메뉴 건너뛰기




Volumn 50, Issue 1, 1998, Pages 106-113

Reduced immunoreactivity to calcium-binding proteins in Purkinje cells precedes onset of ataxia in spinocerebellar ataxia-1 transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

CALBINDIN; CALCIUM BINDING PROTEIN; PARVALBUMIN;

EID: 0031883824     PISSN: 00283878     EISSN: None     Source Type: Journal    
DOI: 10.1212/WNL.50.1.106     Document Type: Article
Times cited : (62)

References (48)
  • 2
    • 0024435285 scopus 로고
    • Regulation of neuronal function by calcium
    • Kennedy MB. Regulation of neuronal function by calcium. Trends Neurosci 1989;12:417-419.
    • (1989) Trends Neurosci , vol.12 , pp. 417-419
    • Kennedy, M.B.1
  • 3
    • 0019996075 scopus 로고
    • Calmodulin
    • Cheung WY. Calmodulin. Sci Am 1982;246:62-70.
    • (1982) Sci Am , vol.246 , pp. 62-70
    • Cheung, W.Y.1
  • 4
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sites than insights
    • Heizmann CW, Hunziker W. Intracellular calcium-binding proteins: more sites than insights. Trends Biochem Sci 1991; 16:98-103.
    • (1991) Trends Biochem Sci , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 5
    • 0023285939 scopus 로고
    • 2+-binding proteins in normal and tumor cells: A topical review
    • 2+-binding proteins in normal and tumor cells: a topical review. Cell Calcium 1987;8:1-41.
    • (1987) Cell Calcium , vol.8 , pp. 1-41
    • Heizmann, C.W.1    Berchtold, M.W.2
  • 6
    • 0023085981 scopus 로고
    • Immunolocalization of parvalbumin
    • Helzmann CW, Celio MR. Immunolocalization of parvalbumin. Methods Enzymol 1987;139:552-570.
    • (1987) Methods Enzymol , vol.139 , pp. 552-570
    • Helzmann, C.W.1    Celio, M.R.2
  • 7
    • 0030042570 scopus 로고    scopus 로고
    • Coexistence of parvalbumin and GABA in nonpyramidal neurons of the rat entorhinal cortex
    • Meittinen M, Kovisto E, Riekkinen P, Miettinen R. Coexistence of parvalbumin and GABA in nonpyramidal neurons of the rat entorhinal cortex. Brain Res 1996;706:113-122.
    • (1996) Brain Res , vol.706 , pp. 113-122
    • Meittinen, M.1    Kovisto, E.2    Riekkinen, P.3    Miettinen, R.4
  • 8
    • 0026035290 scopus 로고
    • Parvalbumin immunoreactive neurons in human central nervous system are decreased in Alzheimer's disease
    • Berl
    • Satoh J, Tabira T, Sano M, Nakayama H, Tateishi J. Parvalbumin immunoreactive neurons in human central nervous system are decreased in Alzheimer's disease. Acta Neuropathol (Berl) 1991;81:388-395.
    • (1991) Acta Neuropathol , vol.81 , pp. 388-395
    • Satoh, J.1    Tabira, T.2    Sano, M.3    Nakayama, H.4    Tateishi, J.5
  • 9
    • 0026530110 scopus 로고
    • 2+-binding proteins in human neurodegenerative disorders
    • 2+-binding proteins in human neurodegenerative disorders. Trends Neurosci 1992; 15:303-308.
    • (1992) Trends Neurosci , vol.15 , pp. 303-308
    • Heizmann, C.W.1    Braun, K.2
  • 11
    • 0026264820 scopus 로고
    • Effect of parvalbumin and S-100 protein on protein synthesis in rabbit reticulocyte lysate
    • Cheema IR, Western L, Wadley AM. Effect of parvalbumin and S-100 protein on protein synthesis in rabbit reticulocyte lysate. Cytobios 1991;68:77-83.
    • (1991) Cytobios , vol.68 , pp. 77-83
    • Cheema, I.R.1    Western, L.2    Wadley, A.M.3
  • 12
    • 0029150909 scopus 로고
    • Changes in shape and motility of cells transfected with parvalbumin cDNA
    • Andressen C, Gotzos V, Berchtold MW, et al. Changes in shape and motility of cells transfected with parvalbumin cDNA. Exp Cell Res 1995;219:420-426.
    • (1995) Exp Cell Res , vol.219 , pp. 420-426
    • Andressen, C.1    Gotzos, V.2    Berchtold, M.W.3
  • 13
  • 14
    • 0025273543 scopus 로고
    • 2+ influx in cultured hippocampal neurons
    • 2+ influx in cultured hippocampal neurons. Neuron 1990;2:105-117.
