Cellular Redox, Epigenetics and Diseases

Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 61)

Abstract

Since the Central dogma of Molecular Biology was proposed about 40 years ago; our understanding of the intricacies of gene regulation has undergone tectonic shifts almost every decade. It is now widely accepted that the complexity of an organism is not directed by the sheer number of genes it carries but how they are decoded by a myriad of regulatory modules. Over the years, it has emerged that the organizations chromatins and its remodeling; splicing and polyadenylation of pre-mRNAs, stability and localization of mRNAs and modulation of their expression by non-coding and miRNAs play pivotal roles in metazoan gene expression. Nevertheless, in spite of tremendous progress in our understanding of all these mechanisms of gene regulation, the way these events are coordinated leading towards a highly defined proteome of a given cell type remains enigmatic. In that context, the structures of many metazoan genes cannot fully explain their pattern of expression in different tissues, especially during embryonic development and progression of various diseases. Further, numerous studies done during the past quarter of a century suggested that the heritable states of transcriptional activation or repression of a gene can be influenced by the covalent modifications of constituent bases and associated histones; its chromosomal context and long-range interactions between various chromosomal elements (Holliday 1987; Turner 1998; Lyon 1993). However, molecular dissection of these phenomena is largely unknown and is an exciting topic of research under the sub-discipline epigenetics (Gasser et al. 1998).

Keywords

Epigenetic Regulation Cellular Redox Histone Methylation Cigarette Smoke Extract HDAC Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgement

This article is partly supported by the grant awarded to the author by the Council of Scientific and Industrial Research, Govt of India under sanction number 37(1479)/11/EMR II.

References

  1. Abate C, Patel L, Rauscher FJ 3rd, Curran T (1990) Redox regulation of fos and jun DNA-binding activity in vitro. Science 249:1157–1161PubMedCrossRefGoogle Scholar
  2. Antelmann H, Helmann JD (2011) Thiol-based redox switches and gene regulation. Antioxid Redox Signal 14:1049–1063PubMedCrossRefGoogle Scholar
  3. Avila MA, Corrales FJ, Ruiz F, Sánchez-Góngora E, Mingorance J, Carretero MV, Mato IM (1998) Specific interaction of methionine adenosyltransferase with free radicals. Biofactors 8:27–32PubMedCrossRefGoogle Scholar
  4. Bai H, Konat GW (2003) Hydrogen peroxide mediates higher order chromatin degradation. Neurochem Int 42:123–129PubMedCrossRefGoogle Scholar
  5. Banaszynski LA, Allis CD, Lewis PW (2010) Histone variants in metazoan development. Dev Cell 19:662–674PubMedCrossRefGoogle Scholar
  6. Banerjee S, Zmijewski JW, Lorne E, Liu G, Sha Y, Abraham E (2010) Modulation of SCF beta-TrCP-dependent I kappaB alpha ubiquitination by hydrogen peroxide. J Biol Chem 285:2665–2675PubMedCrossRefGoogle Scholar
  7. Barnes PJ (2009) Histone deacetylase-2 and airway disease. Ther Adv Respir Dis 3:235–243PubMedCrossRefGoogle Scholar
  8. Bell O, Tiwari VK, Thomä NH, Schübeler D (2011) Determinants and dynamics of genome accessibility. Nat Rev Genet 12:554–5564PubMedCrossRefGoogle Scholar
