age-associated regulation of AGO2 mRNA stability. Aging Cell, 17:e12753.
[82] Chang G, Leu JS, Ma L, Xie K, Huang S (2019). Methylation of RNA N(6)-methyladenosine in modulation of cytokine responses and tumorigenesis. Cytokine, 118:35-41.
[83] Chang G, Leu JS, Ma L, Xie K, Huang S (2019). Methylation of RNA N(6)-methyladenosine in modulation of cytokine responses and tumorigenesis. Cytokine, 118:35-41.
[84] Shen F, Huang W, Huang JT, Xiong J, Yang Y, Wu K, et al. (2015). Decreased N(6)-methyladenosine in peripheral blood RNA from diabetic patients is associated with FTO expression rather than ALKBH5. J Clin Endocrinol Metab, 100:E148-154.
[85] Huang H, Wang H, Zhou K, Wu T, Zhao BS, Sun M, et al. (2019). Histone H3 trimethylation at lysine 36 guide m6A RNA modification co-transcriptionally. Nature, 567:414-419.
[86] Clyde D (2019). Regulation of RNA methylation by modified histones. Nat Rev Genet, 20:254-255.
[87] Frank-Bertoncelj M, Klein K, Gay S (2017). Interplay between genetic and epigenetic mechanisms in rheumatoid arthritis. Epigenomics, 9:493-504.
[88] Hajjari M, Rahnama S (2019). Association Between SNPs of Long Non-coding RNA HOTAIR and Risk of Different Cancers. Front Genet, 10:113.
[89] Farh KK, Marson A, Zhu J, Kleinewietfeld M, Housley WJ, Beik S, et al. (2015). Genetic and epigenetic fine mapping of causal autoimmune disease variants. Nature, 518:337-343.
[90] Guo H, Ahmed M, Zhang F, Yao CQ, Li S, Liang Y, et al. (2016). Modulation of long noncoding RNAs by risk SNPs underlying genetic predispositions to prostate cancer. Nat Genet, 48:1142-1150.
[91] Lee SM, Kim-Ha J, Choi WY, Lee J, Kim D, Lee J, et al. (2016). Interplay of genetic and epigenetic alterations in hepatocellular carcinoma. Epigenomics, 8:993-1005.
[92] Schulze K, Imbeaud S, Letouze E, Alexandrov LB, Calderaro J, Rebouissou S, et al. (2015). Exome sequencing of hepatocellular carcinomas identifies new mutational signatures and potential therapeutic targets. Nat Genet, 47:505-511.
[93] Nishida N, Goel A (2011). Genetic and epigenetic signatures in human hepatocellular carcinoma: a systematic review. Curr Genomics, 12:130-137.
[94] Tai DJ, Liu YC, Hsu WL, Ma YL, Cheng SJ, Liu SY, et al. (2016). MeCP2 SUMOylation rescues Mecp2-mutant-induced behavioural deficits in a mouse model of Rett syndrome. Nat Commun, 7:10552.
[95] Bannister AJ, Kouzarides T (2011). Regulation of chromatin by histone modifications. Cell Res, 21:381-395.
[96] anGiovanni JP, SanGiovanni PM, Sapieha P, De Guire V (2017). miRNAs, single nucleotide polymorphisms (SNPs) and age-related macular degeneration (AMD). Clin Chem Lab Med, 55:763-775.
[97] Kim EJ, Grant GR, Bowman AS, Haider N, Gudiseva HV, Chavali VRM (2018). Complete Transcriptome Profiling of Normal and Age-Related Macular Degeneration Eye Tissues Reveals Dysregulation of Anti-Sense Transcription. Sci Rep, 8:3040.
[98] Jones PA, Ohtani H, Chakravarthy A, De Carvalho DD (2019). Epigenetic therapy in immune-oncology. Nat Rev Cancer, 19:151-161.
[99] Moufarrij S, Dandapani M, Arthofer E, Gomez S, Srivastava A, Lopez-Acevedo M, et al (2019). Epigenetic therapy for ovarian cancer: promise and progress. Clinical Epigenetics, 11:7.
