메뉴 건너뛰기




Volumn 107, Issue 17, 2010, Pages 7927-7932

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

Author keywords

Cholesterol; Huntington's disease; Metabolism; Sirtuin; Transcription factor SREBP 2

Indexed keywords

HUNTINGTIN; SIRTUIN 2; STEROL;

EID: 77952413052     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002924107     Document Type: Article
Times cited : (288)

References (42)
  • 2
    • 35348880250 scopus 로고    scopus 로고
    • Drug targeting of dysregulated transcription in Huntington's disease
    • DOI 10.1016/j.pneurobio.2007.02.005, PII S0301008207000482, Chromatin Dysfunction in Huntington's Disease
    • Kazantsev AG, Hersch SM (2007) Drug targeting of dysregulated transcription in Huntington's disease. Prog Neurobiol 83:249-259. (Pubitemid 47588641)
    • (2007) Progress in Neurobiology , vol.83 , Issue.4 , pp. 249-259
    • Kazantsev, A.G.1    Hersch, S.M.2
  • 3
    • 47249139200 scopus 로고    scopus 로고
    • Huntington's and other polyglutamine diseases: Many effects of single gene mutations
    • Luthi-Carter R (2007) Huntington's and other polyglutamine diseases: Many effects of single gene mutations. Drug Discov Today Dis Mech 4:111-119.
    • (2007) Drug Discov Today Dis Mech , vol.4 , pp. 111-119
    • Luthi-Carter, R.1
  • 5
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan JS, et al. (2001) Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413:739-743.
    • (2001) Nature , vol.413 , pp. 739-743
    • Steffan, J.S.1
  • 6
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante RJ, et al. (2003) Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J Neurosci 23:9418-9427.
    • (2003) J Neurosci , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 9
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • North BJ, Verdin E (2007) Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PLoS One 2:e784.
    • (2007) PLoS One , vol.2
    • North, B.J.1    Verdin, E.2
  • 10
    • 34447638901 scopus 로고    scopus 로고
    • Proteolipid protein is required for transport of sirtuin 2 into CNS myelin
    • Werner HB, et al. (2007) Proteolipid protein is required for transport of sirtuin 2 into CNS myelin. J Neurosci 27:7717-7730.
    • (2007) J Neurosci , vol.27 , pp. 7717-7730
    • Werner, H.B.1
  • 11
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin
    • DOI 10.1523/JNEUROSCI.4181-06.2007
    • Li W, et al. (2007) Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin. J Neurosci 27:2606-2616. (Pubitemid 46393594)
    • (2007) Journal of Neuroscience , vol.27 , Issue.10 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6    Guo, J.7    Ling, E.-A.8    Liang, F.9
  • 13
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • Pallos J, et al. (2008) Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum Mol Genet 17:3767-3775.
    • (2008) Hum Mol Genet , vol.17 , pp. 3767-3775
    • Pallos, J.1
  • 14
    • 70349316621 scopus 로고    scopus 로고
    • Diminished hippocalcin expression in Huntington's disease brain does not account for increased striatal neuron vulnerability as assessed in primary neurons
    • Rudinskiy N, et al. (2009) Diminished hippocalcin expression in Huntington's disease brain does not account for increased striatal neuron vulnerability as assessed in primary neurons. J Neurochem 111:460-472.
    • (2009) J Neurochem , vol.111 , pp. 460-472
    • Rudinskiy, N.1
  • 15
    • 0037947662 scopus 로고    scopus 로고
    • A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila
    • Apostol BL, et al. (2003) A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila. Proc Natl Acad Sci USA 100:5950-5955.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5950-5955
    • Apostol, B.L.1
  • 16
    • 33846930889 scopus 로고    scopus 로고
    • Microtubule deacetylases, SirT2 and HDAC6, in the nervous system
    • DOI 10.1007/s11064-006-9127-6
    • Southwood CM, Peppi M, Dryden S, Tainsky MA, Gow A (2007) Microtubule deacetylases, SirT2 and HDAC6, in the nervous system. Neurochem Res 32:187-195. (Pubitemid 46238864)
    • (2007) Neurochemical Research , vol.32 , Issue.2 , pp. 187-195
    • Southwood, C.M.1    Peppi, M.2    Dryden, S.3    Tainsky, M.A.4    Gow, A.5
  • 17
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003) The human Sir2 ortholog, SIRT2, is an NAD+dependent tubulin deacetylase. Mol Cell 11:437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 18
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • DOI 10.1111/j.1474-9726.2007.00304.x
    • Wang F, Nguyen M, Qin FX-F, Tong Q (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6:505-514. (Pubitemid 47087055)
    • (2007) Aging Cell , vol.6 , Issue.4 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.-F.3    Tong, Q.4
  • 20
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn CL, et al. (2008) Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J Neurosci 28: 10720-10733.
    • (2008) J Neurosci , vol.28 , pp. 10720-10733
    • Benn, C.L.1
  • 21
    • 55749107270 scopus 로고    scopus 로고
    • Dysregulation of gene expression in primary neuron models of Huntington's disease shows that polyglutamine-related effects on the striatal transcriptome may not be dependent on brain circuitry
