메뉴 건너뛰기




Volumn 74, Issue , 2014, Pages 129-144

Insulin and IGF-1 improve mitochondrial function in a PI-3K/Akt-dependent manner and reduce mitochondrial generation of reactive oxygen species in Huntington's disease knock-in striatal cells

Author keywords

Akt; Huntington disease; Insulin IGF 1 signaling; Mitochondria; Nrf2; Oxidative stress; Reactive oxygen species; Striatal cells

Indexed keywords

CYTOCHROME C OXIDASE; DYNAMIN I; GLUTATHIONE; HUNTINGTIN; INSULIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; SOMATOMEDIN C; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR NRF2; DNA BINDING PROTEIN; DNM1L PROTEIN, MOUSE; DYNAMIN; HDH PROTEIN, MOUSE; HIGH MOBILITY GROUP PROTEIN; HTT PROTEIN, HUMAN; NERVE PROTEIN; NUCLEAR PROTEIN; ONCOPROTEIN; TFAM PROTEIN, MOUSE;

EID: 84904892173     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.06.023     Document Type: Article
Times cited : (112)

References (98)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes Cell 72 1993 971 983
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • DOI 10.1111/j.1460-9568.2008.06310.x
    • J.M. Gil, and A.C. Rego Mechanisms of neurodegeneration in Huntington's disease Eur. J. Neurosci. 27 2008 2803 2820 (Pubitemid 351832229)
    • (2008) European Journal of Neuroscience , vol.27 , Issue.11 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 3
    • 77957993152 scopus 로고    scopus 로고
    • Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease - From clinical features to the bench
    • T.R. Rosenstock, A.I. Duarte, and A.C. Rego Mitochondrial-associated metabolic changes and neurodegeneration in Huntington's disease - from clinical features to the bench Curr. Drug Targets 11 2010 1218 1236
    • (2010) Curr. Drug Targets , vol.11 , pp. 1218-1236
    • Rosenstock, T.R.1    Duarte, A.I.2    Rego, A.C.3
  • 7
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in huntington's disease: Selective vulnerability of the basal ganglia
    • DOI 10.1002/ana.410410514
    • S.E. Browne, A.C. Bowling, U. MacGarvey, M.J. Baik, S.C. Berger, M.M. Muqit, E.D. Bird, and M.F. Beal Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia Ann. Neurol. 41 1997 646 653 (Pubitemid 27212659)
    • (1997) Annals of Neurology , vol.41 , Issue.5 , pp. 646-653
    • Browne, S.E.1    Bowling, A.C.2    MacGarvey, U.3    Baik, M.J.4    Berger, S.C.5    Muqit, M.M.K.6    Bird, E.D.7    Beal, M.F.8
  • 8
    • 0033520166 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex
    • M.C. Polidori, P. Mecocci, S.E. Browne, U. Senin, and M.F. Beal Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex Neurosci. Lett. 272 1999 53 56
    • (1999) Neurosci. Lett. , vol.272 , pp. 53-56
    • Polidori, M.C.1    Mecocci, P.2    Browne, S.E.3    Senin, U.4    Beal, M.F.5
  • 9
    • 79952585486 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: Implications for selective neuronal damage
    • U. Shirendeb, A.P. Reddy, M. Manczak, M.J. Calkins, P. Mao, D.A. Tagle, and P.H. Reddy Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage Hum. Mol. Genet 20 2011 1438 1455
    • (2011) Hum. Mol. Genet , vol.20 , pp. 1438-1455
    • Shirendeb, U.1    Reddy, A.P.2    Manczak, M.3    Calkins, M.J.4    Mao, P.5    Tagle, D.A.6    Reddy, P.H.7
  • 10
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • DOI 10.1046/j.1471-4159.2001.00689.x
    • M.B. Bogdanov, O.A. Andreassen, A. Dedeoglu, R.J. Ferrante, and M.F. Beal Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease J. Neurochem. 79 2001 1246 1249 (Pubitemid 34019802)
    • (2001) Journal of Neurochemistry , vol.79 , Issue.6 , pp. 1246-1249
    • Bogdanov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 12
    • 0032903802 scopus 로고    scopus 로고
    • Oxidative stress in Huntington's disease
    • S.E. Browne, R.J. Ferrante, and M.F. Beal Oxidative stress in Huntington's disease Brain Pathol. 9 1999 147 163 (Pubitemid 29056525)
    • (1999) Brain Pathology , vol.9 , Issue.1 , pp. 147-163