  9. Berger SL, Kouzarides T, Shiekhattar R, Shilatifard A (2009) An operational definition of epigenetics. Genes Dev 23:781–783PubMedCrossRefGoogle Scholar
  10. Boivin B, Yang M, Tonks NK (2010) Targeting the reversibly oxidized protein tyrosine phosphatase superfamily. Sci Signal 3(137):l2CrossRefGoogle Scholar
  11. Bregere C, Rebrin I, Sohal RS (2008) Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins. Methods Enzymol 44:339–349CrossRefGoogle Scholar
  12. Brower V (2011) Epigenetics: unravelling the cancer code. Nature 471:S12–S13PubMedCrossRefGoogle Scholar
  13. Burgoyne JR, Eaton P (2010) A rapid approach for the detection, quantification, and discovery of novel sulfenic acid or S-nitrosothiol modified proteins using a biotin-switch method. Methods Enzymol 473:281–303PubMedCrossRefGoogle Scholar
  14. Burhans WC, Heintz NH (2009) The cell cycle is a redox cycle: linking phase-specific targets to cell fate. Free Radic Biol Med 47:1282–1293PubMedCrossRefGoogle Scholar
  15. Cairns RA, Harris IS, Mak TW (2011) Regulation of cancer cell metabolism. Nat Rev Cancer 11:85–95PubMedCrossRefGoogle Scholar
  16. Chagin VO, Stear JH, Cardoso MC (2010) Organization of DNA replication. Cold Spring Harb Perspect Biol 2:a000737PubMedCrossRefGoogle Scholar
  17. Chakraborty A, Shen Z, Prasanth SG (2011) “ORCanization” on heterochromatin: linking DNA replication initiation to chromatin organization. Epigenetics 6:665–670PubMedCrossRefGoogle Scholar
  18. Chen CA, Wang TY, Varadharaj S, Reyes LA, Hemann C, Talukder MA, Chen YR, Druhan LJ, Zweier JL (2010) S-glutathionylation uncouples eNOS and regulates its cellular and vascular function. Nature 468:1115–1118PubMedCrossRefGoogle Scholar
  19. Chen SJ, Zhou GB, Zhang XW, Mao JH, de Thé H, Chen Z (2011) From an old remedy to a magic bullet: molecular mechanisms underlying the therapeutic effects of arsenic in fighting leukemia. Blood 117:6425–6437PubMedCrossRefGoogle Scholar
  20. Cheng X, Blumenthal RM (2008) Mammalian DNA methyltransferases: a structural perspective. Structure 16:341–350PubMedCrossRefGoogle Scholar
  21. Cheng X, Blumenthal RM (2010) Coordinated chromatin control: structural and functional linkage of DNA and histone methylation. Biochemistry 49:2999–3008PubMedCrossRefGoogle Scholar
  22. Coppin JF, Qu W, Waalkes MP (2008) Interplay between cellular methyl metabolism and adaptive efflux during oncogenic transformation from chronic arsenic exposure in human cells. J Biol Chem 283:19342–19350PubMedCrossRefGoogle Scholar
  23. Corpet A, Almouzni G (2009) Making copies of chromatin: the challenge of nucleosomal organization and epigenetic information. Trends Cell Biol 19:29–41PubMedCrossRefGoogle Scholar
  24. Cyr AR, Domann FE (2011) The redox basis of epigenetic modifications: from mechanisms to functional consequences. Antioxid Redox Signal 15:551–589PubMedCrossRefGoogle Scholar
  25. Dabkowski ER, Baseler WA, Williamson CL, Powell M, Razunguzwa TT, Frisbee JC, Hollander JM (2010) Mitochondrial dysfunction in the type 2 diabetic heart is associated with alterations in spatially distinct mitochondrial proteomes. Am J Physiol Heart Circ Physiol 299(2):H529–H540PubMedCrossRefGoogle Scholar
  26. Dansen TB, Smits LM, van Triest MH, de Keizer PL, van Leenen D, Koerkamp MG, Szypowska A, Meppelink A, Brenkman AB, Yodoi J, Holstege FC, Burgering BM (2009) Redox-sensitive cysteines bridge p300/CBP-mediated acetylation and FoxO4 activity. Nat Chem Biol 5:664–672PubMedCrossRefGoogle Scholar
