Editorial: Epigenetic therapy: Targeting histones and their modifications in human disease

Future Medicinal Chemistry

Volumn 2, Issue 4, 2010, Pages 543-548

  Gunjan, Akash ^a   Singh, Rakesh Kumar ^b  

^a FLORIDA STATE UNIVERSITY COLLEGE OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE; HISTONE DEACETYLASE; RESVERATROL; ROMIDEPSIN; SIRTUIN; VALPROIC ACID; VORINOSTAT;

ACETYLATION; BIPOLAR DISORDER; CHROMATIN; CLINICAL RESEARCH; CUTANEOUS T CELL LYMPHOMA; DNA METHYLATION; EDITORIAL; EPIGENETICS; EPILEPSY; FOOD AND DRUG ADMINISTRATION; GENE THERAPY; GENERAL ASPECTS OF DISEASE; HUMAN; METABOLIC DISORDER; METABOLIC SYNDROME X; MIGRAINE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; PRIORITY JOURNAL; PROPHYLAXIS; PROTEIN MODIFICATION; SCHIZOPHRENIA; DRUG DEVELOPMENT; GENETIC EPIGENESIS; GENETICS; METABOLISM;

DISEASE; DRUG DISCOVERY; EPIGENESIS, GENETIC; HISTONES; HUMANS;

EID: 77953428840     PISSN: 17568919     EISSN: None     Source Type: Journal    
DOI: 10.4155/fmc.10.18     Document Type: Editorial

References (57)

