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Volumn 3, Issue 2, 2000, Pages 157-163

Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1

Author keywords

[No Author keywords available]

Indexed keywords

POLYGLUTAMINE;

EID: 0033995175     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/72101     Document Type: Article
Times cited : (333)

References (47)
  • 2
    • 0032528167 scopus 로고    scopus 로고
    • Mice lacking ataxin-1 display learning deficits and decreased hippocampal paired-pulse facilitation
    • Matilla, A. et al. Mice lacking ataxin-1 display learning deficits and decreased hippocampal paired-pulse facilitation. J. Neurosci. 18, 5508-5516 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 5508-5516
    • Matilla, A.1
  • 3
    • 0029163222 scopus 로고
    • SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat
    • Burright, E. N. et al. SCA1 transgenic mice: a model for neurodegeneration caused by an expanded CAG trinucleotide repeat. Cell 82, 937-948 (1995).
    • (1995) Cell , vol.82 , pp. 937-948
    • Burright, E.N.1
  • 4
    • 0030864463 scopus 로고    scopus 로고
    • Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations
    • Clark, H. B. et al. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations. J. Neurosci. 17, 7385-7395 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 7385-7395
    • Clark, H.B.1
  • 5
    • 0030666001 scopus 로고    scopus 로고
    • Ataxin-1 with extra glutamines induces alterations in nuclear matrix-associated structures
    • Skinner, P. J. et al. Ataxin-1 with extra glutamines induces alterations in nuclear matrix-associated structures. Nature 389, 971-974 (1997).
    • (1997) Nature , vol.389 , pp. 971-974
    • Skinner, P.J.1
  • 6
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement, I. A. et al. Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95, 41-53 (1998).
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1
  • 7
    • 0032511057 scopus 로고    scopus 로고
    • Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum
    • Dai, Q. et al. Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. J. Biol. Chem. 273, 15030-15034 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15030-15034
    • Dai, Q.1
  • 8
    • 0031020235 scopus 로고    scopus 로고
    • Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis
    • Imai, Y., Davey, J., Kawagishi-Kobayashi, M. & Yamamoto, M. Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis. Mol. Cell. Biol. 17, 1543-1551 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1543-1551
    • Imai, Y.1    Davey, J.2    Kawagishi-Kobayashi, M.3    Yamamoto, M.4
  • 10
    • 15144355753 scopus 로고    scopus 로고
    • 2+ channel isoforms in mouse brain
    • 2+ channel isoforms in mouse brain. Neuroreport 9, 507-515 (1998).
    • (1998) Neuroreport , vol.9 , pp. 507-515
    • Mori, Y.1
  • 11
    • 0029958203 scopus 로고    scopus 로고
    • EAAT4 is a post-synaptic glutamate transporter at Purkinje cell synapses
    • Yamada, K. et al. EAAT4 is a post-synaptic glutamate transporter at Purkinje cell synapses. Neuroreport 7, 2013-2017 (1996).
    • (1996) Neuroreport , vol.7 , pp. 2013-2017
    • Yamada, K.1
  • 12
    • 0026717024 scopus 로고
    • Comparison of neuronal inositol 1,4,5-trisphosphate 3-kinase and receptor mRNA distributions in the adult rat brain using in situ hybridization histochemistry
    • Mailleux, P., Takazawa, K., Erneux, C. & Vanderhaeghen, J. J. Comparison of neuronal inositol 1,4,5-trisphosphate 3-kinase and receptor mRNA distributions in the adult rat brain using in situ hybridization histochemistry. Neuroscience 49, 577-590 (1992).
