메뉴 건너뛰기




Volumn 4, Issue 4, 2011, Pages 378-384

Pathological accumulation of atrophin-1 in dentatorubralpallidoluysian atrophy

Author keywords

Atrophin 1 (ATN1); Dentatorubral pallidoluysian atrophy (DRPLA); Neurodegeneration; Polyglutamine (polyQ) disease

Indexed keywords

ATROPHIN 1; ATROPHIN-1; NERVE PROTEIN; PEPTIDE; POLYGLUTAMINE;

EID: 80051607553     PISSN: None     EISSN: 19362625     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi HY and Orr HT. Glutamine repeats and neurodegeneration. Annu Rev Neurosci 2000; 23: 217-247.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 2
    • 65349094883 scopus 로고    scopus 로고
    • Pathological mechanism of neurodegeneration in polyglutamine diseases
    • Edited by Pandalai SG. India, Research Signpost
    • Yazawa I: Pathological mechanism of neurodegeneration in polyglutamine diseases. Recent Research Developments in Biophysics and Biochemistry Vol. 3. Edited by Pandalai SG. India, Research Signpost, 2003, pp. 21-28.
    • (2003) Recent Research Developments in Biophysics and Biochemistry , vol.3 , pp. 21-28
    • Yazawa, I.1
  • 3
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr HT and Zoghbi HY. Trinucleotide repeat disorders. Annu Rev Neurosci 2007; 30: 575-621.
    • (2007) Annu Rev Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 6
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, and Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997; 277: 1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 11
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, Clark HB, Zoghbi HY, and Orr HT. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 1998; 95: 41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 12
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA and Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10(Suppl.): S10-S17.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 13
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, and Greenberg ME. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 1998; 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 15
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 16
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross CA. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 2002; 35: 819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 17
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sánchez I, Mahlke C, and Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 2003; 421: 373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sánchez, I.1    Mahlke, C.2    Yuan, J.3
  • 19
    • 18644379256 scopus 로고    scopus 로고
    • Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno M, Adachi H, Kume A, Li M, Nakagomi Y, Niwa H, Sang C, Kobayashi Y, Doyu M, and Sobue G. Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 2002; 35: 843-854.
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1    Adachi, H.2    Kume, A.3    Li, M.4    Nakagomi, Y.5    Niwa, H.6    Sang, C.7    Kobayashi, Y.8    Doyu, M.9    Sobue, G.10
  • 22
    • 78449292904 scopus 로고    scopus 로고
    • Proteolytic processing regulates pathological accumulation in dentatorubralpallidoluysian atrophy
    • Suzuki Y, Nakayama K, Hashimoto N, and Yazawa I. Proteolytic processing regulates pathological accumulation in dentatorubralpallidoluysian atrophy. FEBS J 2010; 277: 4873-4887.
    • (2010) FEBS J , vol.277 , pp. 4873-4887
    • Suzuki, Y.1    Nakayama, K.2    Hashimoto, N.3    Yazawa, I.4
  • 23
    • 0001294843 scopus 로고
    • Unusual form of cerebellar ataxia; combined dentatorubral and pallido-Luysian degeneration
    • Smith JK, Gonda VE, and Malamud N. Unusual form of cerebellar ataxia; combined dentatorubral and pallido-Luysian degeneration. Neurology 1958; 8: 205-209.
    • (1958) Neurology , vol.8 , pp. 205-209
    • Smith, J.K.1    Gonda, V.E.2    Malamud, N.3
  • 24
    • 0020064620 scopus 로고
    • Familial myoclonus epilepsy and choreoathetosis: hereditary dentatorubral-pallidoluysian atrophy
    • Naito H and Oyanagi S. Familial myoclonus epilepsy and choreoathetosis: hereditary dentatorubral-pallidoluysian atrophy. Neurology 1982; 32: 798-807.
    • (1982) Neurology , vol.32 , pp. 798-807
    • Naito, H.1    Oyanagi, S.2
  • 25
    • 0023680089 scopus 로고
    • Hereditary dentatorubral-pallidoluysian atrophy: clinical and pathological variants in family
    • Takahashi H, Ohama E, Naito H, Takeda S, Nakashima S, Makifuchi T, and Ikuta F. Hereditary dentatorubral-pallidoluysian atrophy: clinical and pathological variants in family. Neurology 1988; 38: 1065-1070.
    • (1988) Neurology , vol.38 , pp. 1065-1070
    • Takahashi, H.1    Ohama, E.2    Naito, H.3    Takeda, S.4    Nakashima, S.5    Makifuchi, T.6    Ikuta, F.7
  • 30
    • 0029015557 scopus 로고
    • Abnormal gene product identified in hereditary dentatorubralpallidoluysian atrophy (DRPLA) brain
    • Yazawa I, Nukina N, Hashida H, Goto J, Yamada M, and Kanazawa I. Abnormal gene product identified in hereditary dentatorubralpallidoluysian atrophy (DRPLA) brain. Nat Genet 1995; 10: 3-4.
    • (1995) Nat Genet , vol.10 , pp. 3-4