  27. Dennery PA (2010) Oxidative stress in development: nature or nurture? Free Radic Biol Med 49:1147–1151PubMedCrossRefGoogle Scholar
  28. Diaz Vivancos P, Wolff T, Markovic J, Pallardó FV, Foyer CH (2010) A nuclear glutathione cycle within the cell cycle. Biochem J 431:169–178PubMedCrossRefGoogle Scholar
  29. Doyle K, Fitzpatrick FA (2010) Redox signaling, alkylation (carbonylation) of conserved cysteines inactivates class I histone deacetylases 1, 2, and 3 and antagonizes their transcriptional repressor function. J Biol Chem 285:17417–17424PubMedCrossRefGoogle Scholar
  30. Drenckhahn JD (2011) Heart development: mitochondria in command of cardiomyocyte differentiation. Dev Cell 21:392–393PubMedCrossRefGoogle Scholar
  31. Dulce RA, Schulman IH, Hare JM (2011) S-glutathionylation: a redox-sensitive switch participating in nitroso-redox balance. Circ Res 108:531–533PubMedCrossRefGoogle Scholar
  32. Easwaran HP, Van Neste L, Cope L, Sen S, Mohammad HP, Pageau GJ, Lawrence JB, Herman JG, Schuebel KE, Baylin SB (2010) Aberrant silencing of cancer-related genes by CpG hypermethylation occurs independently of their spatial organization in the nucleus. Cancer Res 70(20):8015–8024PubMedCrossRefGoogle Scholar
  33. Ernster L, LEE CP (1964) Biological oxidoreductions. Annu Rev Biochem 33:729–790PubMedCrossRefGoogle Scholar
  34. Fialkow L, Wang Y, Downey GP (2007) Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function. Free Radic Biol Med 42:153–164PubMedCrossRefGoogle Scholar
  35. Finley LW, Carracedo A, Lee J, Souza A, Egia A, Zhang J, Teruya-Feldstein J, Moreira PI, Cardoso SM, Clish CB, Pandolfi PP, Haigis MC (2011) SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization. Cancer Cell 19:416–428PubMedCrossRefGoogle Scholar
  36. Flora SJ (2011) Arsenic-induced oxidative stress and its reversibility. Free Radic Biol Med 51:257–281PubMedCrossRefGoogle Scholar
  37. Gasser SM, Paro R, Stewart F, Aasland R (1998) The genetics of epigenetics. Cell Mol Life Sci 54:1–5PubMedCrossRefGoogle Scholar
  38. Gloire G, Piette J (2009) Redox regulation of nuclear post-translational modifications during NF-kappa B activation. Antioxid Redox Signal 11:2209–2222PubMedCrossRefGoogle Scholar
  39. Gloire G, Legrand-Poels S, Piette J (2006) NF-kappaB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol 72:1493–1505PubMedCrossRefGoogle Scholar
  40. Gough NR, Foley JF (2010) Focus issue: systems analysis of protein phosphorylation. Sci Signal 3(137):eg6PubMedCrossRefGoogle Scholar
  41. Gutteridge JM, Halliwell B (2010) Antioxidants: molecules, medicines, and myths. Biochem Biophys Res Commun 393:561–564PubMedCrossRefGoogle Scholar
  42. Guttmann RP (2010) Redox regulation of cysteine-dependent enzymes. J Anim Sci 88:1297–1306PubMedCrossRefGoogle Scholar
  43. Guz J, Foksinski M, Siomek A, Gackowski D, Rozalski R, Dziaman T, Szpila A, Olinski R (2008) The relationship between 8-oxo-7,8-dihydro-2′-deoxyguanosine level and extent of cytosine methylation in leukocytes DNA of healthy subjects and in patients with colon adenomas and carcinomas. Mutat Res 640:170–173PubMedCrossRefGoogle Scholar
  44. Haig D (2004) The (dual) origin of epigenetics. Cold Spring Harb Symp Quant Biol 69:67–70PubMedCrossRefGoogle Scholar
  45. Haqqani AS, Kelly JF, Birnboim HC (2002) Selective nitration of histone tyrosine residues in vivo in mutatect tumors. J Biol Chem 277:3614–3621PubMedCrossRefGoogle Scholar