    • Runne H, et al. (2008) Dysregulation of gene expression in primary neuron models of Huntington's disease shows that polyglutamine-related effects on the striatal transcriptome may not be dependent on brain circuitry. J Neurosci 28:9723-9731.
    • (2008) J Neurosci , vol.28 , pp. 9723-9731
    • Runne, H.1
  • 24
  • 27
    • 55749085638 scopus 로고    scopus 로고
    • Plasma 24S-hydroxycholesterol and caudate MRI in pre-manifest and early Huntington's disease
    • Leoni V, et al. (2008) Plasma 24S-hydroxycholesterol and caudate MRI in pre-manifest and early Huntington's disease. Brain 131:2851-2859.
    • (2008) Brain , vol.131 , pp. 2851-2859
    • Leoni, V.1
  • 28
    • 34249715853 scopus 로고    scopus 로고
    • Huntingtin interacting proteins are genetic modifiers of neurodegeneration
    • Kaltenbach LS, et al. (2007) Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet 3:e82.
    • (2007) PLoS Genet , vol.3
    • Kaltenbach, L.S.1
  • 29
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
    • DOI 10.1016/j.cmet.2007.07.003, PII S155041310700191X
    • Jing E, Gesta S, Kahn CR (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 6:105-114. (Pubitemid 47163621)
    • (2007) Cell Metabolism , vol.6 , Issue.2 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 30
    • 63849221643 scopus 로고    scopus 로고
    • Specific loss of brain ABCA1 increases brain cholesterol uptake and influences neuronal structure and function
    • Karasinska JM, et al. (2009) Specific loss of brain ABCA1 increases brain cholesterol uptake and influences neuronal structure and function. J Neurosci 29:3579-3589.
    • (2009) J Neurosci , vol.29 , pp. 3579-3589
    • Karasinska, J.M.1
  • 31
    • 79954586803 scopus 로고    scopus 로고
    • Cyp46-mediated cholesterol loss promotes survival in stressed hippocampal neurons
    • 10.1016/j.neurobiolaging.2009.04.022
    • Martin M, et al. (2009) Cyp46-mediated cholesterol loss promotes survival in stressed hippocampal neurons. Neurobiol Aging, 10.1016/j.neurobiolaging. 2009.04.022.
    • (2009) Neurobiol Aging
    • Martin, M.1
  • 32
    • 66249083144 scopus 로고    scopus 로고
    • Mitochondrial cholesterol loading exacerbates amyloid beta peptide-induced inflammation and neurotoxicity
    • Fernández A, Llacuna L, Fernández-Checa JC, Colell A (2009) Mitochondrial cholesterol loading exacerbates amyloid beta peptide-induced inflammation and neurotoxicity. J Neurosci 29:6394-6405.
    • (2009) J Neurosci , vol.29 , pp. 6394-6405
    • Fernández, A.1    Llacuna, L.2    Fernández-Checa, J.C.3    Colell, A.4
  • 34
  • 35
    • 58149220667 scopus 로고    scopus 로고
    • Cholesterol in Alzheimer's disease: Unresolved questions
    • Stefani M, Liguri G (2009) Cholesterol in Alzheimer's disease: Unresolved questions. Curr Alzheimer Res 6:15-29.
    • (2009) Curr Alzheimer Res , vol.6 , pp. 15-29
    • Stefani, M.1    Liguri, G.2
  • 36
    • 63849292182 scopus 로고    scopus 로고
    • Molecular consequences of altered neuronal cholesterol biosynthesis
    • Korade Z, Kenworthy AK, Mirnics K (2009) Molecular consequences of altered neuronal cholesterol biosynthesis. J Neurosci Res 87:866-875.
    • (2009) J Neurosci Res , vol.87 , pp. 866-875
    • Korade, Z.1    Kenworthy, A.K.2    Mirnics, K.3
  • 37
    • 0038265008 scopus 로고    scopus 로고
    • Knockout of the cholesterol 24-hydroxylase gene in mice reveals a brain-specific mechanism of cholesterol turnover
    • Lund EG, et al. (2003) Knockout of the cholesterol 24-hydroxylase gene in mice reveals a brain-specific mechanism of cholesterol turnover. J Biol Chem 278:22980-22988.
    • (2003) J Biol Chem , vol.278 , pp. 22980-22988
    • Lund, E.G.1
  • 38
    • 45549102514 scopus 로고    scopus 로고
    • The effect of 24S-hydroxycholesterol on cholesterol homeostasis in neurons: Quantitative changes to the cortical neuron proteome
    • Wang Y, Muneton S, Sjövall J, Jovanovic JN, Griffiths WJ (2008) The effect of 24S-hydroxycholesterol on cholesterol homeostasis in neurons: Quantitative changes to the cortical neuron proteome. J Proteome Res 7:1606-1614.
    • (2008) J Proteome Res , vol.7 , pp. 1606-1614
    • Wang, Y.1    Muneton, S.2    Sjövall, J.3    Jovanovic, J.N.4    Griffiths, W.J.5
  • 39
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated Huntingtin
    • DOI 10.1074/jbc.M508786200
    • Iwata A, Riley BE, Johnston JA, Kopito RR (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280: 40282-40292. (Pubitemid 41779165)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 40
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre JP, et al. (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J Neurosci 27:3571-3583.
    • (2007) J Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1
  • 41
    • 62549132123 scopus 로고    scopus 로고
    • Reduction of cholesterol synthesis in the mouse brain does not affect amyloid formation in Alzheimer's disease, but does extend lifespan
    • Halford RW, Russell DW (2009) Reduction of cholesterol synthesis in the mouse brain does not affect amyloid formation in Alzheimer's disease, but does extend lifespan. Proc Natl Acad Sci USA 106:3502-3506.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3502-3506
    • Halford, R.W.1    Russell, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.