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Volumn 9, Issue 3, 2014, Pages

Roles of autophagy in MPP+-induced neurotoxicity in vivo: The involvement of mitochondria and α-synuclein aggregation

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; ALPHA SYNUCLEIN; ATG7 PROTEIN; BIOLOGICAL MARKER; CHLORAL HYDRATE; CYTOCHROME C OXIDASE; HEME OXYGENASE 1; LC3 II PROTEIN; SMALL INTERFERING RNA; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; 1,3-BIS(4-HYDROXYPHENYL)-4-METHYL-5-(4-(2-PIPERIDINYLETHOXY)PHENOL)-1H-PYRAZOLE; ATG7 PROTEIN, RAT; CASP9 PROTEIN, RAT; CASPASE 9; LC3 PROTEIN, RAT; MICROTUBULE ASSOCIATED PROTEIN; PIPERIDINE DERIVATIVE; PROTEIN AGGREGATE; PYRAZOLE DERIVATIVE; TYROSINE 3 MONOOXYGENASE;

EID: 84898622934     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0091074     Document Type: Article
Times cited : (33)

References (53)
  • 1
    • 0034529528 scopus 로고    scopus 로고
    • Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy
    • Fengsrud M, Erichsen ES, Berg TO, Raiborg C, Seglen PO (2000) Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy. Eur J Cell Biol 79: 871-882. (Pubitemid 32000721)
    • (2000) European Journal of Cell Biology , vol.79 , Issue.12 , pp. 871-882
    • Fengsrud, M.1    Erichsen, E.S.2    Berg, T.O.3    Raiborg, C.4    Seglen, P.O.5
  • 4
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo AM (2004) Autophagy: in sickness and in health. Trends Cell Biol 14: 70-77.
    • (2004) Trends Cell Biol , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 5
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade P, Vyas S, Javoy-Agid F, Herrero MT, Michel PP, et al. (1997) Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 12: 25-31. (Pubitemid 27106916)
    • (1997) Histology and Histopathology , vol.12 , Issue.1 , pp. 25-31
    • Anglade, P.1
  • 6
    • 78650824020 scopus 로고    scopus 로고
    • Parkinson's disease involves autophagy and abnormal distribution of cathepsin L
    • Li L, Wang X, Fei X, Xia L, Qin Z, et al. (2011) Parkinson's disease involves autophagy and abnormal distribution of cathepsin L. Neurosci Lett 489:62-67
    • (2011) Neurosci Lett , vol.489 , pp. 62-67
    • Li, L.1    Wang, X.2    Fei, X.3    Xia, L.4    Qin, Z.5
  • 7
    • 82755161734 scopus 로고    scopus 로고
    • Autophagy and disease: Always two sides to a problem
    • Sridhar S, Botbol Y, Macian F, Cuervo AM (2012) Autophagy and disease: always two sides to a problem. J Pathol 226: 255-273.
    • (2012) J Pathol , vol.226 , pp. 255-273
    • Sridhar, S.1    Botbol, Y.2    Macian, F.3    Cuervo, A.M.4
  • 8
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • Hung SY, Huang WP, Liou HC, Fu WM (2009) Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy 5: 502-510.
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3    Fu, W.M.4
  • 10
    • 84877615360 scopus 로고    scopus 로고
    • Therapeutic induction of autophagy to modulate neurodegenerative disease progression
    • Hochfeld WE, Lee S, Rubinsztein DC (2013) Therapeutic induction of autophagy to modulate neurodegenerative disease progression. Acta Pharmacol Sin 34: 600-604.
    • (2013) Acta Pharmacol Sin , vol.34 , pp. 600-604
    • Hochfeld, W.E.1    Lee, S.2    Rubinsztein, D.C.3
  • 11
    • 84871606902 scopus 로고    scopus 로고
    • Therapeutic Effects of Rapamycin on MPTP-Induced Parkinsonism in Mice
    • Liu K, Shi N, Sun Y, Zhang T, Sun X (2013) Therapeutic Effects of Rapamycin on MPTP-Induced Parkinsonism in Mice. Neurochem Res 38: 201-207.
