Metabolic control of the epigenome in systemic Lupus erythematosus

References

• Kyttaris V. C., and G. C. Tsokos. 2004. T lymphocytes in systemic lupus erythematosus: an update. Curr. Opin. Rheumatol. 16: 548–552
   PubMed Web of Science ®Google Scholar
• Anolik J., and I. Sanz. 2004. B cells in human and murine systemic lupus erythematosus. Curr. Opin. Rheumatol. 16: 505–512
   PubMed Web of Science ®Google Scholar
• Nagy G., A. Koncz, and A. Perl. 2005. T- and B-cell abnormalities in systemic lupus erythematosus. Crit. Rev. Immunol. 25: 123–140
   PubMed Web of Science ®Google Scholar
• Pascual V., J. Banchereau, and A. K. Palucka. 2003. The central role of dendritic cells and interferon-alpha in SLE. Curr. Opin. Rheumatol. 15: 548–556
   PubMed Web of Science ®Google Scholar
• Crispin J. C., and J. Alcocer-Varela. 2007. The role myeloid dendritic cells play in the pathogenesis of systemic lupus erythematosus. Autoimmun. Rev. 6: 450–456
   PubMed Web of Science ®Google Scholar
• Rao T., and B. Richardson. 1999. Environmentally induced autoimmune diseases: potential mechanisms. Environ. Health Perspect. 107: 737–742
   PubMed Web of Science ®Google Scholar
• Manderson A. P., M. Botto, and M. J. Walport. 2004. The role of complement in the development of systemic lupus erythematosus. Annu. Rev. Immunol. 22: 431–456
   PubMed Web of Science ®Google Scholar
• Gateva V., J. K. Sandling, G. Hom, et al. 2009. A large-scale replication study identifies TNIP1, PRDM1, JAZF1, UHRF1BP1 and IL10 as risk loci for systemic lupus erythematosus. Nat. Genet. 41: 1228–1233
   PubMed Web of Science ®Google Scholar
• Nagy G., J. Ward, D. D. Mosser, et al. 2006. Regulation of CD4 expression via recycling by HRES-1/RAB4 controls susceptibility to HIV infection. J. Biol. Chem. 281: 34574–34591
   PubMed Web of Science ®Google Scholar
• Vaughn S. E., L. C. Kottyan, M. E. Munroe, and J. B. Harley. 2012. Genetic susceptibility to lupus: the biological basis of genetic risk found in B cell signaling pathways. J. Leukoc. Biol. 92: 577--591
   PubMed Web of Science ®Google Scholar
• Flesher D. L., X. Sun, T. W. Behrens, et al. 2010. Recent advances in the genetics of systemic lupus erythematosus. Expert Rev. Clin. Immunol. 6: 461–479
   PubMed Web of Science ®Google Scholar
• Richardson B. 2003. DNA methylation and autoimmune disease. Clin. Immunol. 109: 72–79
   PubMed Web of Science ®Google Scholar
• Patel DR, and B. C. Richardson. 2010. Epigenetic mechanisms in lupus. Curr. Opin. Rheumatol. 22: 478–482
   PubMed Web of Science ®Google Scholar
• Richardson B. 2007. Primer: epigenetics of autoimmunity. Nat. Clin. Pract. Rheumatol. 3: 521–527
   PubMedGoogle Scholar
• Brooks W. H., C. Le Dantec, J. O. Pers, et al. 2010. Epigenetics and autoimmunity. J. Autoimmun. 34: J207–J219
   PubMed Web of Science ®Google Scholar
• Zouali M. Epigenetics in lupus. 2011. Ann. N. Y. Acad. Sci. 1217: 154–165
   PubMed Web of Science ®Google Scholar
• Richardson B., L. Scheinbart, J. Strahler, et al. 1990. Evidence for impaired T cell DNA methylation in systemic lupus erythematosus and rheumatoid arthritis. Arthritis Rheum. 33: 1665–1673
   PubMed Web of Science ®Google Scholar
• Zhang Y., M. Zhao, A. H. Sawalha, et al. 2013. Impaired DNA methylation and its mechanisms in CD4(+)T cells of systemic lupus erythematosus. J. Autoimmun. 41: 92–99
   PubMed Web of Science ®Google Scholar
• Coit P., M. Jeffries, N. Altorok, et al. 2013. Genome-wide DNA methylation study suggests epigenetic accessibility and transcriptional poising of interferon-regulated genes in naive CD4+ T cells from lupus patients. J. Autoimmun. 43: 78–84