    • (1990) Neuron , vol.2 , pp. 105-117
    • Mattson, M.P.1
  • 15
    • 0026069449 scopus 로고
    • Evidence for calcium-reducing and excitoprotective roles for the calcium binding protein calbindin-D28k in cultured hippocampal neurons
    • Mattson MP, Rychlik B, Chu C, Christakos S. Evidence for calcium-reducing and excitoprotective roles for the calcium binding protein calbindin-D28k in cultured hippocampal neurons. Neuron 1991;6:41-51.
    • (1991) Neuron , vol.6 , pp. 41-51
    • Mattson, M.P.1    Rychlik, B.2    Chu, C.3    Christakos, S.4
  • 16
    • 0024854985 scopus 로고
    • 2+-binding systems and neuronal aging
    • 2+-binding systems and neuronal aging. Ann NY Acad Sci 1989;568:89-94.
    • (1989) Ann NY Acad Sci , vol.568 , pp. 89-94
    • Michaelis, M.L.1
  • 18
    • 0023219060 scopus 로고
    • Excitotoxicity and the NMDA receptor
    • Rothman SM, Olney JW. Excitotoxicity and the NMDA receptor. Trends Neurosci 1987;10:299-302.
    • (1987) Trends Neurosci , vol.10 , pp. 299-302
    • Rothman, S.M.1    Olney, J.W.2
  • 19
    • 0024093449 scopus 로고
    • Glutamate neurotoxicity and diseases of the nervous system
    • Choi D. Glutamate neurotoxicity and diseases of the nervous system. Neuron 1988;1:623-634.
    • (1988) Neuron , vol.1 , pp. 623-634
    • Choi, D.1
  • 20
    • 0024363137 scopus 로고
    • Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage
    • Siman R, Noszek JC, Kegerise C. Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage. J Neurosci 1989;9:1579-1590.
    • (1989) J Neurosci , vol.9 , pp. 1579-1590
    • Siman, R.1    Noszek, J.C.2    Kegerise, C.3
  • 21
    • 0029665882 scopus 로고    scopus 로고
    • Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated cytotoxicity
    • Ho BK, Alexianu ME, Colom LV, Mohamed AH, Serrano F, Appel SH. Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated cytotoxicity. Natl Acad Sci USA 1996;93:6796-6801.
    • (1996) Natl Acad Sci USA , vol.93 , pp. 6796-6801
    • Ho, B.K.1    Alexianu, M.E.2    Colom, L.V.3    Mohamed, A.H.4    Serrano, F.5    Appel, S.H.6
  • 22
    • 0028958969 scopus 로고
    • Calbindin-D28k immunoreactivity in the cerebellum of spinocerebellar degeneration
    • Ishikawa K, Mizusawa H, Fujita T. Calbindin-D28k immunoreactivity in the cerebellum of spinocerebellar degeneration. J Neurol Sci 1995;129:179-185.
    • (1995) J Neurol Sci , vol.129 , pp. 179-185
    • Ishikawa, K.1    Mizusawa, H.2    Fujita, T.3
  • 23
    • 0030056030 scopus 로고    scopus 로고
    • Decreased parvalbumin immunoreactivity in surviving Purkinje's cells of patients with spinocerebellar ataxia-1
    • Vig PJS, Fratkin JD, Desaiah D, Currier RD, Subramony SH. Decreased parvalbumin immunoreactivity in surviving Purkinje's cells of patients with spinocerebellar ataxia-1. Neurology 1996;47:249-253.
    • (1996) Neurology , vol.47 , pp. 249-253
    • Vig, P.J.S.1    Fratkin, J.D.2    Desaiah, D.3    Currier, R.D.4    Subramony, S.H.5
  • 24
    • 0031012399 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the α1A-voltage-dependent calcium channel
    • Zhuchenko O, Bailey J, Bonncn P, et al. Autosomal dominant cerebellar ataxia (SCA6) associated with small polyglutamine expansions in the α1A-voltage-dependent calcium channel. Nat Genet 1997;15:62-69.
    • (1997) Nat Genet , vol.15 , pp. 62-69
    • Zhuchenko, O.1    Bailey, J.2    Bonncn, P.3
  • 25
    • 0029245258 scopus 로고
    • Spinocerebellar ataxia type 1
    • Zoghbi HY, Orr HT. Spinocerebellar ataxia type 1. Semin Cell Biol 1995;6:29-35.
