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Volumn 62, Issue 5, 2013, Pages 653-663

Gene expression profiling of rotenone-mediated cortical neuronal death: Evidence for inhibition of ubiquitin-proteasome system and autophagy-lysosomal pathway, and dysfunction of mitochondrial and calcium signaling

Author keywords

Mitochondria complex I inhibition; Neurodegeneration; Oxidative stress; Programmed cell death; Protein handling; Rotenone

Indexed keywords

CHAPERONE; PROTEASOME; ROTENONE; UBIQUITIN;

EID: 84875757800     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2012.11.011     Document Type: Article
Times cited : (18)

References (49)
  • 2
    • 29444459269 scopus 로고    scopus 로고
    • Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse
    • K. Aoyama, S.W. Suh, A.M. Hamby, J. Liu, W.Y. Chan, Y. Chen, and R.A. Swanson Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse Nat. Neurosci. 9 2006 119 126
    • (2006) Nat. Neurosci. , vol.9 , pp. 119-126
    • Aoyama, K.1    Suh, S.W.2    Hamby, A.M.3    Liu, J.4    Chan, W.Y.5    Chen, Y.6    Swanson, R.A.7
  • 3
    • 84858013809 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II (CaMKII) inhibition induces neurotoxicity via dysregulation of glutamate/calcium signaling and hyperexcitability
    • N.M. Ashpole, W. Song, T. Brustovetsky, E.A. Engleman, N. Brustovetsky, T.R. Cummins, and A. Hudmon Calcium/calmodulin-dependent protein kinase II (CaMKII) inhibition induces neurotoxicity via dysregulation of glutamate/calcium signaling and hyperexcitability J. Biol. Chem. 287 2012 8495 8506
    • (2012) J. Biol. Chem. , vol.287 , pp. 8495-8506
    • Ashpole, N.M.1    Song, W.2    Brustovetsky, T.3    Engleman, E.A.4    Brustovetsky, N.5    Cummins, T.R.6    Hudmon, A.7
  • 4
    • 34548514227 scopus 로고    scopus 로고
    • CaMKII and CaMKIV mediate distinct prosurvival signaling pathways in response to depolarization in neurons
    • J. Bok, Q. Wang, J. Huang, and S.H. Green CaMKII and CaMKIV mediate distinct prosurvival signaling pathways in response to depolarization in neurons Mol. Cell. Neurosci. 36 2007 13 26
    • (2007) Mol. Cell. Neurosci. , vol.36 , pp. 13-26
    • Bok, J.1    Wang, Q.2    Huang, J.3    Green, S.H.4
  • 5
    • 79960635284 scopus 로고    scopus 로고
    • Fighting neurodegeneration with rapamycin: Mechanistic insights
    • J. Bove, M. Martinez-Vicente, and M. Vila Fighting neurodegeneration with rapamycin: mechanistic insights Nat. Rev. Neurosci. 12 2011 437 452
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 437-452
    • Bove, J.1    Martinez-Vicente, M.2    Vila, M.3
  • 6
    • 0037343974 scopus 로고    scopus 로고
    • The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures
    • Y. Chen, and R.A. Swanson The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures J. Neurochem. 84 2003 1332 1339
    • (2003) J. Neurochem. , vol.84 , pp. 1332-1339
    • Chen, Y.1    Swanson, R.A.2
  • 8
    • 0032191207 scopus 로고    scopus 로고
    • Micromolar l-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurons
    • N.S. Cheung, C.J. Pascoe, S.F. Giardina, C.A. John, and P.M. Beart Micromolar l-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurons Neuropharmacology 37 1998 1419 1429
    • (1998) Neuropharmacology , vol.37 , pp. 1419-1429
    • Cheung, N.S.1    Pascoe, C.J.2    Giardina, S.F.3    John, C.A.4    Beart, P.M.5
  • 9
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • J.E. Chipuk, and D.R. Green How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol. 18 2008 157 164