  46. He XJ, Chen T, Zhu JK (2011) Regulation and function of DNA methylation in plants and animals. Cell Res 21:442–465PubMedCrossRefGoogle Scholar
  47. Heo J (2011) Redox control of GTPases: from molecular mechanisms to functional significance in health and disease. Antioxid Redox Signal 14:689–724PubMedCrossRefGoogle Scholar
  48. Herring SW (1993) Formation of the vertebrate face: epigenetic and functional influences. Am Zool 33:472Google Scholar
  49. Higuchi Y, Yoshimoto T (2004) Promoting effects of polyunsaturated fatty acids on chromosomal giant DNA fragmentation associated with cell death induced by glutathione depletion. Free Radic Res 38:649–658PubMedCrossRefGoogle Scholar
  50. Hitchler MJ, Domann FE (2007) An epigenetic perspective on the free radical theory of development. Free Radic Biol Med 43:1023–1036PubMedCrossRefGoogle Scholar
  51. Holliday R (1987) The inheritance of epigenetic defects. Science 238:163–170PubMedCrossRefGoogle Scholar
  52. Ishimoto T, Nagano O, Yae T, Tamada M, Motohara T, Oshima H, Oshima M, Ikeda T, Asaba R, Yagi H, Masuko T, Shimizu T, Ishikawa T, Kai K, Takahashi E, Imamura Y, Baba Y, Ohmura M, Suematsu M, Baba H, Saya H (2011) CD44 variant regulates redox status in cancer cells by stabilizing the xCT subunit of system xc(−) and thereby promotes tumor growth. Cancer Cell 19:387–400PubMedCrossRefGoogle Scholar
  53. Janssen-Heininger YM, Mossman BT, Heintz NH, Forman HJ, Kalyanaraman B, Finkel T, Stamler JS, Rhee SG, van der Vliet A (2008) Redox-based regulation of signal transduction: principles, pitfalls, and promises. Free Radic Biol Med 45:1–17PubMedCrossRefGoogle Scholar
  54. Jindal E, Goswami SK (2011) In cardiac myoblasts, cellular redox regulates FosB and Fra-1 through multiple cis-regulatory modules. Free Radic Biol Med 51:1512–1521PubMedCrossRefGoogle Scholar
  55. Joulie M, Miotto B, Defossez PA (2010) Mammalian methyl-binding proteins: what might they do? Bioessays 32:1025–1032PubMedCrossRefGoogle Scholar
  56. Kabra DG, Gupta J, Tikoo K (2009) Insulin induced alteration in post-translational modifications of histone H3 under a hyperglycemic condition in L6 skeletal muscle myoblasts. Biochim Biophys Acta 1792:574–583PubMedCrossRefGoogle Scholar
  57. Kim KS, Choi HW, Yoon HE, Kim IY (2010) Reactive oxygen species generated by NADPH oxidase 2 and 4 are required for chondrogenic differentiation. J Biol Chem 285:40294–44302PubMedCrossRefGoogle Scholar
  58. Klatt P, Molina EP, Lamas S (1999) Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J Biol Chem 274:15857–15864PubMedCrossRefGoogle Scholar
  59. Kornberg MD, Sen N, Hara MR, Juluri KR, Nguyen JV, Snowman AM, Law L, Hester LD, Snyder SH (2010) GAPDH mediates nitrosylation of nuclear proteins. Nat Cell Biol 12:1094–1100PubMedCrossRefGoogle Scholar
  60. Lindermayr C, Saalbach G, Bahnweg G, Durner J (2006) Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation. J Biol Chem 281:4285–4291PubMedCrossRefGoogle Scholar
  61. Liu S, Wu LC, Pang J, Santhanam R, Schwind S, Wu YZ, Hickey CJ, Yu J, Becker H, Maharry K, Radmacher MD, Li C, Whitman SP, Mishra A, Stauffer N, Eiring AM, Briesewitz R, Baiocchi RA, Chan KK, Paschka P, Caligiuri MA, Byrd JC, Croce CM, Bloomfield CD, Perrotti D, Garzon R, Marcucci G (2010) Sp1/NFkappaB/HDAC/miR-29b regulatory network in KIT-driven myeloid leukemia. Cancer Cell 17:333–347PubMedCrossRefGoogle Scholar
