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Volumn 51, Issue 3, 2011, Pages 594-608

Acute exposure to prion infection induces transient oxidative stress progressing to be cumulatively deleterious with chronic propagation in vitro

Author keywords

Caspase; Free radicals; Lipid peroxidation; Lysosome; Prion; ROS

Indexed keywords

CASPASE; PHOSPHATIDYLSERINE; PRION PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 79959935920     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.03.035     Document Type: Article
Times cited : (31)

References (52)
  • 2
    • 0242363656 scopus 로고    scopus 로고
    • Depleting Neuronal PrP in Prion Infection Prevents Disease and Reverses Spongiosis
    • DOI 10.1126/science.1090187
    • G. Mallucci, A. Dickinson, J. Linehan, P.C. Klöhn, S. Brandner, and J. Collinge Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis Science 302 2003 871 874 (Pubitemid 37339628)
    • (2003) Science , vol.302 , Issue.5646 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3    Klohn, P.-C.4    Brandner, S.5    Collinge, J.6
  • 4
    • 66049152925 scopus 로고    scopus 로고
    • Design of anti- and pro-aggregation variants to assess the effects of methioine oxidation in human prion protein
    • C. Wolschner, A. Giese, H.A. Kretzschmar, R. Huber, L. Moroder, and N. Budisa Design of anti- and pro-aggregation variants to assess the effects of methioine oxidation in human prion protein Proc. Natl. Acad Sci. U.S.A. 106 19 2009 7756 7761
    • (2009) Proc. Natl. Acad Sci. U.S.A. , vol.106 , Issue.19 , pp. 7756-7761
    • Wolschner, C.1    Giese, A.2    Kretzschmar, H.A.3    Huber, R.4    Moroder, L.5    Budisa, N.6
  • 5
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • D.R. Brown, and A. Besinger Prion protein expression and superoxide dismutase activity Biochem. J. 334 1998 423 429 (Pubitemid 28448586)
    • (1998) Biochemical Journal , vol.334 , Issue.2 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 10
    • 0037080043 scopus 로고    scopus 로고
    • Lack of prion protein expression results in a neuronal phenotype sensitive to stress
    • DOI 10.1002/jnr.10118
    • D.R. Brown, R.S.J. Nicholas, and L. Canevari Lack of Prion Protein Expression Results in a Neuronal Phenotype Sensitive to Stress J. Neurosci. Res. 67 2002 211 224 (Pubitemid 34052040)
    • (2002) Journal of Neuroscience Research , vol.67 , Issue.2 , pp. 211-224
    • Brown, D.R.1    Nicholas, R.S.J.2    Canevari, L.3
  • 13
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • DOI 10.1042/0264-6021:3620253
    • A.M. Thackray, R. Knight, S.J. Haswell, R. Bujdoso, and D.R. Brown Metal imbalance and compromised anti-oxidant function are early changes in prion disease Biochem. J. 362 2002 253 258 (Pubitemid 34174483)
    • (2002) Biochemical Journal , vol.362 , Issue.1 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 16
    • 0025237864 scopus 로고
    • Establishment and characterization of multipotent neural cell lines using retrovirus vector-mediated oncogene transfer
    • E.F. Ryder, E.Y. Snyder, and C.L. Cepko Establishment and characterization of multipotent neural cell lines using retrovirus vector-mediated oncogene transfer J. Neurobiol. 21 2 1990 356 375 (Pubitemid 20108088)
    • (1990) Journal of Neurobiology , vol.21 , Issue.2 , pp. 356-375
    • Ryder, E.F.1    Snyder, E.Y.2    Cepko, C.L.3
  • 18
    • 67649963292 scopus 로고    scopus 로고
    • Dominant roles of the polybasic proline motif and copper in PrP23-89 mediated stress protection response
    • C.L. Haigh, S.C. Drew, M.P. Boland, C.L. Masters, K.J. Barnham, V.A. Lawson, and S.J. Collins Dominant roles of the polybasic proline motif and copper in PrP23-89 mediated stress protection response J. Cell Sci. 122 10 2009 1518 1528
    • (2009) J. Cell Sci. , vol.122 , Issue.10 , pp. 1518-1528
    • Haigh, C.L.1    Drew, S.C.2    Boland, M.P.3    Masters, C.L.4    Barnham, K.J.5    Lawson, V.A.6    Collins, S.J.7
  • 19
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • DOI 10.1128/JVI.74.9.4377-4386.2000
    • P.J. Bosque, and S.B. Prusiner Cultured cell sublines highly susceptible to prion infection J. Virol. 74 2000 4377 4386 (Pubitemid 30214445)
    • (2000) Journal of Virology , vol.74 , Issue.9 , pp. 4377-4386
    • Bosque, P.J.1    Prusiner, S.B.2
  • 20
    • 69949131244 scopus 로고    scopus 로고
    • PrPC related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site
    • C.L. Haigh, V. Lewis, L.J. Vella, C.L. Masters, A.F. Hill, V.A. Lawson, and S.J. Collins PrPC related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site Cell Res. 19 2009 1062 1078