    • (1992) Neuroscience , vol.49 , pp. 577-590
    • Mailleux, P.1    Takazawa, K.2    Erneux, C.3    Vanderhaeghen, J.J.4
  • 13
    • 0030725663 scopus 로고    scopus 로고
    • Expression of rat cGMP-binding cGMP-specific phosphodiesterase mRNA in Purkinje cell layers during postnatal neuronal development
    • Kotera, J. et al. Expression of rat cGMP-binding cGMP-specific phosphodiesterase mRNA in Purkinje cell layers during postnatal neuronal development. Eur. J. Biochem. 249 ,434-442 (1997).
    • (1997) Eur. J. Biochem. , vol.249 , pp. 434-442
    • Kotera, J.1
  • 14
    • 0028980413 scopus 로고
    • The rat phospholipase C beta 4 gene is expressed at high abundance in cerebellar Purkinje cells
    • Roustan, P. et al. The rat phospholipase C beta 4 gene is expressed at high abundance in cerebellar Purkinje cells. Neuroreport 6, 1837-1841 (1995).
    • (1995) Neuroreport , vol.6 , pp. 1837-1841
    • Roustan, P.1
  • 15
    • 0025943056 scopus 로고
    • Isolation of two cDNAs encoding novel alpha 1-antichymotrypsin-like proteins in a murine chondrocytic cell line
    • Inglis, J. D., Lee, M., Davidson, D. R. & Hill, R. E. Isolation of two cDNAs encoding novel alpha 1-antichymotrypsin-like proteins in a murine chondrocytic cell line. Gene 106, 213-220 (1991).
    • (1991) Gene , vol.106 , pp. 213-220
    • Inglis, J.D.1    Lee, M.2    Davidson, D.R.3    Hill, R.E.4
  • 16
    • 0028301839 scopus 로고
    • Neurotrophic regulation of mouse muscle beta-amyloid protein precursor and alpha 1-antichymotrypsin as revealed by axotomy
    • Akaaboune, M., Ma, J., Festoff, B. W., Greenberg, B. D. & Hantai, D. Neurotrophic regulation of mouse muscle beta-amyloid protein precursor and alpha 1-antichymotrypsin as revealed by axotomy. J. Neurobiol. 25, 503-514 (1994).
    • (1994) J. Neurobiol. , vol.25 , pp. 503-514
    • Akaaboune, M.1    Ma, J.2    Festoff, B.W.3    Greenberg, B.D.4    Hantai, D.5
  • 17
    • 0032192481 scopus 로고    scopus 로고
    • Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation
    • Jiang, Y. H. et al. Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 21,799-811 (1998).
    • (1998) Neuron , vol.21 , pp. 799-811
    • Jiang, Y.H.1
  • 18
    • 0023838532 scopus 로고
    • Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • Abraham, C. R., Selkoe, D. J. & Potter, H. Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52, 487-501 (1988).
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 19
    • 0028889206 scopus 로고
    • Expression of the Alzheimer amyloid-promoting factor antichymotrypsin is induced in human astrocytes by IL-1
    • Das, S. & Potter, H. Expression of the Alzheimer amyloid-promoting factor antichymotrypsin is induced in human astrocytes by IL-1. Neuron 14, 447-456 (1995).
    • (1995) Neuron , vol.14 , pp. 447-456
    • Das, S.1    Potter, H.2
  • 20
    • 0026004598 scopus 로고
    • Developmental expression of alpha 1-antichymotrypsin in brain may be related to astrogliosis
    • Koo, E. H., Abraham, C. R., Potter, H., Cork, L. C. & Price, D. L. Developmental expression of alpha 1-antichymotrypsin in brain may be related to astrogliosis. Neurobiol. Aging 12, 495-501 (1991).
    • (1991) Neurobiol. Aging , vol.12 , pp. 495-501
    • Koo, E.H.1    Abraham, C.R.2    Potter, H.3    Cork, L.C.4    Price, D.L.5
  • 21
    • 0030872228 scopus 로고    scopus 로고
    • Extra-junctional localization of glutamate transporter EAAT4 at excitatory Purkinje cell synapses