  62. Lujambio A, Esteller M (2009) How epigenetics can explain human metastasis: a new role for microRNAs. Cell Cycle 8:377–382PubMedCrossRefGoogle Scholar
  63. Lyon MF (1993) Epigenetic inheritance in mammals. Trends Genet 9:123–128PubMedCrossRefGoogle Scholar
  64. Maller C, Schröder E, Eaton P (2011) Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody. Antioxid Redox Signal 14:49–60PubMedCrossRefGoogle Scholar
  65. Markovic J, García-Gimenez JL, Gimeno A, Viña J, Pallardó FV (2010) Role of glutathione in cell nucleus. Free Radic Res 44:721–733PubMedCrossRefGoogle Scholar
  66. Matés JM, Segura JA, Alonso FJ, Márquez J (2010) Roles of dioxins and heavy metals in cancer and neurological diseases using ROS-mediated mechanisms. Free Radic Biol Med 49:1328–1341PubMedCrossRefGoogle Scholar
  67. Mitra S, Izumi T, Boldogh I, Bhakat KK, Hill JW, Hazra TK (2002) Choreography of oxidative damage repair in mammalian genomes. Free Radic Biol Med 33:15–28PubMedCrossRefGoogle Scholar
  68. Moldovan L, Moldovan NI (2004) Oxygen free radicals and redox biology of organelles. Histochem Cell Biol 122:395–412PubMedCrossRefGoogle Scholar
  69. Nediani C, Raimondi L, Borchi E, Cerbai E (2011) NO/ROS generation and nitroso/redox imbalance in heart failure: from molecular mechanisms to therapeutic implications. Antioxid Redox Signal 14:289–331PubMedCrossRefGoogle Scholar
  70. Nelson KK, Subbaram S, Connor KM, Dasgupta J, Ha XF, Meng TC, Tonks NK, Melendez JA (2006) Redox-dependent matrix metalloproteinase-1 expression is regulated by JNK through Ets and AP-1 promoter motifs. J Biol Chem 281:14100–14110PubMedCrossRefGoogle Scholar
  71. Nikitovic D, Holmgren A, Spyrou G (1998) Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos. Biochem Biophys Res Commun 242:109–112PubMedCrossRefGoogle Scholar
  72. Nishida M, Ogushi M, Suda R, Toyotaka M, Saiki S, Kitajima N, Nakaya M, Kim KM, Ide T, Sato Y, Inoue K, Kurose H (2011) Heterologous down-regulation of angiotensin type 1 receptors by purinergic P2Y2 receptor stimulation through S-nitrosylation of NF-{kappa}B. Proc Natl Acad Sci U S A 108:6662–6667PubMedCrossRefGoogle Scholar
  73. Nott A, Watson PM, Robinson JD, Crepaldi L, Riccio A (2008) S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons. Nature 455:411–415PubMedCrossRefGoogle Scholar
  74. Oliveira-Marques V, Marinho HS, Cyrne L, Antunes F (2009) Role of hydrogen peroxide in NF-kappaB activation: from inducer to modulator. Antioxid Redox Signal 11:2223–2243PubMedCrossRefGoogle Scholar
  75. Osoata GO, Yamamura S, Ito M, Vuppusetty C, Adcock IM, Barnes PJ, Ito K (2009) Nitration of distinct tyrosine residues causes inactivation of histone deacetylase 2. Biochem Biophys Res Commun 384:366–371PubMedCrossRefGoogle Scholar
  76. Pamplona R, Naudí A, Gavín R, Pastrana MA, Sajnani G, Ilieva EV, Del Río JA, Portero-Otín M, Ferrer I, Requena JR (2008) Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease. Free Radic Biol Med 45:1159–1166PubMedCrossRefGoogle Scholar
  77. Perkins C, Kim CN, Fang G, Bhalla KN (2000) Arsenic induces apoptosis of multidrug-resistant human myeloid leukemia cells that express Bcr-Abl or overexpress MDR, MRP, Bcl-2, or Bcl-x(L). Blood 95:1014–1022PubMedGoogle Scholar
