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Volumn 58, Issue 4, 2011, Pages 512-520

The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells

Author keywords

Synuclein; Autophagy lysosomal pathway; Chaperones; DJ 1; Glutathione; p Tau; Parkinson's disease; Proteasome activity; Tau; Ubiquitination

Indexed keywords

ALPHA SYNUCLEIN; CHAPERONE; DISACCHARIDE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPOXOMICIN; FREE RADICAL; GLUTATHIONE; HEAT SHOCK PROTEIN 70; MITOCHONDRIAL PROTEIN; POL PROTEIN; POLYUBIQUITIN; PROTEASOME; PROTEIN; SCAVENGER; SYNUCLEIN; TAU PROTEIN; TREHALOSE; UBIQUITIN;

EID: 79952104480     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2011.01.008     Document Type: Article
Times cited : (95)

References (52)
  • 2
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • DOI 10.1016/S0014-5793(04)00326-6, PII S0014579304003266
    • A. Arora, C. Ha, and C.B. Park Inhibition of insulin amyloid formation by small stress molecules FEBS Lett. 564 2004 121 125 (Pubitemid 38490710)
    • (2004) FEBS Letters , vol.564 , Issue.1-2 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 5
    • 0347124698 scopus 로고    scopus 로고
    • Selective and persistent activation of extracellular signal-regulated protein kinase by nitric oxide in glial cells induces neuronal degeneration in glutathione-depleted midbrain cultures
    • DOI 10.1016/j.mcn.2003.08.004
    • S. Canals, M.J. Casarejos, S. de Bernardo, R.M. Solano, and M.A. Mena Selective and persistent activation of extracellular signal-regulated protein kinase by nitric oxide in glial cells induces neuronal degeneration in glutathione-depleted midbrain cultures Mol. Cell. Neurosci. 24 2003 1012 1026 (Pubitemid 38091513)
    • (2003) Molecular and Cellular Neuroscience , vol.24 , Issue.4 , pp. 1012-1026
    • Canals, S.1    Casarejos, M.J.2    De Bernardo, S.3    Solano, R.M.4    Mena, M.A.5
  • 6
    • 23844529467 scopus 로고    scopus 로고
    • Differential effects of L-DOPA on monoamine metabolism, cell survival and glutathione production in midbrain neuronal-enriched cultures from parkin knockout and wild-type mice
    • DOI 10.1111/j.1471-4159.2005.03249.x
    • M.J. Casarejos, R.M. Solano, J. Menendez, J.A. Rodriguez-Navarro, C. Correa, J. Garcia de Yebenes, and M.A. Mena Differential effects of l-DOPA on monoamine metabolism, cell survival and glutathione production in midbrain neuronal-enriched cultures from parkin knockout and wild-type mice J. Neurochem. 94 2005 1005 1014 (Pubitemid 41170588)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.4 , pp. 1005-1014
    • Casarejos, M.J.1    Solano, R.M.2    Menendez, J.3    Rodriguez-Navarro, J.A.4    Correa, C.5    Garcia De Yebenes, J.6    Mena, M.A.7
  • 7
    • 68949208061 scopus 로고    scopus 로고
    • Parkin deficiency increases the resistance of midbrain neurons and glia to mild proteasome inhibition: The role of autophagy and glutathione homeostasis
    • M.J. Casarejos, R.M. Solano, J.A. Rodriguez-Navarro, A. Gomez, J. Perucho, J.G. Castano, J. Garcia de Yebenes, and M.A. Mena Parkin deficiency increases the resistance of midbrain neurons and glia to mild proteasome inhibition: the role of autophagy and glutathione homeostasis J. Neurochem. 110 2009 1523 1537
    • (2009) J. Neurochem. , vol.110 , pp. 1523-1537
    • Casarejos, M.J.1    Solano, R.M.2    Rodriguez-Navarro, J.A.3    Gomez, A.4    Perucho, J.5    Castano, J.G.6    Garcia De Yebenes, J.7    Mena, M.A.8
  • 8
    • 4644236078 scopus 로고    scopus 로고
    • Role of trehalose phosphate synthase and trehalose during hypoxia: From flies to mammals
    • DOI 10.1242/jeb.01133
    • Q. Chen, and G.G. Haddad Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals J. Exp. Biol. 207 2004 3125 3129 (Pubitemid 39275286)
    • (2004) Journal of Experimental Biology , vol.207 , Issue.18 , pp. 3125-3129
    • Chen, Q.1    Haddad, G.G.2
  • 10
    • 49849088116 scopus 로고    scopus 로고
    • Aggregopathy in neurodegenerative diseases: Mechanisms and therapeutic implication
    • C.P. Dohm, P. Kermer, and M. Bahr Aggregopathy in neurodegenerative diseases: mechanisms and therapeutic implication Neurodegener. Dis. 5 2008 321 338