    • Tanaka, J., Ichikawa, R., Watanabe, M., Tanaka, K. & Inoue, Y. Extra-junctional localization of glutamate transporter EAAT4 at excitatory Purkinje cell synapses. Neuroreport 8, 2461-2464 (1997).
    • (1997) Neuroreport , vol.8 , pp. 2461-2464
    • Tanaka, J.1    Ichikawa, R.2    Watanabe, M.3    Tanaka, K.4    Inoue, Y.5
  • 22
    • 12644282563 scopus 로고    scopus 로고
    • On the molecular basis and regulation of cellular capacitative calcium entry: Roles for Trp proteins
    • Birnbaumer, L. et al. On the molecular basis and regulation of cellular capacitative calcium entry: roles for Trp proteins. Proc. Natl. Acad. Sci. USA 93, 15195-15202 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15195-15202
    • Birnbaumer, L.1
  • 23
    • 0029994314 scopus 로고    scopus 로고
    • 2+ entry
    • 2+ entry. Cell 85, 661-671 (1996).
    • (1996) Cell , vol.85 , pp. 661-671
    • Zhu, X.1
  • 24
    • 0029905185 scopus 로고    scopus 로고
    • The family of inositol and phosphatidylinositol polyphosphate 5-phosphatases
    • Drayer, A. L. et al. The family of inositol and phosphatidylinositol polyphosphate 5-phosphatases. Biochem. Soc. Trans. 24, 1001-1005 (1996).
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 1001-1005
    • Drayer, A.L.1
  • 25
    • 0030663666 scopus 로고    scopus 로고
    • Inositol lipid 5-phosphatases - Traffic signals and signal traffic
    • Woscholski, R. & Parker, P. J. Inositol lipid 5-phosphatases - traffic signals and signal traffic. Trends Biochem. Sci. 22, 427-431 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 427-431
    • Woscholski, R.1    Parker, P.J.2
  • 26
    • 0028263379 scopus 로고
    • Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells
    • De Smedt, F., Verjans, B., Mailleux, P. & Erneux, C. Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 347, 69-72 (1994).
    • (1994) FEBS Lett. , vol.347 , pp. 69-72
    • De Smedt, F.1    Verjans, B.2    Mailleux, P.3    Erneux, C.4
  • 27
    • 0026610662 scopus 로고
    • 2+-ATPase, and calsequestrin
    • 2+-ATPase, and calsequestrin. J. Neurosci. 12, 489-505 (1992).
    • (1992) J. Neurosci. , vol.12 , pp. 489-505
    • Takei, K.1
  • 28
    • 0026624823 scopus 로고
    • 2+ transport
    • 2+ transport. Neuroscience 49, 467-477 (1992).
    • (1992) Neuroscience , vol.49 , pp. 467-477
    • Villa, A.1
  • 30
    • 13344250473 scopus 로고    scopus 로고
    • Ataxia and epileptic seizures in mice lacking type 1 inositol 1,4,5-trisphosphate receptor
    • Matsumoto, M. et al. Ataxia and epileptic seizures in mice lacking type 1 inositol 1,4,5-trisphosphate receptor. Nature 379, 168-171 (1996).
    • (1996) Nature , vol.379 , pp. 168-171
    • Matsumoto, M.1
  • 31
    • 0031021124 scopus 로고    scopus 로고
    • The type 1 inositol 1,4,5-trisphosphate receptor gene is altered in the opisthotonos mouse
    • Street, V. A. et al. The type 1 inositol 1,4,5-trisphosphate receptor gene is altered in the opisthotonos mouse. J. Neurosci. 17, 635-645 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 635-645
    • Street, V.A.1
  • 32
    • 0025898829 scopus 로고
    • Localization of an endoplasmic reticulum calcium ATPase mRNA in rat brain by in situ hybridization
    • Miller, K. K., Verma, A., Snyder, S. H. & Ross, C. A. Localization of an endoplasmic reticulum calcium ATPase mRNA in rat brain by in situ hybridization. Neuroscience 43, 1-9 (1991).
    • (1991) Neuroscience , vol.43 , pp. 1-9
    • Miller, K.K.1    Verma, A.2    Snyder, S.H.3    Ross, C.A.4
  • 33
    • 0025939795 scopus 로고
    • Immunohistochemical localization of an inositol 1,4,5-trisphosphate receptor, P400, in neural tissue: Studies in developing and adult mouse brain