    • Browne, S.E.1    Ferrante, R.J.2    Beal, M.F.3
  • 13
    • 79954575043 scopus 로고    scopus 로고
    • Modulation of lipid peroxidation and mitochondrial function improves neuropathology in Huntington's disease mice
    • J. Lee, B. Kosaras, S.J. Del Signore, K. Cormier, A. McKee, R.R. Ratan, N.W. Kowall, and H. Ryu Modulation of lipid peroxidation and mitochondrial function improves neuropathology in Huntington's disease mice Acta Neuropathol. 121 2011 487 498
    • (2011) Acta Neuropathol. , vol.121 , pp. 487-498
    • Lee, J.1    Kosaras, B.2    Del Signore, S.J.3    Cormier, K.4    McKee, A.5    Ratan, R.R.6    Kowall, N.W.7    Ryu, H.8
  • 15
    • 84455173005 scopus 로고    scopus 로고
    • In vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production
    • S. Hands, M.U. Sajjad, M.J. Newton, and A. Wyttenbach in vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production J. Biol. Chem. 286 2011 44512 44520
    • (2011) J. Biol. Chem. , vol.286 , pp. 44512-44520
    • Hands, S.1    Sajjad, M.U.2    Newton, M.J.3    Wyttenbach, A.4
  • 18
    • 84859724251 scopus 로고    scopus 로고
    • Huntingtons disease and the striatal medium spiny neuron: Cell-autonomous and non-cell-autonomous mechanisms of disease
    • M.E. Ehrlich Huntingtons disease and the striatal medium spiny neuron: cell-autonomous and non-cell-autonomous mechanisms of disease Neurotherapeutics 9 2012 270 284
    • (2012) Neurotherapeutics , vol.9 , pp. 270-284
    • Ehrlich, M.E.1
  • 19
    • 84887018742 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain complex activity and bioenergetic alterations in human platelets derived from pre-symptomatic and symptomatic Huntingtons disease carriers
    • A.C. Silva, S. Almeida, M. Laco, A.I. Duarte, J. Domingues, C.R. Oliveira, C. Januario, and A.C. Rego Mitochondrial respiratory chain complex activity and bioenergetic alterations in human platelets derived from pre-symptomatic and symptomatic Huntingtons disease carriers Mitochondrion 13 2013 801 809
    • (2013) Mitochondrion , vol.13 , pp. 801-809
    • Silva, A.C.1    Almeida, S.2    Laco, M.3    Duarte, A.I.4    Domingues, J.5    Oliveira, C.R.6    Januario, C.7    Rego, A.C.8
  • 20
    • 84873446708 scopus 로고    scopus 로고
    • Defective mitochondrial disulfide relay system, altered mitochondrial morphology and function in Huntingtons disease
    • E. Napoli, S. Wong, C. Hung, C. Ross-Inta, P. Bomdica, and C. Giulivi Defective mitochondrial disulfide relay system, altered mitochondrial morphology and function in Huntingtons disease Hum. Mol. Genet 22 2013 989 1004
    • (2013) Hum. Mol. Genet , vol.22 , pp. 989-1004
    • Napoli, E.1    Wong, S.2    Hung, C.3    Ross-Inta, C.4    Bomdica, P.5    Giulivi, C.6
  • 25
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • DOI 10.1093/hmg/ddh162
    • Y.S. Choo, G.V. Johnson, M. MacDonald, P.J. Detloff, and M. Lesort Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release Hum. Mol. Genet 13 2004 1407 1420 (Pubitemid 39023049)
    • (2004) Human Molecular Genetics , vol.13 , Issue.14 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.W.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 28
    • 0346749473 scopus 로고    scopus 로고
    • Enhanced Akt Signaling Is an Early Pro-survival Response That Reflects N-Methyl-D-aspartate Receptor Activation in Huntington's Disease Knock-in Striatal Cells
    • DOI 10.1074/jbc.M309348200
    • S. Gines, E. Ivanova, I.S. Seong, C.A. Saura, and M.E. MacDonald Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-D-aspartate receptor activation in Huntingtons disease knock-in striatal cells J. Biol. Chem. 278 2003 50514 50522 (Pubitemid 37548897)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50514-50522
    • Gines, S.1    Ivanova, E.2    Seong, I.-S.3    Saura, C.A.4    MacDonald, M.E.5
  • 31
    • 43549087343 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression
    • A.I. Duarte, P. Santos, C.R. Oliveira, M.S. Santos, and A.C. Rego Insulin neuroprotection against oxidative stress is mediated by Akt and GSK-3beta signaling pathways and changes in protein expression Biochim. Biophys. Acta 1783 2008 994 1002
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 994-1002
    • Duarte, A.I.1    Santos, P.2    Oliveira, C.R.3    Santos, M.S.4    Rego, A.C.5
  • 32
    • 56049102574 scopus 로고    scopus 로고
    • Insulin stimulation of gamma-glutamylcysteine ligase catalytic subunit expression increases endothelial GSH during oxidative stress: Influence of low glucose
    • W. Langston, M.L. Circu, and T.Y. Aw Insulin stimulation of gamma-glutamylcysteine ligase catalytic subunit expression increases endothelial GSH during oxidative stress: influence of low glucose Free Radic. Biol. Med. 45 2008 1591 1599
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1591-1599
    • Langston, W.1    Circu, M.L.2    Aw, T.Y.3
  • 33
    • 84874564486 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and Nrf2 signaling contribute to compromised responses to oxidative stress in striatal cells expressing full-length mutant huntingtin
    • Y.N. Jin, Y.V. Yu, S. Gundemir, C. Jo, M. Cui, K. Tieu, and G.V. Johnson Impaired mitochondrial dynamics and Nrf2 signaling contribute to compromised responses to oxidative stress in striatal cells expressing full-length mutant huntingtin PLoS One 8 2013 e57932
    • (2013) PLoS One , vol.8 , pp. 57932
    • Jin, Y.N.1    Yu, Y.V.2    Gundemir, S.3    Jo, C.4    Cui, M.5    Tieu, K.6    Johnson, G.V.7
  • 34
    • 84890247564 scopus 로고    scopus 로고
    • Inhibition of ERK-DLP1 signaling and mitochondrial division alleviates mitochondrial dysfunction in Alzheimers disease cybrid cell
    • X. Gan, S. Huang, L. Wu, Y. Wang, G. Hu, G. Li, H. Zhang, H. Yu, R.H. Swerdlow, J.X. Chen, and S.S. Yan Inhibition of ERK-DLP1 signaling and mitochondrial division alleviates mitochondrial dysfunction in Alzheimers disease cybrid cell Biochim. Biophys. Acta 1842 2014 220 231
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 220-231
    • Gan, X.1    Huang, S.2    Wu, L.3    Wang, Y.4    Hu, G.5    Li, G.6    Zhang, H.7    Yu, H.8    Swerdlow, R.H.9    Chen, J.X.10    Yan, S.S.11
  • 36
    • 34548508404 scopus 로고    scopus 로고
    • Mitochondrial-targeted active Akt protects SH-SY5Y neuroblastoma cells from staurosporine-induced apoptotic cell death
    • DOI 10.1002/jcb.21287
    • P. Mookherjee, R. Quintanilla, M.S. Roh, A.A. Zmijewska, R.S. Jope, and G.V. Johnson Mitochondrial-targeted active Akt protects SH-SY5Y neuroblastoma cells from staurosporine-induced apoptotic cell death J. Cell. Biochem. 102 2007 196 210 (Pubitemid 47378922)
    • (2007) Journal of Cellular Biochemistry , vol.102 , Issue.1 , pp. 196-210
    • Mookherjee, P.1    Quintanilla, R.2    Roh, M.-S.3    Zmijewska, A.A.4    Jope, R.S.5    Johnson, G.V.W.6
  • 39
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • C.P. LeBel, H. Ischiropoulos, and S.C. Bondy Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress Chem. Res. Toxicol. 5 1992 227 231
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 227-231
    • Lebel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 40
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine
    • V.P. Bindokas, J. Jordan, C.C. Lee, and R.J. Miller Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine J. Neurosci. 16 1996 1324 1336 (Pubitemid 26145913)
    • (1996) Journal of Neuroscience , vol.16 , Issue.4 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 42
    • 82355183880 scopus 로고    scopus 로고
    • Fluorescence measurement of mitochondrial membrane potential changes in cultured cells
    • D.G. Nicholls Fluorescence measurement of mitochondrial membrane potential changes in cultured cells Methods Mol. Biol. 810 2012 119 133
    • (2012) Methods Mol. Biol. , vol.810 , pp. 119-133
    • Nicholls, D.G.1
  • 44