    • (1995) Semin Cell Biol , vol.6 , pp. 29-35
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 26
    • 0027164698 scopus 로고
    • Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
    • Orr HT, Chung M-Y, Bonfi S, et al. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. Nat Genet 1993;4:221-226.
    • (1993) Nat Genet , vol.4 , pp. 221-226
    • Orr, H.T.1    Chung, M.-Y.2    Bonfi, S.3
  • 27
    • 0029968460 scopus 로고    scopus 로고
    • Trinucleotide repeats in neurogenetic disorders
    • Paulson HL, Fishbeck KH. Trinucleotide repeats in neurogenetic disorders. Annu Rev Neurosci 1996;19:79-107.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 79-107
    • Paulson, H.L.1    Fishbeck, K.H.2
  • 28
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers. Their possible role in inherited neurodegenerative diseases
    • Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers. Their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 1994;91:5355-5358.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 29
    • 0029163222 scopus 로고
    • SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat
    • Burright EN, Clark HB, Servadio A, et al. SCA1 transgenic mice: a model for neurodegeneration caused by an expanded CAG trinucleotide repeat. Cell 1995;82:937-948.
    • (1995) Cell , vol.82 , pp. 937-948
    • Burright, E.N.1    Clark, H.B.2    Servadio, A.3
  • 30
    • 0029074494 scopus 로고
    • Distribution of calretinin, calbindin D28k, and parvalbumin in subcellular fractions of rat cerebellum: Effect of calcium
    • Winsky L, Kuznicki J. Distribution of calretinin, calbindin D28k, and parvalbumin in subcellular fractions of rat cerebellum: effect of calcium. J Neurochem 1995;65:381-388.
    • (1995) J Neurochem , vol.65 , pp. 381-388
    • Winsky, L.1    Kuznicki, J.2
  • 31
    • 0030059870 scopus 로고    scopus 로고
    • Antibody recognition of calcium-binding proteins depends on their calcium-binding status
    • Winsky L, Kuznicki J. Antibody recognition of calcium-binding proteins depends on their calcium-binding status. J Neurochem 1996;66:764-770.
    • (1996) J Neurochem , vol.66 , pp. 764-770
    • Winsky, L.1    Kuznicki, J.2
  • 32
    • 0025635675 scopus 로고
    • Short-term changes of parvalbumin and calbindin immunoreactivity in the rat hippocampus following cerebral ischemia
    • Johansen FF, Tonder N, Zimmer J, Baimbridge KG, Diemer NH. Short-term changes of parvalbumin and calbindin immunoreactivity in the rat hippocampus following cerebral ischemia. Neurosci Lett 1990;120:171-174.
    • (1990) Neurosci Lett , vol.120 , pp. 171-174
    • Johansen, F.F.1    Tonder, N.2    Zimmer, J.3    Baimbridge, K.G.4    Diemer, N.H.5
  • 34
    • 0027988121 scopus 로고
    • Parvalbumin immunohistochemistry in denervated skeletal muscle
    • Olive M, Ferrer I. Parvalbumin immunohistochemistry in denervated skeletal muscle. Neuropathol Appl Neurobiol 1994;20(5):495-500.
    • (1994) Neuropathol Appl Neurobiol , vol.20 , Issue.5 , pp. 495-500
    • Olive, M.1    Ferrer, I.2
  • 35
    • 0025875466 scopus 로고
    • Calcium binding proteins calbindin (28k) and parvalbumin immunocytochemistry in the normal and epileptic human hippocampus
    • Sloviter RS, Sollas AL, Barbaro NM, Laxer DK. Calcium binding proteins calbindin (28k) and parvalbumin immunocytochemistry in the normal and epileptic human hippocampus. J Comp Neurol 1991;308:381-391.
    • (1991) J Comp Neurol , vol.308 , pp. 381-391
    • Sloviter, R.S.1    Sollas, A.L.2    Barbaro, N.M.3    Laxer, D.K.4
  • 36
    • 0027131842 scopus 로고
    • Selective loss of calbindin D28k-immunoreactive neurons in the cortical layer II in brains of Alzheimer's disease: A morphometric study
    • Nishiyama E, Ohwade J, Iwamoto N, Arai H. Selective loss of calbindin D28k-immunoreactive neurons in the cortical layer II in brains of Alzheimer's disease: a morphometric study. Neurosci Lett 1993;163:223-226.