   PubMed Web of Science ®Google Scholar
• Kaelin W. G.Jr, and S. L. McKnight. 2013. Influence of metabolism on epigenetics and disease. Cell. 153: 56–69
   PubMed Web of Science ®Google Scholar
• Lu C., and C. B. Thompson. 2012. Metabolic regulation of epigenetics. Cell. Metab. 16: 9–17
   PubMed Web of Science ®Google Scholar
• Ray P. D., B. W. Huang, and Y. Tsuji. 2012. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell Signal. 24: 981–990
   PubMed Web of Science ®Google Scholar
• Ulrey C. L., L. Liu, L. G. Andrews, and T. O. Tollefsbol. 2005. The impact of metabolism on DNA methylation. Hum. Mol. Genet. 14: R139–R147
   PubMed Web of Science ®Google Scholar
• Perl A. 2012. Oxidative stress and endosome recycling are complementary mechanisms reorganizing the T-cell receptor signaling complex in SLE. Clin. Immunol. 142: 219–222
   PubMed Web of Science ®Google Scholar
• Goswami S. K. 2012. Cellular redox, epigenetics and diseases. Subcell. Biochem. 61: 527–542
   Google Scholar
• Adam-Vizi V. 2005. Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources. Antioxid. Redox Signal. 7: 1140–1149
   PubMed Web of Science ®Google Scholar
• Perl A., R. Hanczko, and E. Doherty. 2012. Assessment of mitochondrial dysfunction in lymphocytes of patients with systemic lupus erythematosus. Methods Mol. Biol. 900: 61–89
   PubMedGoogle Scholar
• Corvetta A., R. Della Bitta, M. M. Luchetti, and G. Pomponio. 1991. 5-methylcytosine content of DNA in blood, synovial mononuclear cells and synovial tissue from patients affected by autoimmune rheumatic diseases. J. Chromatogr. 566: 481–491
   PubMed Web of Science ®Google Scholar
• Lu S. C., L. Alvarez, Z. Z. Huang, et al. 2001. Methionine adenosyltransferase 1A knockout mice are predisposed to liver injury and exhibit increased expression of genes involved in proliferation. Proc. Natl. Acad. Sci. USA. 98: 5560–5565
   PubMed Web of Science ®Google Scholar
• Avila M. A., F. J. Corrales, F. Ruiz, et al. 1998. Specific interaction of methionine adenosyltransferase with free radicals. Biofactors. 8:27–32
   PubMed Web of Science ®Google Scholar
• Selhub J., and J. W. Miller. 1992. The pathogenesis of homocysteinemia: interruption of the coordinate regulation by S-adenosylmethionine of the remethylation and transsulfuration of homocysteine. Am. J. Clin. Nutr. 55: 131–138
   PubMed Web of Science ®Google Scholar
• Sipka S. 2011. Adenosine inhibits the release of arachidonic acid in activated human peripheral mononuclear cells. A proposed model for physiologic and pathologic regulation in systemic lupus erythematosus. Scientific World J. 11: 972–980
   Web of Science ®Google Scholar
• Dawson H., G. Collins, R. Pyle, et al. 2004. The immunoregulatory effects of homocysteine and its intermediates on T-lymphocyte function. Mech. Ageing Dev. 125: 107–110
   PubMed Web of Science ®Google Scholar
• do Prado R., V. M. D'Almeida, E. Guerra-Shinohara, et al. 2006. Increased concentration of plasma homocysteine in children with systemic lupus erythematosus. Clin. Exp. Rheumatol. 24: 594–598
   PubMed Web of Science ®Google Scholar
• Svedruzic Z. M., and N. O. Reich. 2005. DNA cytosine C5 methyltransferase Dnmt1: catalysis-dependent release of allosteric inhibition. Biochemistry. 44: 9472–9485
   PubMed Web of Science ®Google Scholar
• Deng C., M. J. Kaplan, J. Yang, et al. 2001. Decreased ras-mitogen-activated protein kinase signaling may cause DNA hypomethylation in T lymphocytes from lupus patients. Arthritis Rheum. 44: 397–407