  78. Pierard V, Guiguen A, Colin L, Wijmeersch G, Vanhulle C, Van Driessche B, Dekoninck A, Blazkova J, Cardona C, Merimi M, Vierendeel V, Calomme C, Nguyên TL, Nuttinck M, Twizere JC, Kettmann R, Portetelle D, Burny A, Hirsch I, Rohr O, Van Lint C (2010) DNA cytosine methylation in the bovine leukemia virus promoter is associated with latency in a lymphoma-derived B-cell line: potential involvement of direct inhibition of cAMP-responsive element (CRE)-binding protein/CRE modulator/activation transcription factor binding. J Biol Chem 285:19434–19449PubMedCrossRefGoogle Scholar
  79. Rahman I (2002) Oxidative stress, transcription factors and chromatin remodelling in lung inflammation. Biochem Pharmacol 64:935–942PubMedCrossRefGoogle Scholar
  80. Rahman I, Marwick J, Kirkham P (2004) Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem Pharmacol 68:1255–1267PubMedCrossRefGoogle Scholar
  81. Rajendrasozhan S, Yang SR, Edirisinghe I, Yao H, Adenuga D, Rahman I (2008) Deacetylases and NF-kappaB in redox regulation of cigarette smoke-induced lung inflammation: epigenetics in pathogenesis of COPD. Antioxid Redox Signal 10:799–811PubMedCrossRefGoogle Scholar
  82. Rakyan VK, Down TA, Balding DJ, Beck S (2011) Epigenome-wide association studies for common human diseases. Nat Rev Genet 12:529–541PubMedCrossRefGoogle Scholar
  83. Riggs AD, Martienssen RA, Russo VEA (1996) Introduction in epigenetic mechanisms of gene regulation. In: Russo VEA et al (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp 1–4Google Scholar
  84. Rishi V, Bhattacharya P, Chatterjee R, Rozenberg J, Zhao J, Glass K, Fitzgerald P, Vinson C (2010) CpG methylation of half-CRE sequences creates C/EBPalpha binding sites that activate some tissue-specific genes. Proc Natl Acad Sci U S A 107:20311–20316PubMedCrossRefGoogle Scholar
  85. Schreck R, Rieber P, Baeuerle PA (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10:2247–2258PubMedGoogle Scholar
  86. Selvi BR, Mohankrishna DV, Ostwal YB, Kundu TK (2010) Small molecule modulators of histone acetylation and methylation: a disease perspective. Biochim Biophys Acta 1799:810–828PubMedCrossRefGoogle Scholar
  87. Shlomai J (2010) Redox control of protein-DNA interactions: from molecular mechanisms to significance in signal transduction, gene expression, and DNA replication. Antioxid Redox Signal 13:1429–1476PubMedCrossRefGoogle Scholar
  88. Simone NL, Soule BP, Ly D, Saleh AD, Savage JE, Degraff W, Cook J, Harris CC, Gius D, Mitchell JB (2009) Ionizing radiation-induced oxidative stress alters miRNA expression. PLoS One 4:e6377PubMedCrossRefGoogle Scholar
  89. Svedruzić ZM, Reich NO (2005) DNA cytosine C5 methyltransferase Dnmt1: catalysis-dependent release of allosteric inhibition. Biochemistry 44:9472–9485PubMedCrossRefGoogle Scholar
  90. Tanaka T, Kurose A, Halicka HD, Huang X, Traganos F, Darzynkiewicz Z (2006) Nitrogen oxide-releasing aspirin induces histone H2AX phosphorylation, ATM activation and apoptosis preferentially in S-phase cells: involvement of reactive oxygen species. Cell Cycle 5:1669–1674PubMedCrossRefGoogle Scholar
  91. Tasaka S, Amaya F, Hashimoto S, Ishizaka A (2008) Roles of oxidants and redox signaling in the pathogenesis of acute respiratory distress syndrome. Antioxid Redox Signal 10:739–753PubMedCrossRefGoogle Scholar
  92. Tew KD, Townsend DM (2011) Redox platforms in cancer drug discovery and development. Curr Opin Chem Biol 15(1):156–161PubMedCrossRefGoogle Scholar
  93. Tikoo K, Lau SS, Monks TJ (2001) Histone H3 phosphorylation is coupled to poly-(ADP-ribosylation) during reactive oxygen species-induced cell death in renal proximal tubular epithelial cells. Mol Pharmacol 60:394–402PubMedGoogle Scholar
