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Volumn 37, Issue 5, 2004, Pages 643-653

Aberrant neuronal and mitochondrial proteins in hippocampus of transgenic mice overexpressing human Cu/Zn superoxide dismutase 1

Author keywords

2 DE; ATP; ATP synthase; Cu Zn superoxide dismutase 1; Down syndrome; DS; DYN1; dynamin 1; EFTU; Free radicals; Hippocampus; Mitochondrial protein; Neuronal proteins; Transgenic mice; Two dimensional gel electrophoresis; two dimensional gel electrophoresis

Indexed keywords

BRAIN PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; DYNAMIN I; ELONGATION FACTOR TU; MITOCHONDRIAL PROTEIN; N ETHYLMALEIMIDE; NEUROFILAMENT PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; TROPOMODULIN;

EID: 3342931462     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.05.019     Document Type: Article
Times cited : (39)

References (40)
  • 1
    • 0022271547 scopus 로고
    • Molecular structure and expression of the gene locus on chromosome 21 encoding the Cu/Zn superoxide dismutase and its relevance to Down syndrome
    • Groner Y., Lieman-Hurwitz J., Dafni N., Sherman L., Levanon D., Bernstein Y., Danciger E., Elroy-Stein O. Molecular structure and expression of the gene locus on chromosome 21 encoding the Cu/Zn superoxide dismutase and its relevance to Down syndrome. Ann. NY Acad. Sci. 450:1985;133-156
    • (1985) Ann. NY Acad. Sci. , vol.450 , pp. 133-156
    • Groner, Y.1    Lieman-Hurwitz, J.2    Dafni, N.3    Sherman, L.4    Levanon, D.5    Bernstein, Y.6    Danciger, E.7    Elroy-Stein, O.8
  • 2
    • 0035144524 scopus 로고    scopus 로고
    • Superoxide dismutase SOD1, encoded on chromosome 21, but not SOD2 is overexpressed in brains patients with Down syndrome
    • Gulesserian T., Seidl R., Hardmeier R., Cairns N., Lubec G. Superoxide dismutase SOD1, encoded on chromosome 21, but not SOD2 is overexpressed in brains patients with Down syndrome. J. Invest. Med. 49:2001;41-46
    • (2001) J. Invest. Med. , vol.49 , pp. 41-46
    • Gulesserian, T.1    Seidl, R.2    Hardmeier, R.3    Cairns, N.4    Lubec, G.5
  • 4
    • 0026096819 scopus 로고
    • Down's syndrome: Morphological remodelling and increased complexity in the neuromuscular junction of transgenic CuZn-superoxide dismutase mice
    • Avraham K.B., Sugarman H., Rotshenker S., Groner Y. Down's syndrome: morphological remodelling and increased complexity in the neuromuscular junction of transgenic CuZn-superoxide dismutase mice. J. Neurocytol. 20:1991;208-215
    • (1991) J. Neurocytol. , vol.20 , pp. 208-215
    • Avraham, K.B.1    Sugarman, H.2    Rotshenker, S.3    Groner, Y.4
  • 5
    • 0031865781 scopus 로고    scopus 로고
    • Reversible impairment of long-term potentiation in transgenic Cu/Zn-SOD mice
    • Gahtan E., Auerbach J.M., Groner Y., Segal M. Reversible impairment of long-term potentiation in transgenic Cu/Zn-SOD mice. Eur. J. Neurosci. 10:1998;538-544
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 538-544
    • Gahtan, E.1    Auerbach, J.M.2    Groner, Y.3    Segal, M.4
  • 6
    • 0029983348 scopus 로고    scopus 로고
    • Transgenic mice overexpressing the human Cu/Zn-SOD gene: Ultrastructural studies of a premature thymic involution model of Down's syndrome (trisomy 21)
    • Nabarra B., Casanova M., Paris D., Nicole A., Toyama K., Sinet P.M., Ceballos I., London J. Transgenic mice overexpressing the human Cu/Zn-SOD gene: ultrastructural studies of a premature thymic involution model of Down's syndrome (trisomy 21). Lab. Invest. 74:1996;617-626
    • (1996) Lab. Invest. , vol.74 , pp. 617-626
    • Nabarra, B.1    Casanova, M.2    Paris, D.3    Nicole, A.4    Toyama, K.5    Sinet, P.M.6    Ceballos, I.7    London, J.8
  • 7
    • 0024366919 scopus 로고
    • Diminished serotonin uptake in platelets of transgenic mice with increased Cu/Zn-superoxide dismutase activity
    • Schickler M., Knobler H., Avraham K.B., Elroy-Stein O., Groner Y. Diminished serotonin uptake in platelets of transgenic mice with increased Cu/Zn-superoxide dismutase activity. EMBO J. 8:1989;1385-1392
    • (1989) EMBO J. , vol.8 , pp. 1385-1392
    • Schickler, M.1    Knobler, H.2    Avraham, K.B.3    Elroy-Stein, O.4    Groner, Y.5
  • 8
    • 0034520591 scopus 로고    scopus 로고
    • Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1