   PubMed Web of Science ®Google Scholar
• Perl A. 2010. Pathogenic mechanisms in systemic lupus erythematosus. Autoimmunity. 43: 1–6
   PubMed Web of Science ®Google Scholar
• Deng C, J. Yang, J. Scott, et al. 1998. Role of the ras-MAPK signaling pathway in the DNA methyltransferase response to DNA hypomethylation. Biol. Chem. 379: 1113–1120
   PubMedGoogle Scholar
• Gorelik G., J. Y. Fang, A. Wu, et al. 2007. Impaired T cell protein kinase C delta activation decreases ERK pathway signaling in idiopathic and hydralazine-induced lupus. J. Immunol. 179: 5553–5563
   PubMed Web of Science ®Google Scholar
• Januchowski R., M. Wudarski, H. Chwalinska-Sadowska, and P. P. Jagodzinski. 2008. Prevalence of ZAP-70, LAT, SLP-76, and DNA methyltransferase 1 expression in CD4+ T cells of patients with systemic lupus erythematosus. Clin. Rheumatol. 27: 21–27
   PubMed Web of Science ®Google Scholar
• Gorelik G. J., S. Yarlagadda, and B. C. Richardson. 2012. Protein kinase cdelta oxidation contributes to ERK inactivation in lupus T cells. Arthritis Rheum. 64: 2964–2974
   PubMed Web of Science ®Google Scholar
• Cornacchia E., J. Golbus, J. Maybaum, et al. 1988. Hydralazine and procainamide inhibit T cell DNA methylation and induce autoreactivity. J. Immunol. 140: 2197–2200
   PubMed Web of Science ®Google Scholar
• Li-Weber M., M. K. Treiber, M. Giaisi, et al. 2005. Ultraviolet irradiation suppresses T cell activation via blocking TCR-mediated ERK and NF-kappa B signaling pathways. J. Immunol. 175: 2132–2143
   PubMed Web of Science ®Google Scholar
• Belot, A., P. R. Kasher, E. W. Trotter, et al. 2013. Protein kinase C delta deficiency causes mendelian systemic lupus erythematosus with B-cell defective apoptosis and hyperproliferation. Arthritis Rheum. 65: 2161--2171
   Google Scholar
• Mazari L., M. Ouarzane, and M. Zouali. 2007. Subversion of B lymphocyte tolerance by hydralazine, a potential mechanism for drug-induced lupus. Proc. Natl. Acad. Sci. USA. 104: 6317–6322
   PubMed Web of Science ®Google Scholar
• Franchini D. M., K. M. Schmitz, and S. K. Petersen-Mahrt. 2012. 5-methylcytosine DNA demethylation: more than losing a methyl group. Annu. Rev. Genet. 46: 419–441
   PubMed Web of Science ®Google Scholar
• Zan H., and P. Casali. 2013. Regulation of aicda expression and AID activity. Autoimmunity. 46: 83–101
   PubMed Web of Science ®Google Scholar
• Garcia-Manteiga J. M., S. Mari, Godejohann M., et al. 2011. Metabolomics of B to plasma cell differentiation. J. Proteome Res. 10: 4165–4176
   PubMed Web of Science ®Google Scholar
• Wu T., C. Xie, J. Han, et al. 2012. Metabolic disturbances associated with systemic lupus erythematosus. PLoS One. 7: e37210
   PubMed Web of Science ®Google Scholar
• Hoffman D. R., D. W. Marion, W. E. Cornatzer, and J. A. Duerre. 1980. S-adenosylmethionine and S-adenosylhomocystein metabolism in isolated rat liver. effects of l-methionine, l-homocystein, and adenosine. J. Biol. Chem. 255: 10822–10827
   PubMed Web of Science ®Google Scholar
• Yi P., S. Melnyk, M. Pogribna, et al. 2000. Increase in plasma homocysteine associated with parallel increases in plasma S-adenosylhomocysteine and lymphocyte DNA hypomethylation. J. Biol. Chem. 275: 29318–29323
   PubMed Web of Science ®Google Scholar
• Lertratanangkoon K., C. J. Wu, N. Savaraj, and M. L. Thomas. 1997. Alterations of DNA methylation by glutathione depletion. Cancer Lett. 120: 149–156
   PubMed Web of Science ®Google Scholar