    • (1993) Neurosci Lett , vol.163 , pp. 223-226
    • Nishiyama, E.1    Ohwade, J.2    Iwamoto, N.3    Arai, H.4
  • 37
    • 0025358695 scopus 로고
    • Specific reduction of calcium binding protein (28-kilodalton calbindin-D) gene expression in aging and neurodegenerative diseases
    • Iacopino AM, Christakos S. Specific reduction of calcium binding protein (28-kilodalton calbindin-D) gene expression in aging and neurodegenerative diseases. Proc Natl Acad Sci USA 1990;87:4078-4082.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4078-4082
    • Iacopino, A.M.1    Christakos, S.2
  • 38
    • 0345539671 scopus 로고
    • Differential gene expression in ALS-sensitive and ALS-resistant motor neurons
    • Elliott J, Snider W. Differential gene expression in ALS-sensitive and ALS-resistant motor neurons [abstract]. Neurology 1995;45(suppl 4):305.
    • (1995) Neurology , vol.45 , Issue.4 SUPPL. , pp. 305
    • Elliott, J.1    Snider, W.2
  • 39
    • 0031019589 scopus 로고    scopus 로고
    • Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of calbindin D28k gene
    • Airaksinen MS, Eilers J, Garaschuk O, Thoenen H, Konnerth R, Meyer M. Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of calbindin D28k gene. Proc Natl Acad Sci USA 1997;94:1488-1493.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1488-1493
    • Airaksinen, M.S.1    Eilers, J.2    Garaschuk, O.3    Thoenen, H.4    Konnerth, R.5    Meyer, M.6
  • 40
    • 0028977967 scopus 로고
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons. Nature (London) 1995;373:155-158.
    • (1995) Nature (London) , vol.373 , pp. 155-158
    • Eilers, J.1    Augustine, G.J.2    Konnerth, A.3
  • 41
    • 0002113815 scopus 로고
    • Patch-clamp and calcium imaging in brain slices
    • Sakmann B, Neher E, eds. New York: Plenum
    • Eilers J, Schneggenburger R, Konneth A. Patch-clamp and calcium imaging in brain slices. In: Sakmann B, Neher E, eds. Single channel recordings. New York: Plenum, 1995:213-229.
    • (1995) Single Channel Recordings , pp. 213-229
    • Eilers, J.1    Schneggenburger, R.2    Konneth, A.3
  • 42
    • 0018910557 scopus 로고
    • Electrophysiological properties of in vitro Purkinje cell dendrites in mammalian cerebellar slices
    • Llinas R, Sugimori M. Electrophysiological properties of in vitro Purkinje cell dendrites in mammalian cerebellar slices. J Physiol 1980;305:197-213.
    • (1980) J Physiol , vol.305 , pp. 197-213
    • Llinas, R.1    Sugimori, M.2
  • 43
    • 0024535231 scopus 로고
    • Synaptic control of excitability in turtle cerebellar Purkinje cells
    • Hounsgaard J, Midtgaard J. Synaptic control of excitability in turtle cerebellar Purkinje cells. J Physiol 1989;409:157-170.
    • (1989) J Physiol , vol.409 , pp. 157-170
    • Hounsgaard, J.1    Midtgaard, J.2
  • 44
    • 0025923797 scopus 로고
    • Calbindin-D28k (CaBP) levels and calcium currents in acutely dissociated epileptic neurons
    • Kohr G, Lambert CE, Mody I. Calbindin-D28k (CaBP) levels and calcium currents in acutely dissociated epileptic neurons. Exp Brain Res 1991;85:543-551.
    • (1991) Exp Brain Res , vol.85 , pp. 543-551
    • Kohr, G.1    Lambert, C.E.2    Mody, I.3
  • 45
    • 0026660055 scopus 로고
    • Brief dendritic calcium signals initiate long-lasting synaptic depression in cerebellar Purkinje cells
    • Konnerth A, Dreessen J, Augustine GJ. Brief dendritic calcium signals initiate long-lasting synaptic depression in cerebellar Purkinje cells. Proc Natl Acad Sci USA 1992;89: 7051-7055.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7051-7055
    • Konnerth, A.1    Dreessen, J.2    Augustine, G.J.3
  • 46
    • 0026526070 scopus 로고
    • Synaptic excitation produces a long-lasting rebound potentiation of inhibitory synaptic signals in cerebellar Purkinje cells
    • Kano M, Rexhausen U, Dreesen J, Konnerth A. Synaptic excitation produces a long-lasting rebound potentiation of inhibitory synaptic signals in cerebellar Purkinje cells. Nature (London) 1992;356:601-604.
    • (1992) Nature (London) , vol.356 , pp. 601-604
    • Kano, M.1    Rexhausen, U.2    Dreesen, J.3    Konnerth, A.4
  • 48
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B, Matilla T, Burright EN, et al. Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Hum Mol Genet 1996;5:1311-1318.
    • (1996) Hum Mol Genet , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.