    • (2008) Neurodegener. Dis. , vol.5 , pp. 321-338
    • Dohm, C.P.1    Kermer, P.2    Bahr, M.3
  • 13
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • E. Itakura, and N. Mizushima Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins Autophagy 6 2010 764 776
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 14
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • N.K. Jain, and I. Roy Effect of trehalose on protein structure Protein Sci. 18 2009 24 36
    • (2009) Protein Sci. , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 17
    • 69449090071 scopus 로고    scopus 로고
    • A novel link between autophagy and the ubiquitin-proteasome system
    • V.I. Korolchuk, F.M. Menzies, and D.C. Rubinsztein A novel link between autophagy and the ubiquitin-proteasome system Autophagy 5 2009 862 863
    • (2009) Autophagy , vol.5 , pp. 862-863
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 18
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42
    • DOI 10.1016/j.nbd.2005.02.003, PII S0969996105000628
    • R. Liu, H. Barkhordarian, S. Emadi, C.B. Park, and M.R. Sierks Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42 Neurobiol. Dis. 20 2005 74 81 (Pubitemid 41219204)
    • (2005) Neurobiology of Disease , vol.20 , Issue.1 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Chan, B.P.4    Sierks, M.R.5
  • 19
    • 7244243876 scopus 로고    scopus 로고
    • Stabilization of α-synuclein protein with aging and familial Parkinson's disease-linked A53T mutation
    • DOI 10.1523/JNEUROSCI.1370-04.2004
    • W. Li, C. Lesuisse, Y. Xu, J. Troncoso, C. Price, and M.K. D.L. Lee Stabilization of alpha-synuclein protein with aging and familial Parkinson's disease-linked A53T mutation J. Neurosci. 24 2004 7400 7409 (Pubitemid 39100708)
    • (2004) Journal of Neuroscience , vol.24 , Issue.33 , pp. 7400-7409
    • Li, W.1    Lesuisse, C.2    Xu, Y.3    Troncoso, J.C.4    Price, D.L.5    Lee, M.K.6
  • 20
    • 70349849851 scopus 로고    scopus 로고
    • Proteasome inhibition increases tau accumulation independent of phosphorylation
    • Y.H. Liu, W. Wei, J. Yin, G.P. Liu, Q. Wang, F.Y. Cao, and J.Z. Wang Proteasome inhibition increases tau accumulation independent of phosphorylation Neurobiol. Aging 30 2009 1949 1961
    • (2009) Neurobiol. Aging , vol.30 , pp. 1949-1961
    • Liu, Y.H.1    Wei, W.2    Yin, J.3    Liu, G.P.4    Wang, Q.5    Cao, F.Y.6    Wang, J.Z.7
  • 21
    • 42649103288 scopus 로고    scopus 로고
    • Proteasome inhibitors prevent oxidative stress-induced nerve cell death by a novel mechanism
    • P. Maher Proteasome inhibitors prevent oxidative stress-induced nerve cell death by a novel mechanism Biochem. Pharmacol. 75 2008 1994 2006
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 1994-2006
    • Maher, P.1
  • 22
    • 68149156531 scopus 로고    scopus 로고
    • Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: How neurons are lost in the Bermuda triangle
    • K.A. Malkus, E. Tsika, and H. Ischiropoulos Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle Mol. Neurodegener. 4 2009 24
    • (2009) Mol. Neurodegener. , vol.4 , pp. 24
    • Malkus, K.A.1    Tsika, E.2    Ischiropoulos, H.3
  • 23
    • 75149126921 scopus 로고    scopus 로고
    • Does impairment of the ubiquitin-proteasome system or the autophagy-lysosome pathway predispose individuals to neurodegenerative disorders such as Parkinson's disease?
    • N. Matsuda, and K. Tanaka Does impairment of the ubiquitin-proteasome system or the autophagy-lysosome pathway predispose individuals to neurodegenerative disorders such as Parkinson's disease? J. Alzheimers Dis. 19 2010 1 9
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 1-9
    • Matsuda, N.1    Tanaka, K.2
  • 24
    • 79952103181 scopus 로고    scopus 로고
    • From model system to clinical medicine: Pathophysiologic links of common proteinopathies
    • P.J. McMillan, and J.B. Leverenz From model system to clinical medicine: pathophysiologic links of common proteinopathies Alzheimers Res. Ther. 2 2010 26
    • (2010) Alzheimers Res. Ther. , vol.2 , pp. 26
