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Volumn 199, Issue 2, 2006, Pages 281-290

Cerebral neurons of transgenic ALS mice are vulnerable to glutamate release stimulation but not to increased extracellular glutamate due to transport blockade

Author keywords

Amyotrophic lateral sclerosis; Excitotoxicity; G93A mice; Glutamate; Hippocampus; HSP70; Microdialysis; Motor cortex

Indexed keywords

2,4 PYRROLIDINEDICARBOXYLIC ACID; 4 AMINOPYRIDINE; BIOLOGICAL MARKER; COPPER ZINC SUPEROXIDE DISMUTASE; DIZOCILPINE; GLUTAMIC ACID; HEAT SHOCK PROTEIN 70; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT;

EID: 33745270015     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2005.11.005     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0034099564 scopus 로고    scopus 로고
    • Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase
    • Alexander G.M., Deitch J.S., Seeburger J.L., Del Valle L., and Heiman-Patterson T.D. Elevated cortical extracellular fluid glutamate in transgenic mice expressing human mutant (G93A) Cu/Zn superoxide dismutase. J. Neurochem. 74 (2000) 1666-1673
    • (2000) J. Neurochem. , vol.74 , pp. 1666-1673
    • Alexander, G.M.1    Deitch, J.S.2    Seeburger, J.L.3    Del Valle, L.4    Heiman-Patterson, T.D.5
  • 2
    • 0035051503 scopus 로고    scopus 로고
    • Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation
    • Andreassen O.A., Jenkins B.G., Dedeoglu A., Ferrante K.L., Bogdanov M.B., Kaddurah-Daouk R., and Beal M.F. Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation. J. Neurochem. 77 (2001) 383-390
    • (2001) J. Neurochem. , vol.77 , pp. 383-390
    • Andreassen, O.A.1    Jenkins, B.G.2    Dedeoglu, A.3    Ferrante, K.L.4    Bogdanov, M.B.5    Kaddurah-Daouk, R.6    Beal, M.F.7
  • 3
    • 0043073214 scopus 로고    scopus 로고
    • Expression of heat shock protein 70 induced by 4-aminopyridine through glutamate-mediated excitotoxic stress in rat hippocampus in vivo
    • Ayala G.X., and Tapia R. Expression of heat shock protein 70 induced by 4-aminopyridine through glutamate-mediated excitotoxic stress in rat hippocampus in vivo. Neuropharmacology 45 (2003) 649-660
    • (2003) Neuropharmacology , vol.45 , pp. 649-660
    • Ayala, G.X.1    Tapia, R.2
  • 4
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal M.F. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 23 (2000) 298-304
    • (2000) Trends Neurosci. , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 6
    • 0029584941 scopus 로고
    • Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function
    • Brown Jr. R.H. Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function. Curr. Opin. Neurobiol. 5 (1995) 841-846
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 841-846
    • Brown Jr., R.H.1
  • 7
    • 0033231494 scopus 로고    scopus 로고
    • From Charcot to SOD1: mechanisms of selective motor neuron death in ALS
    • Cleveland D.W. From Charcot to SOD1: mechanisms of selective motor neuron death in ALS. Neuron 24 (1999) 515-520
    • (1999) Neuron , vol.24 , pp. 515-520
    • Cleveland, D.W.1
  • 8
    • 2542498984 scopus 로고    scopus 로고
    • AMPA receptor activation, but not the accumulation of endogenous extracellular glutamate, induces paralysis and motor neuron death in rat spinal cord in vivo
    • Corona J.C., and Tapia R. AMPA receptor activation, but not the accumulation of endogenous extracellular glutamate, induces paralysis and motor neuron death in rat spinal cord in vivo. J. Neurochem. 89 (2004) 988-997
    • (2004) J. Neurochem. , vol.89 , pp. 988-997
    • Corona, J.C.1    Tapia, R.2