    • (2008) Trends Cell Biol. , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 13
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • W.X. Ding, H.M. Ni, W. Gao, T. Yoshimori, D.B. Stolz, D. Ron, and X.M. Yin Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability Am. J. Pathol. 171 2007 513 524
    • (2007) Am. J. Pathol. , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 14
    • 75949120541 scopus 로고    scopus 로고
    • Dysfunctional mitochondria uphold calpain activation: Contribution to Parkinson's disease pathology
    • A.R. Esteves, D.M. Arduíno, R.H. Swerdlow, C.R. Oliveira, and S.M. Cardoso Dysfunctional mitochondria uphold calpain activation: contribution to Parkinson's disease pathology Neurobiol. Dis. 37 2010 723 730
    • (2010) Neurobiol. Dis. , vol.37 , pp. 723-730
    • Esteves, A.R.1    Arduíno, D.M.2    Swerdlow, R.H.3    Oliveira, C.R.4    Cardoso, S.M.5
  • 16
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • A. Ghosh, and M.E. Greenberg Calcium signaling in neurons: molecular mechanisms and cellular consequences Science 268 1995 239 247
    • (1995) Science , vol.268 , pp. 239-247
    • Ghosh, A.1    Greenberg, M.E.2
  • 17
    • 77952541169 scopus 로고    scopus 로고
    • Neuron-selective changes in RNA transcripts related to energy metabolism in toxic models of parkinsonism in rodents
    • J.G. Greene, R. Dingledine, and J.T. Greenamyre Neuron-selective changes in RNA transcripts related to energy metabolism in toxic models of parkinsonism in rodents Neurobiol. Dis. 38 2010 476 481
    • (2010) Neurobiol. Dis. , vol.38 , pp. 476-481
    • Greene, J.G.1    Dingledine, R.2    Greenamyre, J.T.3
  • 20
    • 77956207696 scopus 로고    scopus 로고
    • Oxidative stress: Emerging mitochondrial and cellular themes and variations in neuronal injury
    • G.C. Higgins, P.M. Beart, Y.S. Shin, M.J. Chen, N.S. Cheung, and P. Nagley Oxidative stress: emerging mitochondrial and cellular themes and variations in neuronal injury J. Alzheimers Dis. 20 Suppl. 2 2010 S453 s473
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.SUPPL. 2
    • Higgins, G.C.1    Beart, P.M.2    Shin, Y.S.3    Chen, M.J.4    Cheung, N.S.5    Nagley, P.6
  • 21
    • 33748707584 scopus 로고    scopus 로고
    • Oxidative stress-triggered unfolded protein response is upstream of intrinsic cell death evoked by parkinsonian mimetics
    • W.A. Holtz, J.M. Turetzky, Y.J. Jong, and K.L. O'Malley Oxidative stress-triggered unfolded protein response is upstream of intrinsic cell death evoked by parkinsonian mimetics J. Neurochem. 99 2006 54 69
    • (2006) J. Neurochem. , vol.99 , pp. 54-69
    • Holtz, W.A.1    Turetzky, J.M.2    Jong, Y.J.3    O'Malley, K.L.4
  • 25
    • 84861378458 scopus 로고    scopus 로고
    • Interaction between pathogenic proteins in neurodegenerative disorders
    • K.A. Jellinger Interaction between pathogenic proteins in neurodegenerative disorders J. Cell Mol. Med. 16 2012 1166 1183
    • (2012) J. Cell Mol. Med. , vol.16 , pp. 1166-1183
    • Jellinger, K.A.1
  • 26
    • 79959241490 scopus 로고    scopus 로고
    • Targeting glycogen synthase kinase-3β for therapeutic benefit against oxidative stress in Alzheimer's disease: Involvement of the Nrf2-ARE pathway
    • K. Kanninen, A.R. White, J. Koistinaho, and T. Malm Targeting glycogen synthase kinase-3β for therapeutic benefit against oxidative stress in Alzheimer's disease: involvement of the Nrf2-ARE pathway Int. J. Alzheimers Dis. 2011 2011 985085