• Poirier L. A., C. K. Wise, R. R. Delongchamp, and R. Sinha. 2001. Blood determinations of S-adenosylmethionine, S-adenosylhomocysteine, and homocysteine: correlations with diet. Cancer. Epidemiol. Biomarkers Prev. 10: 649–655
   PubMed Web of Science ®Google Scholar
• Kim Y. I. 2005. Nutritional epigenetics: impact of folate deficiency on DNA methylation and colon cancer susceptibility. J. Nutr. 135: 2703–2709
   PubMed Web of Science ®Google Scholar
• Feil R., and M. F. Fraga. 2012. Epigenetics and the environment: emerging patterns and implications. Nat. Rev. Genet. 13: 97–109
   PubMed Web of Science ®Google Scholar
• Kimura M., K. Umegaki, M. Higuchi, et al. 2004. Methylenetetrahydrofolate reductase C677T polymorphism, folic acid and riboflavin are important determinants of genome stability in cultured human lymphocytes. J. Nutr. 134: 48–56
   PubMed Web of Science ®Google Scholar
• Huck S., and M. Zouali. 1996. DNA methylation: a potential pathway to abnormal autoreactive lupus B cells. Clin. Immunol. Immunopathol. 80: 1–8
   PubMedGoogle Scholar
• Huck S., E. Deveaud, A. Namane, and M. Zouali. 1999. Abnormal DNA methylation and deoxycytosine-deoxyguanine content in nucleosomes from lymphocytes undergoing apoptosis. FASEB J. 13: 1415–1422
   PubMed Web of Science ®Google Scholar
• He Y. F., B. Z. Li, Z. Li, et al. 2011. Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science. 333: 1303–1307
   PubMed Web of Science ®Google Scholar
• Ito S., L. Shen, Q. Dai, et al. 2011. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science. 333: 1300–1303
   PubMed Web of Science ®Google Scholar
• Bruniquel D., and R. H. Schwartz. 2003. Selective, stable demethylation of the interleukin-2 gene enhances transcription by an active process. Nat. Immunol. 4: 235–240
   PubMed Web of Science ®Google Scholar
• Krishna P., M. J. Fritzler, and J. H. Van de Sande. 1993. Interactions of anti-DNA antibodies with Z-DNA. Clin. Exp. Immunol. 92: 51–57
   PubMed Web of Science ®Google Scholar
• Puri H., R. A. Campbell, V. Puri-Harner, et al. 1978. Serum-free polyamines in children with systemic lupus erythematosus. Vol 2. New York: Raven Press. p. 359–367
   Google Scholar
• Thomas T. J., J. R. Seibold, L. E. Adams, and E. V. Hess. 1993. Hydralazine induces Z-DNA conformation in a polynucleotide and elicits anti(Z-DNA) antibodies in treated patients. Biochem. J. 294: 419–425
   PubMed Web of Science ®Google Scholar
• Ahmad N., A. C. Gilliam, S. K. Katiyar, et al. 2001. A definitive role of ornithine decarboxylase in photocarcinogenesis. Am. J. Pathol. 159: 885–892
   PubMed Web of Science ®Google Scholar
• Hobbs C. A., and S. K. Gilmour. 2000. High levels of intracellular polyamines promote histone acetyltransferase activity resulting in chromatin hyperacetylation. J. Cell. Biochem. 77: 345–360
   PubMed Web of Science ®Google Scholar
• Hobbs C. A., B. A. Paul, and S. K. Gilmour. 2002. Deregulation of polyamine biosynthesis alters intrinsic histone acetyltransferase and deacetylase activities in murine skin and tumors. Cancer Res. 62: 67–74
   PubMed Web of Science ®Google Scholar
• Upadhyay A. K., and X. Cheng. 2011. Dynamics of histone lysine methylation: structures of methyl writers and erasers. Prog. Drug Res. 67: 107–124
   PubMedGoogle Scholar
• Barski A., S. Cuddapah, K. Cui, et al. 2007. High-resolution profiling of histone methylations in the human genome. Cell. 129: 823–837
   PubMed Web of Science ®Google Scholar