    • 0018926038 scopus 로고
    • Interactions of insulin-like growth factors I and II and multiplication-stimulating activity with receptors and serum carrier proteins
    • M.M. Rechler, J. Zapf, S.P. Nissley, E.R. Froesch, A.C. Moses, J.M. Podskalny, E.E. Schilling, and R.E. Humbel Interactions of insulin-like growth factors I and II and multiplication-stimulating activity with receptors and serum carrier proteins Endocrinology 107 1980 1451 1459 (Pubitemid 10029739)
    • (1980) Endocrinology , vol.107 , Issue.5 , pp. 1451-1459
    • Rechler, M.M.1    Zapf, J.2    Nissley, S.P.3
  • 45
    • 44949142269 scopus 로고    scopus 로고
    • The selective detection of mitochondrial superoxide by live cell imaging
    • DOI 10.1038/nprot.2008.56, PII NPROT.2008.56
    • K.M. Robinson, M.S. Janes, and J.S. Beckman The selective detection of mitochondrial superoxide by live cell imaging Nat. Protoc. 3 2008 941 947 (Pubitemid 351818682)
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 941-947
    • Robinson, K.M.1    Janes, M.S.2    Beckman, J.S.3
  • 47
    • 41949126549 scopus 로고    scopus 로고
    • Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease
    • D. Lim, L. Fedrizzi, M. Tartari, C. Zuccato, E. Cattaneo, M. Brini, and E. Carafoli Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease J. Biol. Chem. 283 2008 5780 5789
    • (2008) J. Biol. Chem. , vol.283 , pp. 5780-5789
    • Lim, D.1    Fedrizzi, L.2    Tartari, M.3    Zuccato, C.4    Cattaneo, E.5    Brini, M.6    Carafoli, E.7
  • 49
    • 84890357270 scopus 로고    scopus 로고
    • Oxidizing effects of exogenous stressors in Huntingtons disease knock-in striatal cells - Protective effect of cystamine and creatine
    • M. Ribeiro, A.C. Silva, J. Rodrigues, L. Naia, and A.C. Rego Oxidizing effects of exogenous stressors in Huntingtons disease knock-in striatal cells - protective effect of cystamine and creatine Toxicol. Sci. 136 2013 487 499
    • (2013) Toxicol. Sci. , vol.136 , pp. 487-499
    • Ribeiro, M.1    Silva, A.C.2    Rodrigues, J.3    Naia, L.4    Rego, A.C.5
  • 50
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Y. Chen, J. Zhang, Y. Lin, Q. Lei, K.L. Guan, S. Zhao, and Y. Xiong Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS EMBO Rep. 12 2011 534 541
    • (2011) EMBO Rep. , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6    Xiong, Y.7
  • 51
    • 0038537298 scopus 로고    scopus 로고
    • PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells
    • DOI 10.1016/S0014-5793(03)00517-9
    • K. Nakaso, H. Yano, Y. Fukuhara, T. Takeshima, K. Wada-Isoe, and K. Nakashima PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells FEBS Lett. 546 2003 181 184 (Pubitemid 36782407)
    • (2003) FEBS Letters , vol.546 , Issue.2-3 , pp. 181-184
    • Nakaso, K.1    Yano, H.2    Fukuhara, Y.3    Takeshima, T.4    Wada-Isoe, K.5    Nakashima, K.6
  • 52
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the β-globin locus control region
    • DOI 10.1073/pnas.91.21.9926
    • P. Moi, K. Chan, I. Asunis, A. Cao, and Y.W. Kan Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region Proc. Natl. Acad. Sci. USA 91 1994 9926 9930 (Pubitemid 24311921)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.21 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 53
  • 54
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • DOI 10.1074/jbc.M206911200
    • H.C. Huang, T. Nguyen, and C.B. Pickett Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription J. Biol. Chem. 277 2002 42769 42774 (Pubitemid 35285650)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42769-42774
    • Huang, H.-C.1    Nguyen, T.2    Pickett, C.B.3
  • 55
    • 77950887186 scopus 로고    scopus 로고
    • Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation
    • S. Fourquet, R. Guerois, D. Biard, and M.B. Toledano Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation J. Biol. Chem. 285 2010 8463 8471
    • (2010) J. Biol. Chem. , vol.285 , pp. 8463-8471