    • Jaarsma D., Haasdijk E.D., Grashorn J.A., Hawkins R., van Duijn W., Verspaget H.W., London J., Holstege J.C. Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1. Neurobiol. Dis. 7:2000;623-643
    • (2000) Neurobiol. Dis. , vol.7 , pp. 623-643
    • Jaarsma, D.1    Haasdijk, E.D.2    Grashorn, J.A.3    Hawkins, R.4    Van Duijn, W.5    Verspaget, H.W.6    London, J.7    Holstege, J.C.8
  • 9
    • 0030297843 scopus 로고    scopus 로고
    • Rapid fluorescence in situ hybridization on interphasic nuclei to discriminate between homozygous and heterozygous transgenic mice
    • Paris D., Toyama K., Mégarbané A., Casanova M., Sinet P.M., London J. Rapid fluorescence in situ hybridization on interphasic nuclei to discriminate between homozygous and heterozygous transgenic mice. Transgenic Res. 5:1996;397-403
    • (1996) Transgenic Res. , vol.5 , pp. 397-403
    • Paris, D.1    Toyama, K.2    Mégarbané, A.3    Casanova, M.4    Sinet, P.M.5    London, J.6
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 344:1976;125-132
    • (1976) Anal. Biochem. , vol.344 , pp. 125-132
    • Bradford, M.1
  • 11
    • 0036288814 scopus 로고    scopus 로고
    • Reduction of actin-related protein complex 2/3 in fetal Down syndrome brain
    • Weitzdoerfer R., Fountoulakis M., Lubec G. Reduction of actin-related protein complex 2/3 in fetal Down syndrome brain. Biochem. Biophys. Res. Commun. 293:2002;836-841
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 836-841
    • Weitzdoerfer, R.1    Fountoulakis, M.2    Lubec, G.3
  • 14
    • 0027423414 scopus 로고
    • Membrane fusion machinery: Insights from synaptic proteins
    • Sudhof T.C., De Camilli P., Niemann H., Jahn R. Membrane fusion machinery: insights from synaptic proteins. Cell. 75:1993;1-4
    • (1993) Cell , vol.75 , pp. 1-4
    • Sudhof, T.C.1    De Camilli, P.2    Niemann, H.3    Jahn, R.4
  • 15
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett M.K., Scheller R.H. The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA. 90:1993;2559-2563
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 17
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble W.S., Cowan D.M., Scheller R.H. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Natl. Acad. Sci. USA. 85:1988;4538-4542
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 18
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert M., Maycox P.R., Navone F., De Camilli P., Jahn R. Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J. 8:1989;379-384
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 19
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett M.K., Calakos N., Scheller R.H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science. 257:1992;255-259
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 20
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M., Bloom F.E., Wilson M.C. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109:1989;3039-3052
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 21
    • 0036673069 scopus 로고    scopus 로고
    • SNAREs and Munc18 in synaptic vesicle fusion
    • Rizo J., Südhof T.C. SNAREs and Munc18 in synaptic vesicle fusion. Nat. Rev. 3:2002;641-653
    • (2002) Nat. Rev. , vol.3 , pp. 641-653
    • Rizo, J.1    Südhof, T.C.2
  • 22
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
    • Hanson P.I., Otto H., Barton N., Jahn R. The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270:1995;16955-16961
    • (1995) J. Biol. Chem. , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 24
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura K.M., Scheller R.H., Weis W.I. Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature. 404:2000;355-362
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 28
    • 0026634688 scopus 로고
    • The neurofilament triplet is present in distinct subpopulations of neurons in the central nervous system of the guinea-pig
    • Vickers J.C., Costa M. The neurofilament triplet is present in distinct subpopulations of neurons in the central nervous system of the guinea-pig. Neuroscience. 49:1992;73-100
    • (1992) Neuroscience , vol.49 , pp. 73-100
    • Vickers, J.C.1    Costa, M.2
  • 29
    • 0034751077 scopus 로고    scopus 로고
    • Neurofilament proteins NF-L, NF-M and NF-H in brain of patients with Down syndrome and Alzheimer's disease
