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Volumn 8, Issue 6, 2013, Pages

Pharmacological Activation of Sirt1 Ameliorates Polyglutamine-Induced Toxicity through the Regulation of Autophagy

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY PROTEIN 5; BETA LAPACHONE; GREEN FLUORESCENT PROTEIN; HUNTINGTIN; POLYGLUTAMINE; SHORT HAIRPIN RNA; SIRTINOL; SIRTUIN 1; TRANSCRIPTION FACTOR FKHR;

EID: 84878870713     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0064953     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 8144228406 scopus 로고    scopus 로고
    • Trinucleotide repeats and neurodegenerative disease
    • Everett CM, Wood NW, (2004) Trinucleotide repeats and neurodegenerative disease. Brain 127: 2385-2405.
    • (2004) Brain , vol.127 , pp. 2385-2405
    • Everett, C.M.1    Wood, N.W.2
  • 2
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277: 1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5
  • 3
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology
    • Gutekunst CA, Li SH, Yi H, Mulroy JS, Kuemmerle S, et al. (1999) Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology. J Neurosci 19: 2522-2534.
    • (1999) J Neurosci , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Mulroy, J.S.4    Kuemmerle, S.5
  • 4
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana NR, Zemskov EA, Wang G, Nukina N, (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 10: 1049-1059.
    • (2001) Hum Mol Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 6
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, et al. (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 36: 585-595.
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5
  • 7
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto A, Cremona ML, Rothman JE, (2006) Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J Cell Biol 172: 719-731.
    • (2006) J Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 8
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • Martinez-Vicente M, Talloczy Z, Wong E, Tang G, Koga H, et al. (2010) Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease. Nat Neurosci 13: 567-576.
    • (2010) Nat Neurosci , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3    Tang, G.4    Koga, H.5
  • 9
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuins as potential targets for metabolic syndrome
    • Guarente L, (2006) Sirtuins as potential targets for metabolic syndrome. Nature 444: 868-874.
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 10
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo VD, Kennedy BK, (2006) Sirtuins in aging and age-related disease. Cell 126: 257-268.
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 11
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan S, Sinclair D, (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404: 1-13.
    • (2007) Biochem J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 12
    • 41549138483 scopus 로고    scopus 로고
    • A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
    • Lee IH, Cao L, Mostoslavsky R, Lombard DB, Liu J, et al. (2008) A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci U S A 105: 3374-3379.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3374-3379
    • Lee, I.H.1    Cao, L.2    Mostoslavsky, R.3    Lombard, D.B.4    Liu, J.5
  • 13
    • 0033800922 scopus 로고    scopus 로고
    • Regulation of genes encoding NAD(P)H:quinone oxidoreductases
    • Jaiswal AK, (2000) Regulation of genes encoding NAD(P)H:quinone oxidoreductases. Free Radic Biol Med 29: 254-262.
    • (2000) Free Radic Biol Med , vol.29 , pp. 254-262
    • Jaiswal, A.K.1
  • 14
    • 64649104153 scopus 로고    scopus 로고
    • Pharmacological stimulation of NADH oxidation ameliorates obesity and related phenotypes in mice
    • Hwang JH, Kim DW, Jo EJ, Kim YK, Jo YS, et al. (2009) Pharmacological stimulation of NADH oxidation ameliorates obesity and related phenotypes in mice. Diabetes 58: 965-974.
    • (2009) Diabetes , vol.58 , pp. 965-974
    • Hwang, J.H.1    Kim, D.W.2    Jo, E.J.3    Kim, Y.K.4    Jo, Y.S.5
  • 15
    • 65249124172 scopus 로고    scopus 로고
    • Activation of NAD(P)H:quinone oxidoreductase 1 prevents arterial restenosis by suppressing vascular smooth muscle cell proliferation
    • Kim SY, Jeoung NH, Oh CJ, Choi YK, Lee HJ, et al. (2009) Activation of NAD(P)H:quinone oxidoreductase 1 prevents arterial restenosis by suppressing vascular smooth muscle cell proliferation. Circ Res 104: 842-850.
    • (2009) Circ Res , vol.104 , pp. 842-850
    • Kim, S.Y.1    Jeoung, N.H.2    Oh, C.J.3    Choi, Y.K.4    Lee, H.J.5
  • 16
    • 84867428923 scopus 로고    scopus 로고
    • Beta-Lapachone, a Modulator of NAD Metabolism, Prevents Health Declines in Aged Mice
    • Lee JS, Park AH, Lee SH, Kim JH, Yang SJ, et al. (2012) Beta-Lapachone, a Modulator of NAD Metabolism, Prevents Health Declines in Aged Mice. PLoS One 7: e47122.
