SIRT1 is decreased during relapses in patients with multiple sclerosis

Experimental and Molecular Pathology

Volumn 96, Issue 2, 2014, Pages 139-148

  Tegla, Cosmin A ^a,b   Azimzadeh, Philippe ^a   Andrian Albescu, Maria ^a   Martin, Alvaro ^a   Cudrici, Cornelia D ^a   Trippe, Richard ^a   Sugarman, Adam ^a   Chen, Hegang ^a   Boodhoo, Dallas ^a   Vlaicu, Sonia I ^a   Royal, Walter ^a,c   Bever, Christopher ^a,b,c   Rus, Violeta ^a   Rus, Horea ^a,b,c  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b VETERANS AFFAIRS MEDICAL CENTER   (United States)

^c Veterans Administration Multiple Sclerosis Center of Excellence   (United States)

Author keywords

Acetylation; Biomarker; Epigenetics; HDAC3; Multiple sclerosis; Peripheral blood mononuclear cells; RGC 32; SIRT1

Indexed keywords

BIOLOGICAL MARKER; CD4 ANTIGEN; CD8 ANTIGEN; FAS LIGAND; GLIAL FIBRILLARY ACIDIC PROTEIN; HISTONE DEACETYLASE 3; HISTONE H3; MESSENGER RNA; PROTEIN H3K9; PROTEIN RGC 32; SIRTUIN 1; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; HISTONE; HISTONE DEACETYLASE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; MUSCLE PROTEIN; NERVE PROTEIN; RGC32 PROTEIN, HUMAN; SIRT1 PROTEIN, HUMAN;

ADULT; AGED; APOPTOSIS; ARTICLE; BRAIN CELL; CD4+ T LYMPHOCYTE; CD8+ T LYMPHOCYTE; CLINICAL ARTICLE; FEMALE; GENE SILENCING; HISTONE ACETYLATION; HISTONE METHYLATION; HUMAN; HUMAN CELL; HUMAN TISSUE; LYMPHOCYTE COUNT; MALE; MULTIPLE SCLEROSIS; OLIGODENDROGLIA; PERIPHERAL BLOOD MONONUCLEAR CELL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; REGULATORY MECHANISM; RELAPSE; ACETYLATION; ADOLESCENT; BIOSYNTHESIS; BLOOD; BRAIN; CELL LINE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MIDDLE AGED; MONONUCLEAR CELL; PATHOLOGY;

ACETYLATION; ADOLESCENT; ADULT; AGED; APOPTOSIS; BIOLOGICAL MARKERS; BRAIN; CELL CYCLE PROTEINS; CELL LINE; FEMALE; GENE EXPRESSION REGULATION; HISTONE DEACETYLASES; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LEUKOCYTES, MONONUCLEAR; MALE; MIDDLE AGED; MULTIPLE SCLEROSIS; MUSCLE PROTEINS; NERVE TISSUE PROTEINS; RNA, MESSENGER; SIRTUIN 1;

EID: 84894224833     PISSN: 00144800     EISSN: 10960945     Source Type: Journal    
DOI: 10.1016/j.yexmp.2013.12.010     Document Type: Article

References (51)