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 985085
    • Kanninen, K.1    White, A.R.2    Koistinaho, J.3    Malm, T.4
  • 28
    • 0032493935 scopus 로고    scopus 로고
    • 2+ homeostasis in the agonist-sensitive internal store: Functional interactions between mitochondria and the ER measured in situ in intact cells
    • 2+ homeostasis in the agonist-sensitive internal store: functional interactions between mitochondria and the ER measured in situ in intact cells J. Cell Biol. 142 1998 1235 1243
    • (1998) J. Cell Biol. , vol.142 , pp. 1235-1243
    • Landolfi, B.1    Curci, S.2    Debellis, L.3    Pozzan, T.4    Hofer, A.M.5
  • 29
    • 35748967902 scopus 로고    scopus 로고
    • S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains
    • E. Leclerc, G. Fritz, M. Weibel, C.W. Heizmann, and A. Galichet S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains J. Biol. Chem. 282 2007 31317 31331
    • (2007) J. Biol. Chem. , vol.282 , pp. 31317-31331
    • Leclerc, E.1    Fritz, G.2    Weibel, M.3    Heizmann, C.W.4    Galichet, A.5
  • 30
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: Cross-talk and redox signalling
    • J. Lee, S. Giordano, and J. Zhang Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling Biochem. J. 441 2012 523 540
    • (2012) Biochem. J. , vol.441 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 32
    • 34247645457 scopus 로고    scopus 로고
    • + preferentially redistribute apoptosis-inducing factor in apoptotic dopamine neurons
    • + preferentially redistribute apoptosis-inducing factor in apoptotic dopamine neurons Neuroreport 18 2007 307 312
    • (2007) Neuroreport , vol.18 , pp. 307-312
    • Lim, M.L.R.1    Mercer, L.D.2    Nagley, P.3    Beart, P.M.4
  • 33
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 34
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • V.M. Mann, J.M. Cooper, D. Krige, S.E. Daniel, A.H. Schapira, and C.D. Marsden Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease Brain 115 1992 333 342
    • (1992) Brain , vol.115 , pp. 333-342
    • Mann, V.M.1    Cooper, J.M.2    Krige, D.3    Daniel, S.E.4    Schapira, A.H.5    Marsden, C.D.6
  • 35
    • 84857981316 scopus 로고    scopus 로고
    • Toxin models of mitochondrial dysfunction in Parkinson's disease
    • T.N. Martinez, and J.T. Greenamyre Toxin models of mitochondrial dysfunction in Parkinson's disease Antioxid. Redox Signal. 16 2012 920 934
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 920-934
    • Martinez, T.N.1    Greenamyre, J.T.2
  • 36
    • 78649960531 scopus 로고    scopus 로고
    • Calpain and caspase processing of caspase-12 contribute to the ER stress-induced cell death pathway in differentiated PC12 cells
    • J.A. Martinez, Z. Zhang, S.I. Svetlov, R.L. Hayes, K.K. Wang, and S.F. Larner Calpain and caspase processing of caspase-12 contribute to the ER stress-induced cell death pathway in differentiated PC12 cells Apoptosis 15 2010 1480 1493
    • (2010) Apoptosis , vol.15 , pp. 1480-1493
    • Martinez, J.A.1    Zhang, Z.2    Svetlov, S.I.3    Hayes, R.L.4    Wang, K.K.5    Larner, S.F.6
  • 39
    • 84867397192 scopus 로고    scopus 로고
    • Revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease-resemblance to the effect of amphetamine drugs of abuse
    • (Epub ahead of print)
    • R. Perfeito, T. Cunha-Oliveira, and A. Cristina Rego Revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease-resemblance to the effect of amphetamine drugs of abuse Free Radic. Biol. Med. 2012 (Epub ahead of print)