    • Fourquet, S.1    Guerois, R.2    Biard, D.3    Toledano, M.B.4
  • 57
    • 25444524850 scopus 로고    scopus 로고
    • Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
    • DOI 10.1074/jbc.M502876200
    • A. Hahn-Windgassen, V. Nogueira, C.C. Chen, J.E. Skeen, N. Sonenberg, and N. Hay Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity J. Biol. Chem. 280 2005 32081 32089 (Pubitemid 41361813)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32081-32089
    • Hahn-Windgassen, A.1    Nogueira, V.2    Chen, C.-C.3    Skeen, J.E.4    Sonenberg, N.5    Hay, N.6
  • 58
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor creb
    • DOI 10.1038/35085068
    • B. Mayr, and M. Montminy Transcriptional regulation by the phosphorylation-dependent factor CREB Nat. Rev. Mol. Cell. Biol. 2 2001 599 609 (Pubitemid 33674011)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.8 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 59
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional Repression of PGC-1α by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration
    • DOI 10.1016/j.cell.2006.09.015, PII S0092867406012050
    • L. Cui, H. Jeong, F. Borovecki, C.N. Parkhurst, N. Tanese, and D. Krainc Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration Cell 127 2006 59 69 (Pubitemid 44466642)
    • (2006) Cell , vol.127 , Issue.1 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 62
    • 84855395163 scopus 로고    scopus 로고
    • Mutant huntingtins interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntingtons disease
    • U.P. Shirendeb, M.J. Calkins, M. Manczak, V. Anekonda, B. Dufour, J.L. McBride, P. Mao, and P.H. Reddy Mutant huntingtins interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntingtons disease Hum. Mol. Genet 21 2012 406 420
    • (2012) Hum. Mol. Genet , vol.21 , pp. 406-420
    • Shirendeb, U.P.1    Calkins, M.J.2    Manczak, M.3    Anekonda, V.4    Dufour, B.5    McBride, J.L.6    Mao, P.7    Reddy, P.H.8
  • 64
    • 84903275686 scopus 로고    scopus 로고
    • Physiological and pathological significance of dynamin-related protein 1 (Drp1)-dependent mitochondrial fission in the nervous system
    • B. Cho, S.Y. Choi, H.M. Cho, H.J. Kim, and W. Sun Physiological and pathological significance of dynamin-related protein 1 (Drp1)-dependent mitochondrial fission in the nervous system Exp. Neurobiol 22 2013 149 157
    • (2013) Exp. Neurobiol , vol.22 , pp. 149-157
    • Cho, B.1    Choi, S.Y.2    Cho, H.M.3    Kim, H.J.4    Sun, W.5
  • 65
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • C.J. Vlahos, W.F. Matter, K.Y. Hui, and R.F. Brown A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4- one (LY294002) J. Biol. Chem. 269 1994 5241 5248
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 67
    • 84882321254 scopus 로고    scopus 로고
    • Akt phosphorylates HK-II at Thr-473 and increases mitochondrial HK-II association to protect cardiomyocytes
    • D.J. Roberts, V.P. Tan-Sah, J.M. Smith, and S. Miyamoto Akt phosphorylates HK-II at Thr-473 and increases mitochondrial HK-II association to protect cardiomyocytes J. Biol. Chem. 288 2013 23798 23806
    • (2013) J. Biol. Chem. , vol.288 , pp. 23798-23806
    • Roberts, D.J.1    Tan-Sah, V.P.2    Smith, J.M.3    Miyamoto, S.4
  • 69
    • 33644852502 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A induction by redox activation of nuclear respiratory factor 1
    • DOI 10.1074/jbc.M508805200
    • C.A. Piantadosi, and H.B. Suliman Mitochondrial transcription factor A induction by redox activation of nuclear respiratory factor 1 J. Biol. Chem. 281 2006 324 333 (Pubitemid 43671192)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 324-333
    • Piantadosi, C.A.1    Suliman, H.B.2
  • 70
    • 0034915234 scopus 로고    scopus 로고
    • Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntington's disease
    • DOI 10.1023/A:1010911417383