1. Badea T., et al. RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle cells into S-phase. J Biol Chem. 2002, 277:502-508.
2. Badea T.C., et al. Molecular cloning and characterization of RGC-32, a novel gene induced by complement activation in oligodendrocytes. J Biol Chem. 1998, 273:26977-26981.
3. Baur J.A. Biochemical effects of SIRT1 activators. Biochim Biophys Acta 2010, 1804:1626-1634.
4. Bouras T., et al. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J Biol Chem. 2005, 280:10264-10276.
5. Brunet A., et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science. 2004, 303:2011-2015.
6. Camelo S., et al. Transcriptional therapy with the histone deacetylase inhibitor trichostatin A ameliorates experimental autoimmune encephalomyelitis. J Neuroimmunol. 2005, 164:10-21.
7. Chen D., et al. Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 2008, 22:1753-1757.
8. Compston A., Coles A. Multiple sclerosis. Lancet. 2008, 372:1502-1517.
9. Costantino C.M., et al. Multiple sclerosis and regulatory T cells. J Clin Immunol. 2008, 28:697-706.
10. Cudrici C., et al. Dendritic cells are abundant in non-lesional gray matter in multiple sclerosis. Exp Mol Pathol. 2007, 83:198-206.
11. Fonseca-Kelly Z., et al. Resveratrol neuroprotection in a chronic mouse model of multiple sclerosis. Front Neurol. 2012, 3:84.
12. Fosbrink M., et al. Overexpression of RGC-32 in colon cancer and other tumors. Exp Mol Pathol. 2005, 78:116-122.
13. Frohman E.M., et al. Multiple sclerosis - the plaque and its pathogenesis. New Engl J Med. 2006, 354:942-955.
14. Guarente L. Franklin H. Epstein lecture: sirtuins, aging, and medicine. N Engl J Med 2011, 364:2235-2244.
15. He W., et al. Mitochondrial sirtuins: regulators of protein acylation and metabolism. Trends Endocrinol Metab. 2012, 23:467-476.
16. Imai S., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 2000, 403:795-800.
17. Imler T.J., Petro T.M. Decreased severity of experimental autoimmune encephalomyelitis during resveratrol administration is associated with increased IL-17+IL-10+ T cells, CD4- IFN-γ+cells, and decreased macrophage IL-6 expression. Int Immunopharmacol. 2009, 9:134-143.
18. Keegan B.M., Noseworthy J.H. Multiple sclerosis. Annu. Rev. Med. 2002, 53:285-302.
19. Koch M.W., et al. Epigenetic changes in patients with multiple sclerosis. Nat Rev Neurol. 2013, 9:35-43.
20. Koch M.W., et al. Epigenetics and miRNAs in the diagnosis and treatment of multiple sclerosis. Trends Mol Med. 2013, 19:23-30.
21. Kurtzke J.F. Rating neurologic impairment in multiple sclerosis: an expanded disability status scale (EDSS). Neurology. 1983, 33:1444-1452.
22. Lopatinskaya L., et al. The development of clinical activity in relapsing-remitting MS is associated with a decrease of FasL mRNA and an increase of Fas mRNA in peripheral blood. J Neuroimmunol. 2003, 138:123-131.
23. Luo J., et al. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 2000, 408:377-381.
24. Martinez-Pasamar S., et al. Dynamic cross-regulation of antigen-specific effector and regulatory T cell subpopulations and microglia in brain autoimmunity. BMC Syst Biol. 2013, 7:34.
25. McDonald W.I., et al. Recommended diagnostic criteria for multiple sclerosis: guidelines from the International Panel on the diagnosis of multiple sclerosis. Ann Neurol. 2001, 50:121-127.
26. Motta M.C., et al. Mammalian SIRT1 represses forkhead transcription factors. Cell. 2004, 116:551-563.
27. Niculescu F., et al. Activation of Ras and mitogen-activated protein kinase pathway by terminal complement complexes is G protein dependent. J Immunol. 1997, 158:4405-4412.
28. Nimmagadda V.K., et al. Overexpression of SIRT1 protein in neurons protects against experimental autoimmune encephalomyelitis through activation of multiple SIRT1 targets. J Immunol. 2013, 190:4595-4607.
29. Penberthy W.T., Tsunoda I. The importance of NAD in multiple sclerosis. Curr Pharm Des. 2009, 15:64-99.
30. Petro T.M. Regulatory role of resveratrol on Th17 in autoimmune disease. Int Immunopharmacol. 2011, 11:310-318.
31. Polman C.H., et al. Diagnostic criteria for multiple sclerosis: 2005 revisions to the "McDonald Criteria". Ann Neurol. 2005, 58:840-846.
32. Rus H.G., et al. Sublytic complement attack induces cell cycle in oligodendrocytes. J Immunol. 1996, 156:4892-4900.
33. Rus H.G., et al. Interleukin-6 and interleukin-8 protein and gene expression in human arterial atherosclerotic wall. Atherosclerosis. 1996, 127:263-271.
34. Sasaki T., et al. Phosphorylation regulates SIRT1 function. PLoS One. 2008, 3:e4020.
35. Sengupta N., Seto E. Regulation of histone deacetylase activities. J Cell Biochem. 2004, 93:57-67.
36. Shindler K.S., et al. Oral resveratrol reduces neuronal damage in a model of multiple sclerosis. J Neuroophthalmol. 2010, 30:328-339.
37. Singh N.P., et al. Resveratrol (trans-3,5,4'-Trihydroxystilbene) ameliorates experimental allergic encephalomyelitis. Primarily via induction of apoptosis in t cells involving activation of aryl hydrocarbon receptor and estrogen receptor. Mol Pharmacol. 2007, 72:1508-1521.
38. +-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A. 2000, 97:6658-6663.
39. Tegla C.A., et al. Dual role of Response gene to complement-32 in multiple sclerosis. Exp Mol Pathol. 2013, 94:17-28.
40. Turner B.M. Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell Mol Life Sci. 1998, 54:21-31.
41. Vaquero A., et al. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature. 2007, 450:440-444.
42. Vaquero A., et al. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell. 2004, 16:93-105.
43. Vlaicu S.I., et al. Role of C5b-9 complement complex and response gene to complement-32 (RGC-32) in cancer. Immunol Res. 2013, 56:109-121.
44. Vlaicu S.I., et al. Epigenetic modifications induced by RGC-32 in colon cancer. Exp Mol Pathol. 2010, 88:67-76.
45. Wang C., et al. Visualizing epigenetics: current advances and advantages in HDAC PET imaging techniques. Neuroscience 2013, 10.1016/j. neuroscience. 2013.09.018.
46. Wang P., et al. Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1-dependent adenosine monophosphate-activated kinase pathway. Ann Neurol. 2011, 69:360-374.
47. Yeung F., et al. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 2004, 23:2369-2380.
48. Zhang F., et al. Role of HDAC3 on p53 expression and apoptosis in T cells of patients with multiple sclerosis. PLoS One. 2011, 6:e16795.
49. Zhang J., et al. The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice. J Clin Invest. 2009, 119:3048-3058.
50. + metabolism and signaling to the control of cellular functions. Biochim Biophys Acta 2010, 1804:1666-1675.
51. Zhang X., et al. Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes Dev. 2005, 19:827-839.