• Zhang X., Z. Yang, S. I. Khan, et al. 2003. Structural basis for the product specificity of histone lysine methyltransferases. Mol. Cell. 12: 177–185
   PubMed Web of Science ®Google Scholar
• Rauen T., A. P. Grammatikos, C. M. Hedrich, et al. 2012. cAMP-responsive element modulator alpha (CREMalpha) contributes to decreased notch-1 expression in T cells from patients with active systemic lupus erythematosus (SLE). J. Biol. Chem. 287: 42525–42532
   PubMed Web of Science ®Google Scholar
• Zhang Q., H. Long, J. Liao, et al. 2011. Inhibited expression of hematopoietic progenitor kinase 1 associated with loss of jumonji domain containing 3 promoter binding contributes to autoimmunity in systemic lupus erythematosus. J. Autoimmun. 37: 180–189
   PubMed Web of Science ®Google Scholar
• Perillo B., M. N. Ombra, A. Bertoni, et al. 2008. DNA oxidation as triggered by H3K9me2 demethylation drives estrogen-induced gene expression. Science. 319: 202–206
   PubMed Web of Science ®Google Scholar
• Hino S., A. Sakamoto, K. Nagaoka, et al. 2012. FAD-dependent lysine-specific demethylase-1 regulates cellular energy expenditure. Nat. Commun. 3: 758
   PubMed Web of Science ®Google Scholar
• Letouze E., C. Martinelli, C. Loriot, et al. 2013. SDH mutations establish a hypermethylator phenotype in paraganglioma. Cancer Cell. 23: 739–752
   PubMed Web of Science ®Google Scholar
• Chervona Y., and M. Costa. 2012. The control of histone methylation and gene expression by oxidative stress, hypoxia, and metals. Free Radic. Biol. Med. 53: 1041–1047
   PubMed Web of Science ®Google Scholar
• Mimura I., M. Nangaku, Y. Kanki, et al. 2012. Dynamic change of chromatin conformation in response to hypoxia enhances the expression of GLUT3 (SLC2A3) by cooperative interaction of hypoxia-inducible factor 1 and KDM3A. Mol. Cell. Biol. 32: 3018–3032
   PubMed Web of Science ®Google Scholar
• Hudson C. C., M. Liu, G. G. Chiang, et al. 2002. Regulation of hypoxia-inducible factor 1alpha expression and function by the mammalian target of rapamycin. Mol. Cell. Biol. 22: 7004–7014
   PubMed Web of Science ®Google Scholar
• Lee D. Y., J. J. Hayes, D. Pruss, and A. P. Wolffe. 1993. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell. 72: 73–84
   PubMed Web of Science ®Google Scholar
• Forster N., S. Gallinat, J. Jablonska, et al. 2007. P300 protein acetyltransferase activity suppresses systemic lupus erythematosus-like autoimmune disease in mice. J. Immunol. 178: 6941–6948
   PubMed Web of Science ®Google Scholar
• Cai L., B. M. Sutter, B. Li, and B. P. Tu. 2011. Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes. Mol. Cell. 42: 426–437
   PubMed Web of Science ®Google Scholar
• Takahashi H., J. M. McCaffery, R. A. Irizarry, and J. D. Boeke. 2006. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Mol. Cell. 23: 207–217
   PubMed Web of Science ®Google Scholar
• Grassian A. R., C. M. Metallo, J. L. Coloff, et al. 2011. Erk regulation of pyruvate dehydrogenase flux through PDK4 modulates cell proliferation. Genes Dev. 25: 1716--1733
   PubMed Web of Science ®Google Scholar
• Wahl D. R., B. Petersen, R. Warner, et al. 2010. Characterization of the metabolic phenotype of chronically activated lymphocytes. Lupus. 19: 1492–1501
   PubMed Web of Science ®Google Scholar
• Ma L., Z. Chen, H. Erdjument-Bromage, et al. 2005. Phosphorylation and functional inactivation of TSC2 by erk implications for tuberous sclerosis and cancer pathogenesis. Cell. 121: 179–193
   PubMed Web of Science ®Google Scholar