    • (2013) Neurochem Res , vol.38 , pp. 201-207
    • Liu, K.1    Shi, N.2    Sun, Y.3    Zhang, T.4    Sun, X.5
  • 12
    • 84858748850 scopus 로고    scopus 로고
    • Melatonin attenuates kainic acid-induced neurotoxicity in mouse hippocampus via inhibition of autophagy and α-synuclein aggregation
    • Chang CF, Huang HJ, Lee HC, Hung KC, Wu RT, et al. (2012) Melatonin attenuates kainic acid-induced neurotoxicity in mouse hippocampus via inhibition of autophagy and α-synuclein aggregation. J Pineal Res 52: 312-21.
    • (2012) J Pineal Res , vol.52 , pp. 312-321
    • Chang, C.F.1    Huang, H.J.2    Lee, H.C.3    Hung, K.C.4    Wu, R.T.5
  • 13
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • Zhu JH, Horbinski C, Guo F, Watkins S, Uchiyama Y, et al. (2000) Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 170: 75-86.
    • (2000) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5
  • 17
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy mitochondria and oxidative stress: Cross-talk and redox signalling
    • Lee J, Giordano S, Zhang J (2012) Autophagy mitochondria and oxidative stress: cross-talk and redox signalling. Biochem J 41: 523-540.
    • (2012) Biochem J , vol.41 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 18
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • DOI 10.1038/47513
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, et al. (2004) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloidbeta. Nature 403: 98-103. (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 19
    • 0025116342 scopus 로고
    • Mechanism of the neurotoxicity of MPTP
    • Singer TP, Ramsay RR (1990) Mechanism of the neurotoxicity of MPTP. FEBS Lett 274: 1-8.
    • (1990) FEBS Lett , vol.274 , pp. 1-8
    • Singer, T.P.1    Ramsay, R.R.2
  • 20
    • 84861544095 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to depletion of functional mitochondria in chronic MPP+ toxicity: Dual roles for ERK1/2
    • Zhu J H, Gusdon AM, Cimen H, Van Houten B, Koc E, et al. (2012) Impaired mitochondrial biogenesis contributes to depletion of functional mitochondria in chronic MPP+ toxicity: dual roles for ERK1/2. Cell Death Dis 3: e312.
    • (2012) Cell Death Dis , vol.3
    • Zhu, J.H.1    Gusdon, A.M.2    Cimen, H.3    Van Houten, B.4    Koc, E.5
  • 21
    • 84880756245 scopus 로고    scopus 로고
    • Defective autophagy in Parkinson's disease: Role of oxidative stress
    • Janda E, Isidoro C, Carresi C, Mollace V (2012) Defective autophagy in Parkinson's disease: role of oxidative stress. Mol Neurobiol 46: 639-661.
    • (2012) Mol Neurobiol , vol.46 , pp. 639-661
    • Janda, E.1    Isidoro, C.2    Carresi, C.3    Mollace, V.4
  • 22
    • 84867786709 scopus 로고    scopus 로고
    • N-Acetylcysteine protects against methamphetamine-induced dopaminergic neurodegeneration via modulation of redox status and autophagy in dopaminergic cells
    • Chandramani Shivalingappa P, Jin H, Anantharam V, Kanthasamy A, Kanthasamy A (2012) N-Acetylcysteine protects against methamphetamine-induced dopaminergic neurodegeneration via modulation of redox status and autophagy in dopaminergic cells. Parkinsons Dis Article ID 424285.
    • (2012) Parkinsons Dis , pp. 424285
    • Chandramani Shivalingappa, P.1    Jin, H.2    Anantharam, V.3    Kanthasamy, A.4    Kanthasamy, A.5
  • 23
    • 73449111577 scopus 로고    scopus 로고
    • Mitochondrial autophagy as a compensatory response to PINK1 deficiency
    • Cherra SJ, Dagda RK, Tandon A, Chu CT (2009) Mitochondrial autophagy as a compensatory response to PINK1 deficiency. Autophagy 5: 1213-1214.