[100] Kwa FA, Thrimawithana TR (2014). Epigenetic modifications as potential therapeutic targets in age-related macular degeneration and diabetic retinopathy. Drug Discov Today, 19:1387-1393.
[101] Maugeri A, Barchitta M, Mazzone MG, Giuliano F, Basile G, Agodi A (2018). Resveratrol Modulates SIRT1 and DNMT Functions and Restores LINE-1 Methylation Levels in ARPE-19 Cells under Oxidative Stress and Inflammation. Int J Mol Sci, 19.
[102] He S, Barron E, Ishikawa K, Nazari Khanamiri H, Spee C, Zhou P, et al. (2015). Inhibition of DNA Methylation and Methyl-CpG-Binding Protein 2 Suppresses RPE Transdifferentiation: Relevance to Proliferative Vitreoretinopathy. Invest Ophthalmol Vis Sci, 56:5579-5589.
[103] Blanchard F, Chipoy C (2005). Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases? Drug Discov Today, 10:197-204.
[104] Bode KA, Schroder K, Hume DA, Ravasi T, Heeg K, Sweet MJ, et al. (2007). Histone deacetylase inhibitors decrease Toll-like receptor-mediated activation of proinflammatory gene expression by impairing transcription factor recruitment. Immunology, 122:596-606.
[105] Nencioni A, Beck J, Werth D, Grunebach F, Patrone F, Ballestrero A, et al. (2007). Histone deacetylase inhibitors affect dendritic cell differentiation and immunogenicity. Clin Cancer Res, 13:3933-3941.
[106] Suraweera A, O'Byrne KJ, Richard DJ (2018). Combination Therapy With Histone Deacetylase Inhibitors (HDACi) for the Treatment of Cancer: Achieving the Full Therapeutic Potential of HDACi. Front Oncol, 8:92.
[107] Fox CR, Parks GD (2019). Histone Deacetylase Inhibitors Enhance Cell Killing and Block Interferon-Beta Synthesis Elicited by Infection with an Oncolytic Parainfluenza Virus. Viruses, 11:pii:E431.
[108] Patnaik S, Anupriya (2019). Drugs Targeting Epigenetic Modifications and Plausible Therapeutic Strategies Against Colorectal Cancer. Front Pharmacol, 10:588.
[109] Nagai N, Kubota S, Tsubota K, Ozawa Y (2014). Resveratrol prevents the development of choroidal neovascularization by modulating AMP-activated protein kinase in macrophages and other cell types. J Nutr Biochem, 25:1218-1225.
[110] Ishida T, Yoshida T (2017). Potential role of sirtuin 1 in Muller glial cells in mice choroidal neovascularization. PLoS One, 12:e0183775.
[111] Chan N, He S, Spee CK, Ishikawa K, Hinton DR (2015). Attenuation of choroidal neovascularization by histone deacetylase inhibitor. PLoS One, 10:e0120587.
[112] Nagai N, Kubota S, Tsubota K, Ozawa Y (2014). Resveratrol prevents the development of choroidal neovascularization by modulating AMP-activated protein kinase in macrophages and other cell types. J Nutr Biochem, 25:1218-1225.
[113] Tanito M, Masutani H, Kim YC, Nishikawa M, Ohira A, Yodoi J (2005). Sulforaphane induces thioredoxin through the antioxidant-responsive element and attenuates retinal light damage in mice. Invest Ophthalmol Vis Sci, 46:979-987.
[114] Uchida H, Hayashi H, Kuroki M, Uno K, Yamada H, Yamashita Y, et al. (2005). Vitamin A up-regulates the expression of thrombospondin-1 and pigment epithelium-derived factor in retinal pigment epithelial cells. Exp Eye Res, 80:23-30.
[115] Feinberg AP (2010). Epigenomics reveals a functional genome anatomy and a new approach to common disease. Nat Biotechnol, 28:1049-1052.
[116] Wang Y, Han Y, Fan E, Zhang K (2015). Analytical strategies used to identify the readers of histone modifications: A review. Anal Chim Acta, 891:32-42.