    • Nakanishi, S., Maeda, N. & Mikoshiba, K. Immunohistochemical localization of an inositol 1,4,5-trisphosphate receptor, P400, in neural tissue: studies in developing and adult mouse brain. J. Neurosci. 11, 2075-2086 (1991).
    • (1991) J. Neurosci. , vol.11 , pp. 2075-2086
    • Nakanishi, S.1    Maeda, N.2    Mikoshiba, K.3
  • 34
    • 0026508615 scopus 로고
    • Three additional inositol 1,4,5-trisphosphate receptors: Molecular cloning and differential localization in brain and peripheral tissues
    • Ross, C. A., Danoff, S. K., Schell, M. J., Snyder, S. H. & Ullrich, A. Three additional inositol 1,4,5-trisphosphate receptors: molecular cloning and differential localization in brain and peripheral tissues. Proc. Natl. Acad. Sci. USA 89, 4265-4269 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4265-4269
    • Ross, C.A.1    Danoff, S.K.2    Schell, M.J.3    Snyder, S.H.4    Ullrich, A.5
  • 35
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge, M. J. Neuronal calcium signaling. Neuron 21, 13-26 (1998).
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 38
    • 0029978806 scopus 로고    scopus 로고
    • Chemical biology of protein isoprenylation/methylation
    • Rando, R. R. Chemical biology of protein isoprenylation/methylation. Biochim. Biophys. Acta 1300, 5-16 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 5-16
    • Rando, R.R.1
  • 39
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61, 355-386 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 40
    • 0027363447 scopus 로고
    • Modification of eukaryotic signaling proteins by C-terminal methylation reactions
    • Hrycyna, C. A. & Clarke, S. Modification of eukaryotic signaling proteins by C-terminal methylation reactions. Pharmacol. Ther. 59, 281-300 (1993).
    • (1993) Pharmacol. Ther. , vol.59 , pp. 281-300
    • Hrycyna, C.A.1    Clarke, S.2
  • 41
    • 0033538559 scopus 로고    scopus 로고
    • Endomembrane trafficking of ras: The CAAX motif targets proteins to the ER and Golgi
    • Choy, E. et al. Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi. Cell 98, 69-80 (1999).
    • (1999) Cell , vol.98 , pp. 69-80
    • Choy, E.1
  • 42
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C. J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154 (1998).
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1
  • 43
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21 (1994).
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 44
    • 0032404015 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR
    • Masuyama, H. & MacDonald, P. N. Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR. J. Cell. Biochem. 71, 429-440 (1998).
    • (1998) J. Cell. Biochem. , vol.71 , pp. 429-440
    • Masuyama, H.1    MacDonald, P.N.2
  • 46
    • 0032526024 scopus 로고    scopus 로고
    • Proteasomal regulation of nuclear receptor corepressor-mediated repression
    • Zhang, J., Guenther, M. G., Carthew, R. W. & Lazar, M. A. Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev. 12, 1775-1780 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1775-1780
    • Zhang, J.1    Guenther, M.G.2    Carthew, R.W.3    Lazar, M.A.4
  • 47
    • 0033053037 scopus 로고    scopus 로고
    • Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling
    • Doucas, V., Tini, M., Egan, D. A. & Evans, R. M. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc. Natl. Acad. Sci. USA 96, 2627-2632 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2627-2632
    • Doucas, V.1    Tini, M.2    Egan, D.A.3    Evans, R.M.4


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