    • (2009) Autophagy , vol.5 , pp. 1213-1214
    • Cherra, S.J.1    Dagda, R.K.2    Tandon, A.3    Chu, C.T.4
  • 24
    • 79956124664 scopus 로고    scopus 로고
    • Autophagic pathways in Parkinson disease and related disorders
    • Xilouri M, Stefanis L (2011). Autophagic pathways in Parkinson disease and related disorders. Expert Rev Mol Med 13: e8.
    • (2011) Expert Rev Mol Med , vol.13
    • Xilouri, M.1    Stefanis, L.2
  • 25
    • 0032540327 scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson WS, Jonas A, Clayton DF, George JM (1988) Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 273: 9443-49.
    • (1988) J Biol Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 26
    • 84864870837 scopus 로고    scopus 로고
    • Alpha-synuclein: From secretion to dysfunction and death
    • Marques O, Outeiro TF (2012) Alpha-synuclein: from secretion to dysfunction and death. Cell Death Dis 3: e350.
    • (2012) Cell Death Dis , vol.3
    • Marques, O.1    Outeiro, T.F.2
  • 29
    • 0032500599 scopus 로고    scopus 로고
    • Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • DOI 10.1074/jbc.273.41.26292
    • Jensen PH, Nielsen MS, Jakes R, Dotti CG, Goedert M (1998) Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J Biol Chem 273: 26292-26294. (Pubitemid 28471629)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 30
    • 84860471851 scopus 로고    scopus 로고
    • Role of α-synuclein protein levels in mitochondrial morphology and cell survival in cell lines
    • Zhu M, Li W, Lu C (2012) Role of α-synuclein protein levels in mitochondrial morphology and cell survival in cell lines. PLoS One 7: e36377.
    • (2012) PLoS One , vol.7
    • Zhu, M.1    Li, W.2    Lu, C.3
  • 31
    • 67049137602 scopus 로고    scopus 로고
    • + impairs autophagic clearance of α-synuclein by impairing the activity of dynein
    • + impairs autophagic clearance of α-synuclein by impairing the activity of dynein. Neuroreport 20: 569-573.
    • (2009) Neuroreport , vol.20 , pp. 569-573
    • Cai, Z.L.1    Shi, J.J.2    Yang, Y.P.3    Cao, B.Y.4    Wang, F.5
  • 33
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: When the cleaning crew goes on strike
    • DOI 10.1016/S1474-4422(07)70076-5, PII S1474442207700765
    • Martinez-Vicente M, Cuervo AM (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 6: 352-361. (Pubitemid 46367949)
    • (2007) Lancet Neurology , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 36
    • 0024991212 scopus 로고
    • Fluorescent and crosslinked protein formed by free radical and aldehyde species generated during lipid peroxidation
    • Kikugawa K, Kato T, Beppu M, Haysaaka A (1989) Fluorescent and crosslinked protein formed by free radical and aldehyde species generated during lipid peroxidation. Adv Exp Med Biol 266: 345-356.
    • (1989) Adv Exp Med Biol , vol.266 , pp. 345-356
    • Kikugawa, K.1    Kato, T.2    Beppu, M.3    Haysaaka, A.4
  • 39
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblotting
    • Mizushima N, Yoshimori T (2007) How to interpret LC3 immunoblotting. Autophagy 3: 542-545. (Pubitemid 350060049)
    • (2007) Autophagy , vol.3 , Issue.6 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 40
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in eurodegeneration
    • Rubinsztein DC (2006) The roles of intracellular protein-degradation pathways in eurodegeneration. Nature 443: 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 41
    • 1842608814 scopus 로고    scopus 로고
    • Heme oxygenase-1: Transducer of pathological brain iron sequestration under oxidative stress
    • Schipper HM (2004) Heme oxygenase-1: transducer of pathological brain iron sequestration under oxidative stress. Ann NY Acad Sci 1012: 84-93.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 84-93
    • Schipper, H.M.1
  • 42
    • 0036420161 scopus 로고    scopus 로고
    • Increase in mitochondrial mass in human fibroblasts under oxidative stress and during replicative cell senescence
    • Lee HC, Yin PH, Chi CW, Wei YH (2002) Increase in mitochondrial mass in human fibroblasts under oxidative stress and during replicative cell senescence. J Biomed Sci 9: 517-26.