    • (2012) PLoS One , vol.7
    • Lee, J.S.1    Park, A.H.2    Lee, S.H.3    Kim, J.H.4    Yang, S.J.5
  • 17
    • 33644771265 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin
    • Wang H, Lim PJ, Yin C, Rieckher M, Vogel BE, et al. (2006) Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin. Hum Mol Genet 15: 1025-1041.
    • (2006) Hum Mol Genet , vol.15 , pp. 1025-1041
    • Wang, H.1    Lim, P.J.2    Yin, C.3    Rieckher, M.4    Vogel, B.E.5
  • 18
    • 67651210858 scopus 로고    scopus 로고
    • SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1
    • Rajamohan SB, Pillai VB, Gupta M, Sundaresan NR, Birukov KG, et al. (2009) SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol Cell Biol 29: 4116-4129.
    • (2009) Mol Cell Biol , vol.29 , pp. 4116-4129
    • Rajamohan, S.B.1    Pillai, V.B.2    Gupta, M.3    Sundaresan, N.R.4    Birukov, K.G.5
  • 19
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes
    • Frescas D, Valenti L, Accili D, (2005) Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J Biol Chem 280: 20589-20595.
    • (2005) J Biol Chem , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 20
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • Brignull HR, Moore FE, Tang SJ, Morimoto RI, (2006) Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J Neurosci 26: 7597-7606.
    • (2006) J Neurosci , vol.26 , pp. 7597-7606
    • Brignull, H.R.1    Moore, F.E.2    Tang, S.J.3    Morimoto, R.I.4
  • 21
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ, Morimoto RI, (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci U S A 99: 10417-10422.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 22
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY, Orr HT, (2000) Glutamine repeats and neurodegeneration. Annu Rev Neurosci 23: 217-247.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 23
    • 2342598416 scopus 로고    scopus 로고
    • Experimental therapeutics in transgenic mouse models of Huntington's disease
    • Beal MF, Ferrante RJ, (2004) Experimental therapeutics in transgenic mouse models of Huntington's disease. Nat Rev Neurosci 5: 373-384.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 373-384
    • Beal, M.F.1    Ferrante, R.J.2
  • 24
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker JA, Arango M, Abderrahmane S, Lambert E, Tourette C, et al. (2005) Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat Genet 37: 349-350.
    • (2005) Nat Genet , vol.37 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3    Lambert, E.4    Tourette, C.5
  • 25
    • 84865704833 scopus 로고    scopus 로고
    • Integration of beta-catenin, sirtuin, and FOXO signaling protects from mutant huntingtin toxicity
    • Parker JA, Vazquez-Manrique RP, Tourette C, Farina F, Offner N, et al. (2012) Integration of beta-catenin, sirtuin, and FOXO signaling protects from mutant huntingtin toxicity. J Neurosci 32: 12630-12640.
    • (2012) J Neurosci , vol.32 , pp. 12630-12640
    • Parker, J.A.1    Vazquez-Manrique, R.P.2    Tourette, C.3    Farina, F.4    Offner, N.5
  • 26
    • 84855544817 scopus 로고    scopus 로고
    • Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets
    • Jiang M, Wang J, Fu J, Du L, Jeong H, et al. (2011) Neuroprotective role of Sirt1 in mammalian models of Huntington's disease through activation of multiple Sirt1 targets. Nat Med 18: 153-158.
    • (2011) Nat Med , vol.18 , pp. 153-158
    • Jiang, M.1    Wang, J.2    Fu, J.3    Du, L.4    Jeong, H.5
  • 27
    • 84855563516 scopus 로고    scopus 로고
    • Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway
    • Jeong H, Cohen DE, Cui L, Supinski A, Savas JN, et al. (2011) Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway. Nat Med 18: 159-165.
    • (2011) Nat Med , vol.18 , pp. 159-165
    • Jeong, H.1    Cohen, D.E.2    Cui, L.3    Supinski, A.4    Savas, J.N.5
  • 28
    • 26444515364 scopus 로고    scopus 로고
    • Autophagy and its possible roles in nervous system diseases, damage and repair
    • Rubinsztein DC, DiFiglia M, Heintz N, Nixon RA, Qin ZH, et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1: 11-22.
    • (2005) Autophagy , vol.1 , pp. 11-22
    • Rubinsztein, D.C.1    DiFiglia, M.2    Heintz, N.3    Nixon, R.A.4    Qin, Z.H.5
  • 29
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC, (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443: 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 30
    • 77749319356 scopus 로고    scopus 로고
    • Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
    • Bauer PO, Goswami A, Wong HK, Okuno M, Kurosawa M, et al. (2010) Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein. Nat Biotechnol 28: 256-263.
    • (2010) Nat Biotechnol , vol.28 , pp. 256-263
    • Bauer, P.O.1    Goswami, A.2    Wong, H.K.3    Okuno, M.4    Kurosawa, M.5
  • 31
    • 67349273985 scopus 로고    scopus 로고
    • SIRT1: regulation of longevity via autophagy
    • Salminen A, Kaarniranta K, (2009) SIRT1: regulation of longevity via autophagy. Cell Signal 21: 1356-1360.