• Perl A. 2010. Systems biology of lupus: mapping the impact of genomic and environmental factors on gene expression signatures, cellular signaling, metabolic pathways, hormonal and cytokine imbalance, and selecting targets for treatment. Autoimmunity. 43: 32–47
   PubMed Web of Science ®Google Scholar
• Osoata G. O., S. Yamamura, M. Ito, et al. 2009. Nitration of distinct tyrosine residues causes inactivation of histone deacetylase 2. Biochem. Biophys. Res. Commun. 384: 366–371
   PubMed Web of Science ®Google Scholar
• Yang S. R., A. S. Chida, M. R. Bauter, et al. 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. 291: L46–L57
   PubMed Web of Science ®Google Scholar
• Reilly C. M., N. Regna, and N. Mishra. 2011. HDAC inhibition in lupus models. Mol. Med. 17: 417–425
   PubMed Web of Science ®Google Scholar
• Veech R. L., L. V. Eggleston, and H. A. Krebs. 1969. The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J. 115: 609–619
   PubMed Web of Science ®Google Scholar
• Lin S. J., and L. Guarente. 2003. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell. Biol. 15: 241–246
   PubMed Web of Science ®Google Scholar
• Widner B., N. Sepp, E. Kowald, et al. 1999. Degradation of tryptophan in patients with systemic lupus erythematosus. Adv. Exp. Med. Biol. 467: 571–577
   PubMed Web of Science ®Google Scholar
• Widner B., N. Sepp, E. Kowald, et al. 2000. Enhanced tryptophan degradation in systemic lupus erythematosus. Immunobiology. 201: 621–630
   PubMed Web of Science ®Google Scholar
• Yamamori T., J. DeRicco, A. Naqvi, et al. 2010. SIRT1 deacetylates APE1 and regulates cellular base excision repair. Nucleic Acids Res. 38: 832–845
   PubMed Web of Science ®Google Scholar
• Hu N., X. Qiu, Y. Luo, et al. 2008. Abnormal histone modification patterns in lupus CD4+ T cells. J. Rheumatol. 35: 804–810
   PubMed Web of Science ®Google Scholar
• Hu N., H. Long, M. Zhao, et al. 2009. Aberrant expression pattern of histone acetylation modifiers and mitigation of lupus by SIRT1-siRNA in MRL/lpr mice. Scand. J. Rheumatol. 38: 464–471
   PubMed Web of Science ®Google Scholar
• Mishra N., C. M. Reilly, D. R. Brown, et al. 2003. Histone deacetylase inhibitors modulate renal disease in the MRL-lpr/lpr mouse. J. Clin. Invest. 111: 539–552
   PubMed Web of Science ®Google Scholar
• Zhang Z., L. Song, K. Maurer, et al. 2010. Global H4 acetylation analysis by ChIP-chip in systemic lupus erythematosus monocytes. Genes Immun. 11: 124–133
   PubMed Web of Science ®Google Scholar
• Lee J. Y., N. A. Kim, A. Sanford, and K. E. Sullivan. 2003. Histone acetylation and chromatin conformation are regulated separately at the TNF-alpha promoter in monocytes and macrophages. J. Leukoc. Biol. 73: 862–871
   PubMed Web of Science ®Google Scholar
• Phillips R., R. Lomnitzer, A. A. Wadee, and A. R. Rabson. 1985. Defective monocyte function in patients with systemic lupus erythematosus. Clin. Immunol. Immunopathol. 34: 69–76
   PubMedGoogle Scholar
• Banerjee T., and D. Chakravarti. 2011. A peek into the complex realm of histone phosphorylation. Mol. Cell. Biol. 31: 4858–4873
   PubMedGoogle Scholar
• Tato I., R. Bartrons, F. Ventura, and J. L. Rosa. 2011. Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via PI3K/akt signaling. J. Biol. Chem. 286: 6128–6142
   PubMed Web of Science ®Google Scholar
• Bungard D., B. J. Fuerth, P. Y. Zeng, et al. 2010. Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation. Science. 329: 1201–1205
   PubMed Web of Science ®Google Scholar
• Gergely P. Jr, C. Grossman, B. Niland, et al. 2002. Mitochondrial hyperpolarization and ATP depletion in patients with systemic lupus erythematosus. Arthritis Rheum. 46: 175–190