  94. Tong KI, Padmanabhan B, Kobayashi A, Shang C, Hirotsu Y, Yokoyama S, Yamamoto M (2007) Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Mol Cell Biol 27:7511–7521PubMedCrossRefGoogle Scholar
  95. Turner BM (1998) Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell Mol Life Sci 54:21–31PubMedCrossRefGoogle Scholar
  96. Ufer C, Wang CC, Borchert A, Heydeck D, Kuhn H (2010) Redox control in mammalian embryo development. Antioxid Redox Signal 13:833–875PubMedCrossRefGoogle Scholar
  97. Upadhyay AK, Cheng X (2011) Dynamics of histone lysine methylation: structures of methyl writers and erasers. Prog Drug Res 67:107–124PubMedGoogle Scholar
  98. Upham BL, Trosko JE (2009) Oxidative-dependent integration of signal transduction with intercellular gap junctional communication in the control of gene expression. Antioxid Redox Signal 11:297–307PubMedCrossRefGoogle Scholar
  99. Varier RA, Timmers HT (2011) Histone lysine methylation and demethylation pathways in cancer. Biochim Biophys Acta 1815:75–89PubMedGoogle Scholar
  100. Waddington CH (1938) The epigenetics of birds. University Press, Cambridge, UK, 1952Google Scholar
  101. Weaver AM (2009) Regulation of cancer invasion by reactive oxygen species and Tks family scaffold proteins. Sci Signal 2:e56CrossRefGoogle Scholar
  102. Wertz IE, Dixit VM (2010) Signaling to NF-kappaB: regulation by ubiquitination. Cold Spring Harb Perspect Biol 2(3):a003350PubMedCrossRefGoogle Scholar
  103. Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG (2010) Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell 140:517–528PubMedCrossRefGoogle Scholar
  104. Xanthoudakis S, Curran T (1992) Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J 11:653–665PubMedGoogle Scholar
  105. Xie H, Wang M, de Andrade A, Bonaldo MD, Galat V, Arndt K, Rajaram V, Goldman S, Tomita T, Soares MB (2011) Genome-wide quantitative assessment of variation in DNA methylation patterns. Nucleic Acids Res 39:4099–4108Google Scholar
  106. Yang SR, Chida AS, Bauter MR, Shafiq N, Seweryniak K, Maggirwar SB, Kilty I, Rahman I (2006) Cigarette smoke induces proinflammatory cytokine release by activation of NF-kappaB and posttranslational modifications of histone deacetylase in macrophages. Am J Physiol Lung Cell Mol Physiol 29:L46–L57CrossRefGoogle Scholar
  107. Yao H, Hwang JW, Moscat J, Diaz-Meco MT, Leitges M, Kishore N, Li X, Rahman I (2010) Protein kinase C zeta mediates cigarette smoke/aldehyde- and lipopolysaccharide-induced lung inflammation and histone modifications. J Biol Chem 285:5405–5416PubMedCrossRefGoogle Scholar
  108. Yu DS, Cortez D (2011) A role for cdk9-cyclin k in maintaining genome integrity. Cell Cycle 10:28–32PubMedCrossRefGoogle Scholar
  109. Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X (2003) Structural basis for the product specificity of histone lysine methyltransferases. Mol Cell 12:177–185PubMedCrossRefGoogle Scholar
  110. Zhu H, Shan L, Schiller PW, Mai A, Peng T (2010) Histone deacetylase-3 activation promotes tumor necrosis factor-alpha (TNF-alpha) expression in cardiomyocytes during lipopolysaccharide stimulation. J Biol Chem 285:9429–9436PubMedCrossRefGoogle Scholar

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© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.School of Life SciencesJawaharlal Nehru UniversityNew DelhiIndia

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