1. Kossel A. Ueber einen peptonartigen Bestandtheil des Zellkerns. Hoppe-Seyler's Z Physiol. Chem. 8, 511-515 (1884).
2. Rando OJ, Chang HY. Genome-wide views of chromatin structure. Annu. Rev. Biochem. 78, 245-271 (2009).
3. Strahl BD, Allis CD. The language of covalent histone modifications. Nature 403(6765), 41-45 (2000).
4. Suganuma T, Workman JL. Crosstalk among histone modifications. Cell 135(4), 604-607 (2008).
5. Thomas NR. Histone post-translational modification: from discovery to the clinic. IDrugs 9(6), 398-401 (2006).
6. Shahbazian MD, Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 76, 75-100 (2007).
7. Rosenberg G. The mechanisms of action of valproate in neuropsychiatric disorders: can we see the forest for the trees? Cell Mol. Life Sci. 64(16), 2090-2103 (2007).
8. Bolden JE, Peart MJ, Johnstone RW. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 5(9), 769-784 (2006).
9. Haigis MC, Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295 (2010).
10. Milne JC, Lambert PD, Schenk S et al. Small-molecule activators of SIRT1 as therapeutics for the treatment of Type 2 diabetes. Nature 450(7170), 712-716 (2007).
11. Baur JA, Sinclair DA. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev. Drug Discov. 5(6), 493-506 (2006).
12. Guarente L. Sirtuins as potential targets for metabolic syndrome. Nature 444(7121), 868-874 (2006).
13. Westphal CH, Dipp MA, Guarente L. A therapeutic role for sirtuins in diseases of aging? Trends Biochem. Sci. 32(12), 555-560 (2007).
14. Petrij F, Giles RH, Dauwerse HG et al. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 376(6538), 348-351(1995).
15. Sakakura C, Hagiwara A, Yasuoka R et al. Amplification and over-expression of the AIB1 nuclear receptor co-activator gene in primary gastric cancers. Int. J. Cancer 89(3), 217-223 (2000).
16. Panagopoulos I, Fioretos T, Isaksson M et al. Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum. Mol. Genet. 10(4), 395-404 (2001).
17. Gayther SA, Batley SJ, Linger L et al. Mutations truncating the EP300 acetylase in human cancers. Nat. Genet. 24(3), 300-303 (2000).
18. Muraoka M, Konishi M, Kikuchi-Yanoshita R et al. p300 gene alterations in colorectal and gastric carcinomas. Oncogene 12(7), 1565-1569 (1996).
19. Eliseeva ED, Valkov V, Jung M, Jung MO. Characterization of novel inhibitors of histone acetyltransferases. Mol. Cancer Ther. 6(9), 2391-2398 (2007).
20. Lachner M, Jenuwein T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14(3), 286-298 (2002).
21. Kouzarides T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12(2), 198-209 (2002).
22. Schübeler D, MacAlpine DM, Scalzo D et al. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev. 18(11), 1263-1271 (2004).
23. Rice JC, Briggs SD, Ueberheide B et al. Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains. Mol. Cell 12(6), 1591-1598 (2003).
24. Schotta G, Lachner M, Sarma K et al. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18(11), 1251-1262 (2004).
25. Lachner M, Sengupta R, Schotta G, Jenuwein T. Trilogies of histone lysine methylation as epigenetic landmarks of the eukaryotic genome. Cold Spring Harb. Symp. Quant. Biol. 69, 209-218 (2004).
26. Wiencke JK, Zheng S, Morrison Z, Yeh RF. Differentially expressed genes are marked by histone 3 lysine 9 trimethylation in human cancer cells. Oncogene 27(17), 2412-2421 (2008).
27. Copeland RA, Solomon ME, Richon VM. Protein methyltransferases as a target class for drug discovery. Nat. Rev. Drug Discov. 8(9), 724-732 (2009).
28. Qian C, Zhou MM. SET domain protein lysine methyltransferases: structure, specificity and catalysis. Cell Mol. Life Sci. 63(23), 2755-2763 (2006).
29. Krause CD, Yang ZH, Kim YS, Lee JH, Cook JR, Pestka S. Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 113(1), 50-87 (2007).
30. Greiner D, Bonaldi T, Eskeland R, Roemer E, Imhof A. Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat. Chem. Biol. 1(3), 143-145 (2005).
31. Kubicek S, O'Sullivan RJ, August EM et al. Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol. Cell 25(3), 473-481 (2007).
32. Spannhoff A, Heinke R, Bauer I et al. Target-based approach to inhibitors of histone arginine methyltransferases. J. Med. Chem. 50(10), 2319-2325 (2007).
33. Byvoet P, Shepherd GR, Hardin JM, Noland BJ. The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells. Arch. Biochem. Biophys. 148(2), 558-567 (1972).
34. Thomas G, Lange HW, Hempel K. Relative stability of lysine-bound methyl groups in arginie-rich histones and their subfrations in Ehrlich ascites tumor cells in vitro. Hoppe Seylers Z Physiol. Chem. 353(9), 1423-1428 (1972).
35. Shi Y, Lan F, Matson C et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119(7), 941-953 (2004).
36. Shi Y. Histone lysine demethylases: emerging roles in development, physiology and disease. Nat. Rev. Genet. 8(11), 829-833 (2007).
37. Huang Y, Greene E, Murray Stewart T et al. Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes. Proc. Natl Acad. Sci. USA 104(19), 8023-8028 (2007).
38. Huang Y, Stewart TM, Wu Y et al. Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes. Clin. Cancer Res. 15(23), 7217-7228 (2009).
39. Goldknopf IL, Busch H. Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24. Proc. Natl Acad. Sci. USA 74(3), 864-868 (1977).
40. Hershko A, Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67, 425-479 (1998).
41. Jason LJ, Moore SC, Lewis JD, Lindsey G, Ausió J. Histone ubiquitination: a tagging tail unfolds? Bioessays 24(2), 166-174 (2002).
42. Nakanishi S, Lee JS, Gardner KE et al. Histone H2BK123 monoubiquitination is the critical determinant for H3K4 and H3K79 trimethylation by COMPASS and Dot1. J. Cell Biol. 186(3), 371-377 (2009).
43. Wang H, Zhai L, Xu J et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell 22(3), 383-394 (2006).
44. Geng F, Tansey WP. Polyubiquitylation of histone H2B. Mol. Biol. Cell 19(9), 3616-3624 (2008).
45. Gunjan A, Verreault A. A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 115(5), 537-549 (2003).
46. Singh RK, Kabbaj MH, Paik J, Gunjan A. Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat. Cell Biol. 11(8), 925-933 (2009).
47. Singh RK, Liang D, Reddy GU, Paik J, Gunjan A. Excess histone levels mediate cytotoxicity via multiple mechanisms. Cell Cycle (2010) (In Press).
48. Antoni L, Sodha N, Collins I, Garrett MD. CHK2 kinase: cancer susceptibility and cancer therapy - two sides of the same coin? Nat. Rev. Cancer 7(12), 925-936 (2007).
49. Liu Z, Oughtred R, Wing SS. Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones. Mol. Cell Biol. 25(7), 2819-2831 (2005).
50. Confalonieri S, Quarto M, Goisis G et al. Alterations of ubiquitin ligases in human cancer and their association with the natural history of the tumor. Oncogene 28(33), 2959-2968 (2009).
51. Chen D, Brooks CL, Gu W. ARF-BP1 as a potential therapeutic target. Br. J. Cancer 94(11), 1555-1558 (2006).
52. Blagosklonny MV. Overcoming limitations of natural anticancer drugs by combining with artificial agents. Trends Pharmacol. Sci. 26(2), 77-81 (2005).
53. Hirsch JG. Bactericidal action of histone. J. Exp. Med. 108(6), 925-944 (1958).
54. Xu J, Zhang X, Pelayo R et al. Extracellular histones are major mediators of death in sepsis. Nat. Med. 15(11), 1318-1321 (2009).
55. Burlingame RW, Rubin RL. Drug-induced anti-histone autoantibodies display two patterns of reactivity with substructures of chromatin. J. Clin. Invest. 88(2), 680-690 (1991).
56. Barski A, Cuddapah S, Cui K et al. High-resolution profiling of histone methylations in the human genome. Cell 129(4), 823-837 (2007).
57. Mikkelsen TS, Ku M, Jaffe DB et al. Genome-wide maps of chromatin state in pluripotent and lineage-committed cells. Nature 448(7153), 553-560 (2007).