   PubMed Web of Science ®Google Scholar
• Griffey R. H., M. S. Brown, A. D. Bankhurst, et al. 1990. Depletion of high-energy phosphates in the central nervous system of patients with systemic lupus erythematosus, as determined by phosphorus-31 nuclear magnetic resonance spectroscopy. Arthritis Rheum. 33: 827–833
   PubMedGoogle Scholar
• Fernandez D. R., T. Telarico, E. Bonilla, et al. 2009. Activation of mammalian target of rapamycin controls the loss of TCRzeta in lupus T cells through HRES-1/Rab4-regulated lysosomal degradation. J. Immunol. 182: 2063–2073
   PubMed Web of Science ®Google Scholar
• Cline S. D., J. N. Riggins, S. Tornaletti, et al. 2004. Malondialdehyde adducts in DNA arrest transcription by T7 RNA polymerase and mammalian RNA polymerase II. Proc. Natl. Acad. Sci. USA. 101: 7275–7280
   PubMed Web of Science ®Google Scholar
• Marnett L. J. 1999. Lipid peroxidation-DNA damage by malondialdehyde. Mutat. Res. 424: 83–95
   PubMed Web of Science ®Google Scholar
• Doyle K., and F. A. Fitzpatrick. 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: 17417–17424
   PubMed Web of Science ®Google Scholar
• Li Y., M. Zhao, H. Yin, et al. 2010. Overexpression of the growth arrest and DNA damage-induced 45alpha gene contributes to autoimmunity by promoting DNA demethylation in lupus T cells. Arthritis Rheum. 62: 1438–1447
   PubMed Web of Science ®Google Scholar
• Barreto G., A. Schafer, J. Marhold, et al. 2007. Gadd45a promotes epigenetic gene activation by repair-mediated DNA demethylation. Nature. 445: 671–675
   PubMed Web of Science ®Google Scholar
• Fujiki R., W. Hashiba, H. Sekine, et al. 2011. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature. 480: 557–560
   PubMed Web of Science ®Google Scholar
• Deplus R., B. Delatte, M. K. Schwinn, et al. 2013. TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS. EMBO J. 32: 645–655
   PubMed Web of Science ®Google Scholar
• Chen Q., Y. Chen, C. Bian, et al. 2013. TET2 promotes histone O-GlcNAcylation during gene transcription. Nature. 493: 561–564
   PubMed Web of Science ®Google Scholar
• Tsokos G. C., M. P. Nambiar, and Y. T. Juang. 2003. Activation of the ets transcription factor elf-1 requires phosphorylation and glycosylation: defective expression of activated elf-1 is involved in the decreased TCR zeta chain gene expression in patients with systemic lupus erythematosus. Ann. N. Y. Acad. Sci. 987: 240–245
   PubMed Web of Science ®Google Scholar
• Guppy M., E. Greiner, and K. Brand. 1993. The role of the crabtree effect and an endogenous fuel in the energy metabolism of resting and proliferating thymocytes. Eur. J. Biochem. 212: 95–99
   PubMedGoogle Scholar
• Brand K. A., and U. Hermfisse. 1997. Aerobic glycolysis by proliferating cells: a protective strategy against reactive oxygen species. FASEB J. 11: 388–395
   PubMed Web of Science ®Google Scholar
• Yuan M, S. B. Breitkopf, X. Yang, and J. M. Asara. 2012. A positive/negative ion-switching, targeted mass spectrometry-based metabolomics platform for bodily fluids, cells, and fresh and fixed tissue. Nat. Protoc. 7: 872–881
   PubMed Web of Science ®Google Scholar
• Lemasters J. J. 2007. Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism. J. Gastroenterol. Hepatol. 2: S31–S37
   Google Scholar
• Allen T. D., J. M. Cronshaw, S. Bagley, et al. 2000. The nuclear pore complex: mediator of translocation between nucleus and cytoplasm. J. Cell. Sci. 113: 1651–1659
   PubMed Web of Science ®Google Scholar