    • (2009) Cell Signal , vol.21 , pp. 1356-1360
    • Salminen, A.1    Kaarniranta, K.2
  • 32
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME, (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 33
    • 77955359169 scopus 로고    scopus 로고
    • Quantitative relationships between huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis
    • Miller J, Arrasate M, Shaby BA, Mitra S, Masliah E, et al. (2010) Quantitative relationships between huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis. J Neurosci 30: 10541-10550.
    • (2010) J Neurosci , vol.30 , pp. 10541-10550
    • Miller, J.1    Arrasate, M.2    Shaby, B.A.3    Mitra, S.4    Masliah, E.5
  • 35
    • 0018131050 scopus 로고
    • Generation of superoxide anions and hydrogen peroxide from beta-lapachone in bacteria
    • Cruz FS, Docampo R, Boveris A, (1978) Generation of superoxide anions and hydrogen peroxide from beta-lapachone in bacteria. Antimicrob Agents Chemother 14: 630-633.
    • (1978) Antimicrob Agents Chemother , vol.14 , pp. 630-633
    • Cruz, F.S.1    Docampo, R.2    Boveris, A.3
  • 38
    • 0034653956 scopus 로고    scopus 로고
    • Activation of a cysteine protease in MCF-7 and T47D breast cancer cells during beta-lapachone-mediated apoptosis
    • Pink JJ, Wuerzberger-Davis S, Tagliarino C, Planchon SM, Yang X, et al. (2000) Activation of a cysteine protease in MCF-7 and T47D breast cancer cells during beta-lapachone-mediated apoptosis. Exp Cell Res 255: 144-155.
    • (2000) Exp Cell Res , vol.255 , pp. 144-155
    • Pink, J.J.1    Wuerzberger-Davis, S.2    Tagliarino, C.3    Planchon, S.M.4    Yang, X.5
  • 39
    • 1542537372 scopus 로고    scopus 로고
    • Suppression of human prostate cancer cell growth by beta-lapachone via down-regulation of pRB phosphorylation and induction of Cdk inhibitor p21(WAF1/CIP1)
    • Choi YH, Kang HS, Yoo MA, (2003) Suppression of human prostate cancer cell growth by beta-lapachone via down-regulation of pRB phosphorylation and induction of Cdk inhibitor p21(WAF1/CIP1). J Biochem Mol Biol 36: 223-229.
    • (2003) J Biochem Mol Biol , vol.36 , pp. 223-229
    • Choi, Y.H.1    Kang, H.S.2    Yoo, M.A.3
  • 40
    • 33745849783 scopus 로고    scopus 로고
    • Beta-lapachone, a quinone isolated from Tabebuia avellanedae, induces apoptosis in HepG2 hepatoma cell line through induction of Bax and activation of caspase
    • Woo HJ, Park KY, Rhu CH, Lee WH, Choi BT, et al. (2006) Beta-lapachone, a quinone isolated from Tabebuia avellanedae, induces apoptosis in HepG2 hepatoma cell line through induction of Bax and activation of caspase. J Med Food 9: 161-168.
    • (2006) J Med Food , vol.9 , pp. 161-168
    • Woo, H.J.1    Park, K.Y.2    Rhu, C.H.3    Lee, W.H.4    Choi, B.T.5
  • 41
    • 79960611530 scopus 로고    scopus 로고
    • An engineered viral protease exhibiting substrate specificity for a polyglutamine stretch prevents polyglutamine-induced neuronal cell death
    • Sellamuthu S, Shin BH, Han HE, Park SM, Oh HJ, et al. (2011) An engineered viral protease exhibiting substrate specificity for a polyglutamine stretch prevents polyglutamine-induced neuronal cell death. PLoS One 6: e22554.
    • (2011) PLoS One , vol.6
    • Sellamuthu, S.1    Shin, B.H.2    Han, H.E.3    Park, S.M.4    Oh, H.J.5
  • 42
    • 34249692543 scopus 로고    scopus 로고
    • Systematic uncovering of multiple pathways underlying the pathology of Huntington disease by an acid-cleavable isotope-coded affinity tag approach
    • Chiang MC, Juo CG, Chang HH, Chen HM, Yi EC, et al. (2007) Systematic uncovering of multiple pathways underlying the pathology of Huntington disease by an acid-cleavable isotope-coded affinity tag approach. Mol Cell Proteomics 6: 781-797.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 781-797
    • Chiang, M.C.1    Juo, C.G.2    Chang, H.H.3    Chen, H.M.4    Yi, E.C.5
  • 44
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S, (1974) The genetics of Caenorhabditis elegans. Genetics 77: 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 45
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A, Xu S, Montgomery MK, Kostas SA, Driver SE, et al. (1998) Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391: 806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.