    • (2012) Free Radic. Biol. Med.
    • Perfeito, R.1    Cunha-Oliveira, T.2    Cristina Rego, A.3
  • 40
    • 84886725073 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • E.J. Ryu, H.P. Harding, J.M. Angelastro, O.V. Vitolo, D. Ron, and L.A. Greene Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease J. Neurosci. 15 2002 22 24
    • (2002) J. Neurosci. , vol.15 , pp. 22-24
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 41
    • 80052273858 scopus 로고    scopus 로고
    • Calpain inhibition protected spinal cord motoneurons against 1-methyl-4-phenylpyridinium ion and rotenone
    • S. Samantaray, V.H. Knaryan, C. Le Gal, S.K. Ray, and N.L. Banik Calpain inhibition protected spinal cord motoneurons against 1-methyl-4-phenylpyridinium ion and rotenone Neuroscience 192 2011 263 274
    • (2011) Neuroscience , vol.192 , pp. 263-274
    • Samantaray, S.1    Knaryan, V.H.2    Le Gal, C.3    Ray, S.K.4    Banik, N.L.5
  • 43
    • 0141996495 scopus 로고    scopus 로고
    • Mechanism for generation of hydrogen peroxide and change of mitochondrial membrane potential during rotenone-induced apoptosis
    • S. Tada-Oikawa, Y. Hiraku, M. Kawanishi, and S. Kawanishi Mechanism for generation of hydrogen peroxide and change of mitochondrial membrane potential during rotenone-induced apoptosis Life Sci. 73 2003 3277 3288
    • (2003) Life Sci. , vol.73 , pp. 3277-3288
    • Tada-Oikawa, S.1    Hiraku, Y.2    Kawanishi, M.3    Kawanishi, S.4
  • 44
    • 84857977037 scopus 로고    scopus 로고
    • Alzheimer's disease: Redox dysregulation as a common denominator for diverse pathogenic mechanisms
    • R. Von Bernhardi, and J. Eugenin Alzheimer's disease: redox dysregulation as a common denominator for diverse pathogenic mechanisms Antioxid. Redox Signal. 16 2012 974 1031
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 974-1031
    • Von Bernhardi, R.1    Eugenin, J.2
  • 45
    • 35548946779 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis via interaction between glutamate transport-associated protein 3-18 (GTRAP3-18) and excitatory amino acid carrier-1 (EAAC1) at plasma membrane
    • M. Watabe, K. Aoyama, and T. Nakaki Regulation of glutathione synthesis via interaction between glutamate transport-associated protein 3-18 (GTRAP3-18) and excitatory amino acid carrier-1 (EAAC1) at plasma membrane Mol. Pharmacol. 72 2007 1103 1110
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1103-1110
    • Watabe, M.1    Aoyama, K.2    Nakaki, T.3
  • 46
    • 34250188065 scopus 로고    scopus 로고
    • Rotenone potentiates NMDA currents in substantia nigra dopamine neurons
    • Y.-N. Wu, and S.W. Johnson Rotenone potentiates NMDA currents in substantia nigra dopamine neurons Neurosci. Lett. 421 2007 96 100
    • (2007) Neurosci. Lett. , vol.421 , pp. 96-100
    • Wu, Y.-N.1    Johnson, S.W.2
  • 47
    • 61849083067 scopus 로고    scopus 로고
    • 2+-dependent block of NMDA currents in substantia nigra dopamine neurons
    • 2+-dependent block of NMDA currents in substantia nigra dopamine neurons Neurotoxicology 30 2009 320 325
    • (2009) Neurotoxicology , vol.30 , pp. 320-325
    • Wu, Y.-N.1    Johnson, S.W.2
  • 48
    • 70450222302 scopus 로고    scopus 로고
    • The role of lysosomal rupture in neuronal death
    • T. Yamashima, and S. Oikawa The role of lysosomal rupture in neuronal death Prog. Neurobiol. 89 2009 343 358
    • (2009) Prog. Neurobiol. , vol.89 , pp. 343-358
    • Yamashima, T.1    Oikawa, S.2


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