    • Yazawa, I.1    Nukina, N.2    Hashida, H.3    Goto, J.4    Yamada, M.5    Kanazawa, I.6
  • 31
    • 0032497248 scopus 로고    scopus 로고
    • Expanded glutamine repeat enhances complex formation of dentatorubral-pallidoluysian atrophy (DRPLA) protein in human brains
    • Yazawa I, Hazeki N, and Kanazawa I. Expanded glutamine repeat enhances complex formation of dentatorubral-pallidoluysian atrophy (DRPLA) protein in human brains. Biochem Biophys Res Commun 1998; 250: 22-26.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 22-26
    • Yazawa, I.1    Hazeki, N.2    Kanazawa, I.3
  • 32
    • 9444220784 scopus 로고    scopus 로고
    • Sharing of polyglutamine localization by the neuronal nucleus and cytoplasm in CAG-repeat diseases
    • Yamada M, Tan CF, Inenaga C, Tsuji S, and Takahashi H. Sharing of polyglutamine localization by the neuronal nucleus and cytoplasm in CAG-repeat diseases. Neuropathol Appl Neurobiol 2004; 30: 665-675.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 665-675
    • Yamada, M.1    Tan, C.F.2    Inenaga, C.3    Tsuji, S.4    Takahashi, H.5
  • 36
    • 0031948607 scopus 로고    scopus 로고
    • Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy
    • Merry DE, Kobayashi Y, Bailey CK, Taye AA, and Fischbeck KH. Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy. Hum Mol Genet 1998; 7: 693-701.
    • (1998) Hum Mol Genet , vol.7 , pp. 693-701
    • Merry, D.E.1    Kobayashi, Y.2    Bailey, C.K.3    Taye, A.A.4    Fischbeck, K.H.5
  • 38
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpaindependent proteolysis
    • Kim YJ, Yi Y, Sapp E, Wang Y, Cuiffo B, Kegel KB, Qin ZH, Aronin N, and DiFiglia M. Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpaindependent proteolysis. Proc Natl Acad Sci USA. 2001; 98: 12784-12789.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.H.7    Aronin, N.8    DiFiglia, M.9
  • 39
    • 0030670816 scopus 로고    scopus 로고
    • Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis
    • Miyashita T, Okamura-Oho Y, Mito Y, Nagafuchi S, and Yamada M. Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis. J Biol Chem 1997; 272: 29238-29242.
    • (1997) J Biol Chem , vol.272 , pp. 29238-29242
    • Miyashita, T.1    Okamura-Oho, Y.2    Mito, Y.3    Nagafuchi, S.4    Yamada, M.5
  • 42
    • 3342980580 scopus 로고    scopus 로고
    • The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling
    • McLaughlin B. The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling. Apoptosis 2004; 9: 111-121.
    • (2004) Apoptosis , vol.9 , pp. 111-121
    • McLaughlin, B.1
  • 43
    • 0036372055 scopus 로고    scopus 로고
    • Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3
    • Lu C, Fu W, Selvesen GS, and Mattson MP. Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3. Neuromolecular Med 2002; 1: 69-79.
    • (2002) Neuromolecular Med , vol.1 , pp. 69-79
    • Lu, C.1    Fu, W.2    Selvesen, G.S.3    Mattson, M.P.4
  • 44
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A and Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003; 40: 427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 45
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamineinduced pathology in SCA1 mice
    • Cummings CJ, Reinstein E, Sun Y, Antalffy B, Jiang Y, Ciechanover A, Orr HT, Beaudet AL, and Zoghbi HY. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamineinduced pathology in SCA1 mice. Neuron 1999; 24: 879-892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 47
    • 0942287194 scopus 로고    scopus 로고
    • Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways
    • Chai Y, Berke SS, Cohen RE, and Paulson HL. Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways. J Biol Chem 2004; 279: 3605-3611.
    • (2004) J Biol Chem , vol.279 , pp. 3605-3611
    • Chai, Y.1    Berke, S.S.2    Cohen, R.E.3    Paulson, H.L.4
  • 48
    • 0033600134 scopus 로고    scopus 로고
    • Abnormal dentatorubral-pallidoluysian atrophy (DRPLA) protein complex is pathologically ubiquitinated in DRPLA brains
    • Yazawa I, Nakase H, and Kurisaki H. Abnormal dentatorubral-pallidoluysian atrophy (DRPLA) protein complex is pathologically ubiquitinated in DRPLA brains. Biochem Biophys Res Commun 1999; 260: 133-138.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 133-138
    • Yazawa, I.1    Nakase, H.2    Kurisaki, H.3
  • 49
    • 33747881231 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disease: friend, foe or turncoat?
    • Nixon RA. Autophagy in neurodegenerative disease: friend, foe or turncoat? Trends Neurosci 2006; 29: 528-535.
    • (2006) Trends Neurosci , vol.29 , pp. 528-535
    • Nixon, R.A.1
  • 50
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, and Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451: 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 51
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castaño JG, Aronin N, and DiFiglia M. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000; 20: 7268-7278.
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castaño, J.G.5    Aronin, N.6    DiFiglia, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.