    • (2009) Cell Res. , vol.19 , pp. 1062-1078
    • Haigh, C.L.1    Lewis, V.2    Vella, L.J.3    Masters, C.L.4    Hill, A.F.5    Lawson, V.A.6    Collins, S.J.7
  • 21
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • DOI 10.1002/path.2145
    • L.J. Vella, R.A. Sharples, V.A. Lawson, C.L. Masters, R. Cappai, and A.F. Hill Packaging of prions into exosomes is associated with a novel pathway of PrP processing J. Pathol. 211 2007 582 590 (Pubitemid 46502435)
    • (2007) Journal of Pathology , vol.211 , Issue.5 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 25
    • 0037101881 scopus 로고    scopus 로고
    • 581/591, an oxidation-sensitive fluorescent lipid peroxidation probe: (Micro)spectroscopic characterization and validation of methodology
    • DOI 10.1016/S0891-5849(02)00848-1, PII S0891584902008481
    • 581/591, an oxidation-sensitive fluorescent lipid peroxidation probe: (micro)spectroscopic characterisation and validation of methodology Free Radic. Biol. Med. 33 4 2002 473 490 (Pubitemid 34874969)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.4 , pp. 473-490
    • Drummen, G.P.C.1    Van Liebergen, L.C.M.2    Op Den Kamp, J.A.F.3    Post, J.A.4
  • 26
    • 0034656410 scopus 로고    scopus 로고
    • Redox-dependent trafficking of 2,3,4,5,6- pentafluorodihydrotetramethylrosamine, a novel fluorogenic indicator of cellular oxidative activity
    • DOI 10.1016/S0891-5849(00)00265-3, PII S0891584900002653
    • C.S. Chen, and K.R. Gee Redox-dependent trafficking of 2,3,4,5, 6-pentafluorodihydrotetramethylrosamine, a novel fluorogenic indicator of cellular oxidative activity Free Radic. Biol. Med. 28 2000 1266 1278 (Pubitemid 30417470)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.8 , pp. 1266-1278
    • Chen, C.-S.1    Gee, K.R.2
  • 27
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie- associated prion protein accumulation
    • DOI 10.1128/JVI.74.10.4894-4897.2000
    • K. Doh-Ura, T. Iwaki, and B. Caughey Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation J. Virol. 74 10 2000 4894 4897 (Pubitemid 30237920)
    • (2000) Journal of Virology , vol.74 , Issue.10 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 28
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • DOI 10.1073/pnas.011578098
    • J. Ma, and S. Lindquist Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation Proc. Natl. Acad Sci. U.S.A. 98 26 2001 14955 14960 (Pubitemid 34013951)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 31
    • 41149107987 scopus 로고    scopus 로고
    • Complex I specific increase in superoxide formation and respiration rate by PrP-null mouse brain mitochondria
    • DOI 10.1111/j.1471-4159.2007.05123.x
    • A.W. Paterson, J.C. Curtis, and N.K. Macleod Complex I specific increase in superoxide formation and respiration rate by PrP-null mouse brain mitochondria J. Neurochem. 105 1 2008 177 191 (Pubitemid 351441635)
    • (2008) Journal of Neurochemistry , vol.105 , Issue.1 , pp. 177-191
    • Paterson, A.W.J.1    Curtis, J.C.2    MacLeod, N.K.3
  • 32
    • 77957156220 scopus 로고    scopus 로고
    • A radiation induced adaptive response prolongs the survival of prion infected mice
    • 10.1016/j.freeradbiomed.2010.07.025
    • M. Plews, S.L. Simon, and D.R. Boreham A radiation induced adaptive response prolongs the survival of prion infected mice Free Radic. Biol. Med. 2010 10.1016/j.freeradbiomed.2010.07.025
    • (2010) Free Radic. Biol. Med.
    • Plews, M.1    Simon, S.L.2    Boreham, D.R.3
  • 35
    • 34548512806 scopus 로고    scopus 로고
    • Modulation of proteinase K-resistant prion protein in cells and infectious brain homogenate by redox iron: Implications for prion replication and disease pathogenesis
    • DOI 10.1091/mbc.E07-04-0317
    • S. Basu, M.L. Mohan, X. Luo, B. Kundu, Q. Kong, and N. Singh Modulation of proteinase K-resistant prion protein in cells and infectious brain homogenate by redox iron: implications for prion replication and disease pathogenesis Mol. Biol. Cell 18 9 2007 3302 3312 (Pubitemid 47378672)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.9 , pp. 3302-3312
    • Basu, S.1    Mohan, M.L.2    Luo, X.3    Kundu, B.4    Kong, Q.5    Singh, N.6
  • 36
    • 77955348149 scopus 로고    scopus 로고
    • Paradoxical role of prion protein aggregates in redox-iron induced toxicity
    • D. Das, X. Luo, and A. Singh Paradoxical role of prion protein aggregates in redox-iron induced toxicity PLoS One 5 7 2010 e11420