    • A. Santamaria, F. Perez-Severiano, E. Rodriguez-Martinez, P.D. Maldonado, J. Pedraza-Chaverri, C. Rios, and J. Segovia Comparative analysis of superoxide dismutase activity between acute pharmacological models and a transgenic mouse model of Huntingtons disease Neurochem. Res. 26 2001 419 424 (Pubitemid 32691133)
    • (2001) Neurochemical Research , vol.26 , Issue.4 , pp. 419-424
    • Santamaria, A.1    Perez-Severiano, F.2    Rodriguez-Martinez, E.3    Maldonado, P.D.4    Pedraza-Chaverri, J.5    Rios, C.6    Segovia, J.7
  • 72
    • 66349129338 scopus 로고    scopus 로고
    • Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response
    • Z. Sun, Y.E. Chin, and D.D. Zhang Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response Mol. Cell. Biol. 29 2009 2658 2672
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2658-2672
    • Sun, Z.1    Chin, Y.E.2    Zhang, D.D.3
  • 73
    • 0344012006 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ROS in staurosporine-induced retinal cell apoptosis
    • DOI 10.1016/j.freeradbiomed.2003.08.022
    • J. Gil, S. Almeida, C.R. Oliveira, and A.C. Rego Cytosolic and mitochondrial ROS in staurosporine-induced retinal cell apoptosis Free Radic. Biol. Med. 35 2003 1500 1514 (Pubitemid 37452475)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.11 , pp. 1500-1514
    • Gil, J.1    Almeida, S.2    Oliveira, C.R.3    Rego, A.C.4
  • 74
    • 33644623231 scopus 로고    scopus 로고
    • Insulin neuroprotection against oxidative stress in cortical neurons - Involvement of uric acid and glutathione antioxidant defenses
    • A.I. Duarte, M.S. Santos, C.R. Oliveira, and A.C. Rego Insulin neuroprotection against oxidative stress in cortical neurons - involvement of uric acid and glutathione antioxidant defenses Free Radic. Biol. Med. 39 2005 876 889
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 876-889
    • Duarte, A.I.1    Santos, M.S.2    Oliveira, C.R.3    Rego, A.C.4
  • 78
    • 57049184027 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons
    • DOI 10.1093/hmg/ddn281
    • D. Zala, E. Colin, H. Rangone, G. Liot, S. Humbert, and F. Saudou Phosphorylation of mutant huntingtin at S421 restores anterograde and retrograde transport in neurons Hum. Mol. Genet 17 2008 3837 3846 (Pubitemid 352762847)
    • (2008) Human Molecular Genetics , vol.17 , Issue.24 , pp. 3837-3846
    • Zala, D.1    Colin, E.2    Rangone, H.3    Liot, G.4    Humbert, S.5    Saudou, F.6
  • 79
    • 20444448900 scopus 로고    scopus 로고
    • Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo
    • DOI 10.1093/hmg/ddi165
    • S.C. Warby, E.Y. Chan, M. Metzler, L. Gan, R.R. Singaraja, S.F. Crocker, H.A. Robertson, and M.R. Hayden Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo Hum. Mol. Genet 14 2005 1569 1577 (Pubitemid 40823464)
    • (2005) Human Molecular Genetics , vol.14 , Issue.11 , pp. 1569-1577
    • Warby, S.C.1    Chan, E.Y.2    Metzler, M.3    Gan, L.4    Singaraja, R.R.5    Crocker, S.F.6    Robertson, H.A.7    Hayden, M.R.8
  • 81
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • A. Yamamoto, M.L. Cremona, and J.E. Rothman Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway J. Cell. Biol. 172 2006 719 731
    • (2006) J. Cell. Biol. , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 86
    • 84887560529 scopus 로고    scopus 로고
    • Pizotifen Activates ERK and provides neuroprotection in vitro and in vivo in models of Huntingtons disease
    • M.R. Sarantos, T. Papanikolaou, L.M. Ellerby, and R.E. Hughes Pizotifen Activates ERK and provides neuroprotection in vitro and in vivo in models of Huntingtons disease J. Huntingtons Dis 1 2012 195 210
    • (2012) J. Huntingtons Dis , vol.1 , pp. 195-210
    • Sarantos, M.R.1    Papanikolaou, T.2    Ellerby, L.M.3    Hughes, R.E.4
  • 87
    • 15244340082 scopus 로고    scopus 로고
    • Insulin-like growth factor 1 inhibits extracellular signal-regulated kinase to promote neuronal survival via the phosphatidylinositol 3-kinase/protein kinase A/c-Raf pathway