    • McMillan, P.J.1    Leverenz, J.B.2
  • 26
    • 33746839220 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced model of Parkinson's disease
    • DOI 10.1002/ana.20936
    • K.S. McNaught, and C.W. Olanow Proteasome inhibitor-induced model of Parkinson's disease Ann. Neurol. 60 2006 243 247 (Pubitemid 44182399)
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 243-247
    • McNaught, K.S.P.1    Olanow, C.W.2
  • 27
    • 0028785046 scopus 로고
    • Effects of dibutyryl cyclic AMP and retinoic acid on the differentiation of dopamine neurons: Prevention of cell death by dibutyryl cyclic AMP
    • M.A. Mena, M.J. Casarejos, A. Bonin, J.A. Ramos, and J. Garcia Yebenes Effects of dibutyryl cyclic AMP and retinoic acid on the differentiation of dopamine neurons: prevention of cell death by dibutyryl cyclic AMP J. Neurochem. 65 1995 2612 2620
    • (1995) J. Neurochem. , vol.65 , pp. 2612-2620
    • Mena, M.A.1    Casarejos, M.J.2    Bonin, A.3    Ramos, J.A.4    Garcia Yebenes, J.5
  • 32
    • 77950505891 scopus 로고    scopus 로고
    • Autophagy
    • N. Mizushima Autophagy FEBS Lett. 584 7 2010 1279
    • (2010) FEBS Lett. , vol.584 , Issue.7 , pp. 1279
    • Mizushima, N.1
  • 33
    • 33747886310 scopus 로고    scopus 로고
    • Cell Signaling and Function Organized by PB1 Domain Interactions
    • DOI 10.1016/j.molcel.2006.08.002, PII S1097276506005375
    • J. Moscat, M.T. Diaz-Meco, A. Albert, and S. Campuzano Cell signaling and function organized by PB1 domain interactions Mol. Cell. 23 2006 631 640 (Pubitemid 44292560)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 34
    • 79952103900 scopus 로고    scopus 로고
    • S-Nitrosylation of critical protein thiols mediates protein misfolding and mitochondrial dysfunction in neurodegenerative diseases
    • T. Nakamura, and S.A. Lipton S-Nitrosylation of critical protein thiols mediates protein misfolding and mitochondrial dysfunction in neurodegenerative diseases Antioxid. Redox Signal. 2010 3570 Doi 10. 1089/ars. 2010.
    • (2010) Antioxid. Redox Signal. , pp. 3570
    • Nakamura, T.1    Lipton, S.A.2
  • 35
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • T. Pan, S. Kondo, W. Zhu, W. Xie, J. Jankovic, and W. Le Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement Neurobiol. Dis. 32 2008 16 25
    • (2008) Neurobiol. Dis. , vol.32 , pp. 16-25
    • Pan, T.1    Kondo, S.2    Zhu, W.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 36
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant α-Synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • DOI 10.1016/S0896-6273(02)01125-X
    • L. Petrucelli, C. O'Farrell, P.J. Lockhart, M. Baptista, K. Kehoe, L. Vink, P. Choi, B. Wolozin, M. Farrer, J. Hardy, and M.R. Cookson Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons Neuron 36 2002 1007 1019 (Pubitemid 36044504)
    • (2002) Neuron , vol.36 , Issue.6 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6    Choi, P.7    Wolozin, B.8    Farrer, M.9    Hardy, J.10    Cookson, M.R.11
  • 37
    • 0034905714 scopus 로고    scopus 로고
    • L-DOPA and glia-conditioned medium have additive effects on tyrosine hydroxylase expression in human catecholamine-rich neuroblastoma NB69 cells
    • DOI 10.1046/j.1471-4159.2001.00440.x
    • E. Rodriguez-Martin, S. Canals, M.J. Casarejos, S. de Bernardo, A. Handler, and M.A. Mena L-DOPA and glia-conditioned medium have additive effects on tyrosine hydroxylase expression in human catecholamine-rich neuroblastoma NB69 cells J. Neurochem. 78 2001 535 545 (Pubitemid 32729981)
    • (2001) Journal of Neurochemistry , vol.78 , Issue.3 , pp. 535-545
    • Rodriguez-Martin, E.1    Canals, S.2    Casarejos, M.J.3    De Bernardo, S.4    Handler, A.5    Mena, M.A.6
  • 39
    • 34250171697 scopus 로고    scopus 로고
    • Autophagy Induction Rescues Toxicity Mediated by Proteasome Inhibition
    • DOI 10.1016/j.neuron.2007.06.005, PII S089662730700414X
    • D.C. Rubinsztein Autophagy induction rescues toxicity mediated by proteasome inhibition Neuron 54 2007 854 856 (Pubitemid 46907509)
    • (2007) Neuron , vol.54 , Issue.6 , pp. 854-856
    • Rubinsztein, D.C.1
  • 41