[117] Atilano SR, Malik D, Chwa M, Caceres-Del-Carpio J, Nesburn AB, Boyer DS, et al. (2015). Mitochondrial DNA variants can mediate methylation status of inflammation, angiogenesis and signaling genes. Hum Mol Genet, 24:4491-4503.
[118] Fisher VA, Wang L, Deng X, Sarnowski C, Cupples LA, Liu CT. (2018). Do changes in DNA methylation mediate or interact with SNP variation? A pharmacoepigenetic analysis. BMC Genet,19(Suppl 1):70.
[119] Ventham NT, Kennedy NA, Adams AT, Kalla R, Heath S, O'Leary KR, et al. (2016). Integrative epigenome-wide analysis demonstrates that DNA methylation may mediate genetic risk in inflammatory bowel disease. Nat Commun, 7:13507.
[120] Binder S, Stanzel BV, Krebs I, Glittenberg C (2007). Transplantation of the RPE in AMD. Prog Retin Eye Res, 26:516-554.
[121] Mazur PK, Herner A, Mello SS, Wirth M, Hausmann S, Sanchez-Rivera FJ, et al. (2015). Combined inhibition of BET family proteins and histone deacetylases as a potential epigenetics-based therapy for pancreatic ductal adenocarcinoma. Nat Med, 21:1163-1171.
[122] Cheng Z, Gong Y, Ma Y, Lu K, Lu X, Pierce LA, et al. (2013). Inhibition of BET bromodomain targets genetically diverse glioblastoma. Clin Cancer Res, 19:1748-1759.
[123] Lim DA, Alvarez-Buylla A (2014). Adult neural stem cells stake their ground. Trends Neurosci, 37:563-571.
[124] Yong RL, Tsankova NM (2015). Emerging interplay of genetics and epigenetics in gliomas: a new hope for targeted therapy. Semin Pediatr Neurol, 22:14-22.
[1] Tidwell Tia R., Søreide Kjetil, Hagland Hanne R.. Aging, Metabolism, and Cancer Development: from Peto’s Paradox to the Warburg Effect[J]. Aging and disease, 2017, 8(5): 662-676.
[2] Zhao Haiping, Han Ziping, Ji Xunming, Luo Yumin. Epigenetic Regulation of Oxidative Stress in Ischemic Stroke[J]. Aging and disease, 2016, 7(3): 295-306.
[3] N. Nagineni Chandrasekharam, K. Kommineni Vijay, Ganjbaksh Nader, K. Nagineni Krishnasai, J. Hooks John, Detrick Barbara. Inflammatory Cytokines Induce Expression of Chemokines by Human Retinal Cells: Role in Chemokine Receptor Mediated Age-related Macular Degeneration[J]. Aging and disease, 2015, 6(6): 444-455.
[4] Vaiserman* Alexander. Early-life Exposure to Endocrine Disrupting Chemicals and Later-life Health Outcomes: An Epigenetic Bridge?[J]. Aging and Disease, 2014, 5(6): 419-429.
[5] Karen L. Saban,Herbert L. Mathews,Holli A. DeVon,Linda W. Janusek. Epigenetics and Social Context: Implications for Disparity in Cardiovascular Disease[J]. Aging and Disease, 2014, 5(5): 346-355.
[6] Chandrasekharam N. Nagineni,Raghavan Raju,Krishnasai K. Nagineni,Vijay K. Kommineni,Aswini Cherukuri,R. Krishnan Kutty,John J. Hooks,Barbara Detrick. Resveratrol Suppresses Expression of VEGF by Human Retinal Pigment Epithelial Cells: Potential Nutraceutical for Age-related Macular Degeneration[J]. Aging and Disease, 2014, 5(2): 88-100.
Viewed
Full text


Abstract

Cited

  Shared   
Copyright © 2014 Aging and Disease, All Rights Reserved.
Address: Aging and Disease Editorial Office 3400 Camp Bowie Boulevard Fort Worth, TX76106 USA
Fax: (817) 735-0408 E-mail: editorial@aginganddisease.org
Powered by Beijing Magtech Co. Ltd