    • Bajo M., Yoo B.C., Cairns N., Gratzer M., Lubec G. Neurofilament proteins NF-L, NF-M and NF-H in brain of patients with Down syndrome and Alzheimer's disease. Amino Acids. 21:2001;293-301
    • (2001) Amino Acids , vol.21 , pp. 293-301
    • Bajo, M.1    Yoo, B.C.2    Cairns, N.3    Gratzer, M.4    Lubec, G.5
  • 31
    • 0141455220 scopus 로고    scopus 로고
    • Parallel compensatory and pathological events associated with tau pathology in middle aged individuals with Down syndrome
    • Head E., Lott I.T., Hof P.R., Bouras C., Su J.H., Kim R., Haier R., Cotman C.W. Parallel compensatory and pathological events associated with tau pathology in middle aged individuals with Down syndrome. J. Neuropathol. Exp. Neurol. 62:2003;917-926
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 917-926
    • Head, E.1    Lott, I.T.2    Hof, P.R.3    Bouras, C.4    Su, J.H.5    Kim, R.6    Haier, R.7    Cotman, C.W.8
  • 32
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio J., Yankner B.A. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature. 378:1995;776-779
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 34
    • 0037339732 scopus 로고    scopus 로고
    • Molecular changes in fetal Down syndrome brain
    • Engidawork E., Lubec G. Molecular changes in fetal Down syndrome brain. J. Neurochem. 84:2003;895-904
    • (2003) J. Neurochem. , vol.84 , pp. 895-904
    • Engidawork, E.1    Lubec, G.2
  • 35
    • 0035226716 scopus 로고    scopus 로고
    • Fetal life in Down syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure
    • Weitzdoerfer R., Dierssen M., Fountoulakis M., Lubec G. Fetal life in Down syndrome starts with normal neuronal density but impaired dendritic spines and synaptosomal structure. J. Neural. Transm. Suppl. 61:2001;59-70
    • (2001) J. Neural. Transm. Suppl. , vol.61 , pp. 59-70
    • Weitzdoerfer, R.1    Dierssen, M.2    Fountoulakis, M.3    Lubec, G.4
  • 36
    • 0032947530 scopus 로고    scopus 로고
    • Decreased levels of synaptosomal associated protein 25 in the brain of patients with Down syndrome and Alzheimer's disease
    • Greber S., Lubec G., Cairns N., Fountoulakis M. Decreased levels of synaptosomal associated protein 25 in the brain of patients with Down syndrome and Alzheimer's disease. Electrophoresis. 20:1999;928-934
    • (1999) Electrophoresis , vol.20 , pp. 928-934
    • Greber, S.1    Lubec, G.2    Cairns, N.3    Fountoulakis, M.4
  • 37
    • 0035233817 scopus 로고    scopus 로고
    • Decreased protein levels of complex I 30-kDa subunit in fetal Down syndrome brains
    • Kim S.H., Fountoulakis M., Dierssen M., Lubec G. Decreased protein levels of complex I 30-kDa subunit in fetal Down syndrome brains. J. Neural. Transm. Suppl. 61:2001;109-116
    • (2001) J. Neural. Transm. Suppl. , vol.61 , pp. 109-116
    • Kim, S.H.1    Fountoulakis, M.2    Dierssen, M.3    Lubec, G.4
  • 38
    • 0035805113 scopus 로고    scopus 로고
    • The reduction of NADH ubiquinone oxidoreductase 24- and 75-kDa subunits in brains of patients with Down syndrome and Alzheimer's disease
    • Kim S.H., Vlkolinsky R., Cairns N., Fountoulakis M., Lubec G. The reduction of NADH ubiquinone oxidoreductase 24- and 75-kDa subunits in brains of patients with Down syndrome and Alzheimer's disease. Life Sci. 68:2001;2741-2750
    • (2001) Life Sci. , vol.68 , pp. 2741-2750
    • Kim, S.H.1    Vlkolinsky, R.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 39
    • 12244291012 scopus 로고    scopus 로고
    • Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step
    • Chotiner J.K., Khorasani H., Nairn A.C., O'Dell T.J., Watson J.B. Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step. Neuroscience. 116:2003;743-752
    • (2003) Neuroscience , vol.116 , pp. 743-752
    • Chotiner, J.K.1    Khorasani, H.2    Nairn, A.C.3    O'Dell, T.J.4    Watson, J.B.5
  • 40
    • 0035232099 scopus 로고    scopus 로고
    • Deterioration of the transcriptional, splicing and elongation machinery in brain of fetal Down syndrome
    • Freidl M., Gulesserian T., Lubec G., Fountoulakis M., Lubec B. Deterioration of the transcriptional, splicing and elongation machinery in brain of fetal Down syndrome. J. Neural. Transm. Suppl. 61:2001;47-57
    • (2001) J. Neural. Transm. Suppl. , vol.61 , pp. 47-57
    • Freidl, M.1    Gulesserian, T.2    Lubec, G.3    Fountoulakis, M.4    Lubec, B.5


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