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein
    • DOI 10.1074/jbc.M609532200
    • S. Sarkar, J.E. Davies, Z. Huang, A. Tunnacliffe, and D.C. Rubinsztein Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein J. Biol. Chem. 282 2007 5641 5652 (Pubitemid 47093730)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 42
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • M.A. Singer, and S. Lindquist Multiple effects of trehalose on protein folding in vitro and in vivo Mol. Cell. 1 1998 639 648 (Pubitemid 128379242)
    • (1998) Molecular Cell , vol.1 , Issue.5 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 44
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • DOI 10.1038/nm985
    • M. Tanaka, Y. Machida, S. Niu, T. Ikeda, N.R. Jana, H. Doi, M. Kurosawa, M. Nekooki, and N. Nukina Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease Nat. Med. 10 2004 148 154 (Pubitemid 38524884)
    • (2004) Nature Medicine , vol.10 , Issue.2 , pp. 148-154
    • Tanaka, M.1    Machida, Y.2    Niu, S.3    Ikeda, T.4    Jana, N.R.5    Doi, H.6    Kurosawa, M.7    Nekooki, M.8    Nukina, N.9
  • 45
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • F. Tietze Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues Anal. Biochem. 27 1969 502 522
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 46
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • W.J. Welch, and C.R. Brown Influence of molecular and chemical chaperones on protein folding Cell Stress Chaperones. 1 1996 109 115 (Pubitemid 126670772)
    • (1996) Cell Stress and Chaperones , vol.1 , Issue.2 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 47
    • 0034964582 scopus 로고    scopus 로고
    • Human platelets loaded with trehalose survive freeze-drying
    • DOI 10.1006/cryo.2001.2306
    • W.F. Wolkers, N.J. Walker, F. Tablin, and J.H. Crowe Human platelets loaded with trehalose survive freeze-drying Cryobiology 42 2001 79 87 (Pubitemid 32614079)
    • (2001) Cryobiology , vol.42 , Issue.2 , pp. 79-87
    • Wolkers, W.F.1    Walker, N.J.2    Tablin, F.3    Crowe, J.H.4
  • 49
    • 33746805387 scopus 로고    scopus 로고
    • Signaling, polyubiquitination trafficking, and inclusions: Sequestosome 1/p62s role in neurodegenerative disease
    • M.W. Wooten, X. Hu, J.R. Babu, M.L. Seibenhener, T. Geetha, M.G. Paine, and M.C. Wooten Signaling, polyubiquitination trafficking, and inclusions: sequestosome 1/p62s role in neurodegenerative disease J. Biomed. Biotechnol. 2006 2006 62079
    • (2006) J. Biomed. Biotechnol. , vol.2006 , pp. 62079
    • Wooten, M.W.1    Hu, X.2    Babu, J.R.3    Seibenhener, M.L.4    Geetha, T.5    Paine, M.G.6    Wooten, M.C.7
  • 50
    • 33947517977 scopus 로고    scopus 로고
    • Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: Relevance to Parkinson disease
    • DOI 10.1074/jbc.M603712200
    • N. Yamamoto, H. Sawada, Y. Izumi, T. Kume, H. Katsuki, S. Shimohama, and A. Akaike Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: relevance to Parkinson disease J. Biol. Chem. 282 2007 4364 4372 (Pubitemid 47101000)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4364-4372
    • Yamamoto, N.1    Sawada, H.2    Izumi, Y.3    Kume, T.4    Katsuki, H.5    Shimohama, S.6    Akaike, A.7
  • 51
    • 69349090907 scopus 로고    scopus 로고
    • The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases
    • Z. Yue, L. Friedman, M. Komatsu, and K. Tanaka The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases Biochim. Biophys. Acta 1793 2009 1496 1507
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1496-1507
    • Yue, Z.1    Friedman, L.2    Komatsu, M.3    Tanaka, K.4
  • 52
    • 30044449754 scopus 로고    scopus 로고
    • DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T α-synuclein toxicity
    • DOI 10.1074/jbc.M507124200
    • W. Zhou, and C.R. Freed DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T alpha-synuclein toxicity J. Biol. Chem. 280 2005 43150 43158 (Pubitemid 43049281)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.52 , pp. 43150-43158
    • Zhou, W.1    Freed, C.R.2


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