    • (2010) PLoS One , vol.5 , Issue.7 , pp. 11420
    • Das, D.1    Luo, X.2    Singh, A.3
  • 37
    • 39649097627 scopus 로고    scopus 로고
    • Elevated manganese levels in blood and CNS in human prion disease
    • S. Hesketh, J. Sassoon, R. Knight, and D.R. Brown Elevated manganese levels in blood and CNS in human prion disease Mol. Cell. Neurosci. 37 3 2008 590 598
    • (2008) Mol. Cell. Neurosci. , vol.37 , Issue.3 , pp. 590-598
    • Hesketh, S.1    Sassoon, J.2    Knight, R.3    Brown, D.R.4
  • 39
    • 37849013375 scopus 로고    scopus 로고
    • Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors
    • A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors Br. J. Pharmacol. 153 1 2008 6 20
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.1 , pp. 6-20
    • Negre-Salvayre, A.1    Coatrieux, C.2    Ingueneau, C.3    Salvayre, R.4
  • 41
    • 59349116776 scopus 로고    scopus 로고
    • Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion
    • G. Colombo, M. Meli, G. Morra, R. Gabizon, and M. Gasset Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion PLoS One 4 1 2009 e4296
    • (2009) PLoS One , vol.4 , Issue.1 , pp. 4296
    • Colombo, G.1    Meli, M.2    Morra, G.3    Gabizon, R.4    Gasset, M.5
  • 42
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • F. Wang, X. Wang, C.G. Yuan, and J. Ma Generating a prion with bacterially expressed recombinant prion protein Science 327 5969 2010 1132 1135
    • (2010) Science , vol.327 , Issue.5969 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 44
    • 61349083601 scopus 로고    scopus 로고
    • The propagation of hamster-adapted scrapie PrPSc can be enhanced by reduced pyridine nucleotide in vitro
    • S. Shi, C.F. Dong, C. Tian, R.M. Zhou, K. Xu, B.Y. Zhang, C. Gao, J. Han, and X.P. Dong The propagation of hamster-adapted scrapie PrPSc can be enhanced by reduced pyridine nucleotide in vitro FEBS J. 276 6 2009 1536 1545
    • (2009) FEBS J. , vol.276 , Issue.6 , pp. 1536-1545
    • Shi, S.1    Dong, C.F.2    Tian, C.3    Zhou, R.M.4    Xu, K.5    Zhang, B.Y.6    Gao, C.7    Han, J.8    Dong, X.P.9
  • 47
    • 0036791880 scopus 로고    scopus 로고
    • Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model
    • S.J. Collins, V. Lewis, M. Brazier, A.F. Hill, A. Fletcher, and C.L. Masters Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model Ann. Neurol. 52 4 2002 503 506
    • (2002) Ann. Neurol. , vol.52 , Issue.4 , pp. 503-506
    • Collins, S.J.1    Lewis, V.2    Brazier, M.3    Hill, A.F.4    Fletcher, A.5    Masters, C.L.6
  • 49
    • 67249099366 scopus 로고    scopus 로고
    • Identification of an intracellular site of prion conversion
    • Z. Marijanovic, A. Caputo, V. Campana, and C. Zurzolo Identification of an intracellular site of prion conversion PLoS Pathog. 5 5 2009 e1000426
    • (2009) PLoS Pathog. , vol.5 , Issue.5 , pp. 1000426
    • Marijanovic, Z.1    Caputo, A.2    Campana, V.3    Zurzolo, C.4
  • 50
    • 57249089081 scopus 로고    scopus 로고
    • Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy
    • N.M. Veith, H. Plattner, C.A. Stuermer, W.J. Schulz-Schaeffer, and A. Bürkle Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy Eur. J. Cell Biol. 88 1 2009 45 63
    • (2009) Eur. J. Cell Biol. , vol.88 , Issue.1 , pp. 45-63
    • Veith, N.M.1    Plattner, H.2    Stuermer, C.A.3    Schulz-Schaeffer, W.J.4    Bürkle, A.5
  • 51
    • 73649087254 scopus 로고    scopus 로고
    • Constitutive reactive oxygen species generation from autophagosome/ lysosome in neuronal oxidative toxicity
    • C. Kubota, S. Torii, N. Hou, N. Saito, Y. Yoshimoto, H. Imai, and T. Takeuchi Constitutive reactive oxygen species generation from autophagosome/lysosome in neuronal oxidative toxicity J. Biol. Chem. 285 1 2010 667 674
    • (2010) J. Biol. Chem. , vol.285 , Issue.1 , pp. 667-674
    • Kubota, C.1    Torii, S.2    Hou, N.3    Saito, N.4    Yoshimoto, Y.5    Imai, H.6    Takeuchi, T.7
  • 52
    • 33646558563 scopus 로고    scopus 로고
    • Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and non-neuronal cells
    • DOI 10.1111/j.1471-4159.2006.03837.x
    • C. Grenier, C. Bissonnette, L. Volkov, and X. Roucou Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and non-neuronal cells J. Neurochem. 97 5 2006 1456 1466 (Pubitemid 43725584)
    • (2006) Journal of Neurochemistry , vol.97 , Issue.5 , pp. 1456-1466
    • Grenier, C.1    Bissonnette, C.2    Volkov, L.3    Roucou, X.4


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