Page 386 - Read Online

Page 16 of 18 Yelton et al. Neuroimmunol Neuroinflammation 2018;5:46 I http://dx.doi.org/10.20517/2347-8659.2018.58

13. Barker CF, Billingham RE. Immunologically privileged sites. Adv Immunol 1977;25:1-54.
14. Carson MJ, Doose JM, Melchior B, Schmid CD, Ploix CC. CNS immune privilege: hiding in plain sight. Immunol Rev 2006;213:48-65.
15. Keaney J, Campbell M. The dynamic blood-brain barrier. FEBS J 2015;282:4067-79.
16. Wolburg H, Noell S, Fallier-Becker P, Mack AF, Wolburg-Buchholz K. The disturbed blood-brain barrier in human glioblastoma. Mol
Aspects Med 2012;33:579-89.
17. Reardon DA, Wen PY, Wucherpfennig KW, Sampson JH. Immunomodulation for glioblastoma. Curr Opin Neurol 2017;30:361-9.
18. Allen BK, Stathias V, Maloof ME, Vidovic D, Winterbottom EF, et al. Epigenetic pathways and glioblastoma treatment: insights from
signaling cascades. J Cell Biochem 2015;116:351-63.
19. Adamopoulou E, Naumann U. HDAC inhibitors and their potential applications to glioblastoma therapy. Oncoimmunology
2013;2:e25219.
20. Ropero S, Esteller M. The role of histone deacetylases (HDACs) in human cancer. Mol Oncol 2007;1:19-25.
21. Hrabeta J, Stiborova M, Adam V, Kizek R, Eckschlager T. Histone deacetylase inhibitors in cancer therapy. A review. Biomed Pap Med
Fac Univ Palacky Olomouc Czech Repub 2014;158:161-9.
22. Höring E, Podlech O, Silkenstedt B, Rota IA, Adamopoulou E, et al. The histone deacetylase inhibitor trichostatin a promotes apoptosis
and antitumor immunity in glioblastoma cells. Anticancer Res 2013;33:1351-60.
23. Inoue A, Fujimoto D. Enzymatic deacetylation of histone. Biochem Biophys Res Commun 1969;36:146-50.
24. Seto E, Yoshida M. Erasers of histone acetylation: the histone deacetylase enzymes. Cold Spring Harb Perspect Biol 2014;6:a018713.
25. Taunton J, Hassig CA, Schreiber SL. A mammalian histone deacetylase related to the yeast transcriptional regulatory Rpd3p. Science
1996;272:408-11.
26. Weichert W. HDAC expression and clinical prognosis in human malignancies. Cancer Lett 2009;280:168-76.
27. Imai S, Armstrong CM, Kaeberlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone
deacetylase. Nature 2000;403:795-800.
28. Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis.
Proc Natl Acad Sci U S A 1964;51:786-94.
29. Wang Z, Zang C, Cui K, Schones DE, Barski A, et al. Genome-wide mapping of HATs and HDACs reveals distinct functions in active
and inactive genes. Cell 2009;138:1019-31.
30. Kim E, Bisson WH, Löhr CV, Williams DE, Ho E, et al. Histone and non-histone targets of dietary deacetylase inhibitors. Curr Top
Med Chem 2016;16:714-31.
31. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, et al. Lysine acetylation targets protein complexes and co-regulates major
cellular functions. Science 2009;325:834-40.
32. Parbin S, Kar S, Shilpi A, Sengupta D, Deb M, et al. Histone deacetylases: a saga of perturbed acetylation homeostasis in cancer. J
Histochem Cytochem 2014;62:11-33.
33. Falkenberg KJ, Johnstone RW. Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat Rev
Drug Discov 2014;13:673-91.
34. Dawson MA, Kouzarides T. Cancer epigenetics: from mechanism to therapy. Cell 2012;150:12-27.
35. Ropero S, Fraga MF, Ballestar E, Hamelin R, Yamamoto H, et al. A truncating mutation of HDAC2 in human cancers confers resistance
to histone deacetylase inhibition. Nat Genet 2006;38:566-9.
36. Li Y, Seto E. HDACs and HDAC inhibitors in cancer development and therapy. Cold Spring Harb Perspect Med 2016; doi: 10.1101/
cshperspect.a026831.
37. West AC, Johnstone RW. New and emerging HDAC inhibitors for cancer treatment. J Clin Invest 2014;124:30-9.
38. Lucio-Eterovic AK, Cortez MA, Valera ET, Motta FJ, Queiroz RG, et al. Differential expression of 12 histone deacetylase (HDAC)
genes in astrocytomas and normal brain tissue: class II and IV are hypoexpressed in glioblastomas. BMC Cancer 2008;8:243.
39. Nagarajan RP, Costello JF. Epigenetic mechanisms in glioblastoma multiforme. Sem Cancer Biol 2009;19:188-97.
40. Parsons DW, Jones S, Zhang X, Lin JC, Leary RJ, et al. An integrated genomic analysis of human glioblastoma multiforme. Science
2008;321:1807-12.
41. Lee DH, Ryu HW, Won HR, Kwon SH. Advances in epigenetic glioblastoma therapy. Oncotarget 2017;8:18577-89.
42. Staberg M, Michaelsen SR, Rasmussen RD, Villingshøj M, Poulsen HS, et al. Inhibition of histone deacetylases sensitizes glioblastoma
cells to loumustine. Cell Oncol (Dordr) 2017;40:21-32.
43. Yang Y. Cancer immunotherapy: harnessing the immune system to battle cancer. J Clin Invest 2015;125:3335-7.
44. Feng J, Yan PF, Zhao HY, Zhang FC, Zhao WH, et al. SIRT6 suppresses glioma cell growth via induction of apoptosis, inhibition of
oxidative stress, and suppression of JAK2/STAT3 signaling pathway activation. Oncol Rep 2016;35:1395-402.
45. Romeo SG, Conti A, Polito F, Tomasello C, Barresi V, et al. miRNA regulation of sirtuin-1 expression in human astrocytoma. Oncol
Lett 2016;12:2992-8.
46. Pruitt K, Zinn RL, Ohm JE, McGarvey KM, Kang SH, et al. Inhibition of SIRT1 reactivates silenced cancer genes without loss of
promoter DNA hypermethylation. PLoS Genet 2006;2:e40.
47. Deng CX. SIRT1, is it a tumor promoter or tumor suppressor? Int J Biol Sci 2009;5:147-52.
48. Riggs MG, Whittaker RG, Neumann JR, Ingram VM. n-Butyrate causes histone modification in HeLa and friend erythroleukaemia
cells. Nature 1977;268:462-4.
49. Candido EP, Reeves R, Davie JR. Sodium butyrate inhibitis histone deacetylation in cultured cells. Cell 1978;14:105-13.
50. Yoshida M, Kijima M, Akita M, Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by
trichostatin A. J Biol Chem 1990;265:17174-9.
51. Kijima M, Yoshida M, Sugita K, Horinouchi S, Beppu T. Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of
mammalian histone deacetylase. J Biol Chem 1993;268:22429-35.