    • (2002) J Biomed Sci , vol.9 , pp. 517-526
    • Lee, H.C.1    Yin, P.H.2    Chi, C.W.3    Wei, Y.H.4
  • 43
    • 0033614441 scopus 로고    scopus 로고
    • Oxidative stress and upregulation of mitochondrial biogenesis genes in mitochondrial DNA-depleted HeLa cells
    • DOI 10.1006/bbrc.1999.0580
    • Miranda S, Foncea R, Guerrero J, Leighton F (1999) Oxidative stress and upregulation of mitochondrial biogenesis genes in mitochondrial DNA-depleted HeLa cells. Biochem Biophys Res Commun 258:44-49. (Pubitemid 29286999)
    • (1999) Biochemical and Biophysical Research Communications , vol.258 , Issue.1 , pp. 44-49
    • Miranda, S.1    Foncea, R.2    Guerrero, J.3    Leighton, F.4
  • 44
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey B, Lansbury PT (2003) Protofibrils pores fibrils and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26: 267-298. (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 45
    • 34848872767 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is involved in arsenite-induced oxidative injury in rat brain
    • DOI 10.1016/j.taap.2007.06.016, PII S0041008X07002785
    • Lin AM, Chao PL, Fang SF, Chi CW, Yang CH (2007) Endoplasmic reticulum stress is involved in arsenite-induced oxidative injury in rat brain. Toxicol Appl Pharmacol 224: 138-146. (Pubitemid 47494512)
    • (2007) Toxicology and Applied Pharmacology , vol.224 , Issue.2 , pp. 138-146
    • Lin, A.M.Y.1    Chao, P.L.2    Fang, S.F.3    Chi, C.W.4    Yang, C.H.5
  • 46
    • 78349268336 scopus 로고    scopus 로고
    • Anti-inflammatory effects of pioglitazone on iron-induced oxidative injury in the nigrostriatal dopaminergic system
    • Yu HC, Feng SF, Chao PL, Lin AM (2010) Anti-inflammatory effects of pioglitazone on iron-induced oxidative injury in the nigrostriatal dopaminergic system. Neuropathol Applied Neurobiol 36: 612-622.
    • (2010) Neuropathol Applied Neurobiol , vol.36 , pp. 612-622
    • Yu, H.C.1    Feng, S.F.2    Chao, P.L.3    Lin, A.M.4
  • 47
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295. (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 48
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L (2008) Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 283: 23542-23556.
    • (2008) J Biol Chem , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 49
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of α-Synuclein Oligomeric Intermediates via the Lysosomal Degradation Pathway
    • DOI 10.1523/JNEUROSCI.3809-03.2004
    • Lee HJ, Khoshaghideh F, Patel S, Lee SJ (2004) Clearance of α-synuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci 24: 1888-1896. (Pubitemid 38292800)
    • (2004) Journal of Neuroscience , vol.24 , Issue.8 , pp. 1888-1896
    • Lee, H.-J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.-J.4
  • 50
    • 79551647443 scopus 로고    scopus 로고
    • Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson's disease
    • Bellucci A, Navarria L, Zaltieri M, Falarti E, Bodei S, et al. (2011) Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson's disease. J Neurochem 116:588-605
    • (2011) J Neurochem , vol.116 , pp. 588-605
    • Bellucci, A.1    Navarria, L.2    Zaltieri, M.3    Falarti, E.4    Bodei, S.5
  • 51
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • DOI 10.1038/47513
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, et al. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloidbeta. Nature 403: 98-103 (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 53
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • DOI 10.1016/j.molcel.2004.12.021, PII S1097276505010087
    • Bennett E, Bence N, Jayakumar R, Kopito R (2005) Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 17: 351-65. (Pubitemid 40193307)
    • (2005) Molecular Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4


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