    • DOI 10.1523/JNEUROSCI.5060-04.2005
    • S. Subramaniam, N. Shahani, J. Strelau, C. Laliberte, R. Brandt, D. Kaplan, and K. Unsicker Insulin-like growth factor 1 inhibits extracellular signal-regulated kinase to promote neuronal survival via the phosphatidylinositol 3-kinase/protein kinase A/c-Raf pathway J. Neurosci. 25 2005 2838 2852 (Pubitemid 40389242)
    • (2005) Journal of Neuroscience , vol.25 , Issue.11 , pp. 2838-2852
    • Subramaniam, S.1    Shahani, N.2    Strelau, J.3    Laliberte, C.4    Brandt, R.5    Kaplan, D.6    Unsicker, K.7
  • 88
    • 0037632930 scopus 로고    scopus 로고
    • Insulin inhibits extracellular regulated kinase 1/2 phosphorylation in a phosphatidylinositol 3-kinase (PI3) kinase-dependent manner in neuro2a cells
    • DOI 10.1046/j.1471-4159.2003.01828.x
    • L.P. van der Heide, M.F. Hoekman, G.J. Biessels, and W.H. Gispen Insulin inhibits extracellular regulated kinase 1/2 phosphorylation in a phosphatidylinositol 3-kinase (PI3) kinase-dependent manner in Neuro2a cells J. Neurochem. 86 2003 86 91 (Pubitemid 36753849)
    • (2003) Journal of Neurochemistry , vol.86 , Issue.1 , pp. 86-91
    • Van Der Heide, L.P.1    Hoekman, M.F.M.2    Biessels, G.J.3    Gispen, W.H.4
  • 89
  • 90
    • 24744444740 scopus 로고    scopus 로고
    • Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin
    • DOI 10.1074/jbc.M504749200
    • T. Milakovic, and G.V. Johnson Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin J. Biol. Chem. 280 2005 30773 30782 (Pubitemid 41291807)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30773-30782
    • Milakovic, T.1    Johnson, G.V.W.2
  • 91
    • 54449092109 scopus 로고    scopus 로고
    • Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: Possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease
    • R.A. Quintanilla, Y.N. Jin, K. Fuenzalida, M. Bronfman, and G.V. Johnson Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease J. Biol. Chem. 283 2008 25628 25637
    • (2008) J. Biol. Chem. , vol.283 , pp. 25628-25637
    • Quintanilla, R.A.1    Jin, Y.N.2    Fuenzalida, K.3    Bronfman, M.4    Johnson, G.V.5
  • 92
    • 79960079717 scopus 로고    scopus 로고
    • The striatum is highly susceptible to mitochondrial oxidative phosphorylation dysfunctions
    • A.M. Pickrell, H. Fukui, X. Wang, M. Pinto, and C.T. Moraes The striatum is highly susceptible to mitochondrial oxidative phosphorylation dysfunctions J. Neurosci. 31 2011 9895 9904
    • (2011) J. Neurosci. , vol.31 , pp. 9895-9904
    • Pickrell, A.M.1    Fukui, H.2    Wang, X.3    Pinto, M.4    Moraes, C.T.5
  • 93
    • 56549089781 scopus 로고    scopus 로고
    • Ayala-Torres, S. Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntingtons disease
    • K. Acevedo-Torres, L. Berrios, N. Rosario, V. Dufault, S. Skatchkov, M.J. Eaton, and C.A. Torres-Ramos Ayala-Torres, S. Mitochondrial DNA damage is a hallmark of chemically induced and the R6/2 transgenic model of Huntingtons disease DNA Repair (Amst.) 8 2009 126 136
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 126-136
    • Acevedo-Torres, K.1    Berrios, L.2    Rosario, N.3    Dufault, V.4    Skatchkov, S.5    Eaton, M.J.6    Torres-Ramos, C.A.7
  • 94
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • C. Richter, J.W. Park, and B.N. Ames Normal oxidative damage to mitochondrial and nuclear DNA is extensive Proc. Natl. Acad. Sci. USA 85 1988 6465 6467
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.W.2    Ames, B.N.3
  • 96
    • 0346434149 scopus 로고    scopus 로고
    • Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation
    • G.N. Bijur, and R.S. Jope Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation J. Neurochem. 87 2003 1427 1435 (Pubitemid 38020576)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.6 , pp. 1427-1435
    • Bijur, G.N.1    Jope, R.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.