  • 9
    • 0037081303 scopus 로고    scopus 로고
    • GLT-1 glutamate transporter levels are unchanged in mice expressing G93A human mutant SOD1
    • Deitch J.S., Alexander G.M., Del Valle L., and Heiman-Patterson T.D. GLT-1 glutamate transporter levels are unchanged in mice expressing G93A human mutant SOD1. J. Neurol. Sci. 193 (2002) 117-126
    • (2002) J. Neurol. Sci. , vol.193 , pp. 117-126
    • Deitch, J.S.1    Alexander, G.M.2    Del Valle, L.3    Heiman-Patterson, T.D.4
  • 10
    • 0037335463 scopus 로고    scopus 로고
    • Impaired spinal cord glutamate transport capacity and reduced sensitivity to riluzole in a transgenic superoxide dismutase mutant rat model of amyotrophic lateral sclerosis
    • Dunlop J., Beal M.H., She Y., and Howland D.S. Impaired spinal cord glutamate transport capacity and reduced sensitivity to riluzole in a transgenic superoxide dismutase mutant rat model of amyotrophic lateral sclerosis. J. Neurosci. 23 (2003) 1688-1696
    • (2003) J. Neurosci. , vol.23 , pp. 1688-1696
    • Dunlop, J.1    Beal, M.H.2    She, Y.3    Howland, D.S.4
  • 11
    • 0026726279 scopus 로고
    • NMDA receptor antagonists protect against seizures and wet-dog shakes induced by 4-aminopyridine
    • Fragoso-Veloz J., and Tapia R. NMDA receptor antagonists protect against seizures and wet-dog shakes induced by 4-aminopyridine. Eur. J. Pharmacol. 221 (1992) 275-280
    • (1992) Eur. J. Pharmacol. , vol.221 , pp. 275-280
    • Fragoso-Veloz, J.1    Tapia, R.2
  • 15
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins C.M., Jung C., Ding H., and Xu Z. Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS. J. Neurosci. 22 1-6 (2002) RC215
    • (2002) J. Neurosci. , vol.22 , Issue.1-6
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 16
    • 0038707391 scopus 로고    scopus 로고
    • Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses
    • Liochev S.I., and Fridovich I. Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses. Free Radical Biol. Med. 34 (2003) 1383-1389
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 1383-1389
    • Liochev, S.I.1    Fridovich, I.2
  • 17
    • 1642371041 scopus 로고    scopus 로고
    • Altered expression of the glutamate transporter EAAT2b in neurological disease
    • Maragakis N.J., Dykes-Hoberg M., and Rothstein J.D. Altered expression of the glutamate transporter EAAT2b in neurological disease. Ann. Neurol. 55 (2004) 469-477
    • (2004) Ann. Neurol. , vol.55 , pp. 469-477
    • Maragakis, N.J.1    Dykes-Hoberg, M.2    Rothstein, J.D.3
  • 18
    • 0030857058 scopus 로고    scopus 로고
    • Glutamate uptake impairment and neuronal damage in young and aged rats in vivo
    • Massieu L., and Tapia R. Glutamate uptake impairment and neuronal damage in young and aged rats in vivo. J. Neurochem. 69 (1997) 1151-1160
    • (1997) J. Neurochem. , vol.69 , pp. 1151-1160
    • Massieu, L.1    Tapia, R.2
  • 19
    • 0028943731 scopus 로고
    • Accumulation of extracellular glutamate by inhibition of its uptake is not sufficient for inducing neuronal damage: an in vivo microdialysis study
    • Massieu L., Morales-Villagran A., and Tapia R. Accumulation of extracellular glutamate by inhibition of its uptake is not sufficient for inducing neuronal damage: an in vivo microdialysis study. J. Neurochem. 64 (1995) 2262-2272
    • (1995) J. Neurochem. , vol.64 , pp. 2262-2272
    • Massieu, L.1    Morales-Villagran, A.2    Tapia, R.3
  • 20
    • 0029655711 scopus 로고    scopus 로고
    • Preferential stimulation of glutamate release by 4-aminopyridine in rat striatum in vivo
    • Morales-Villagran A., and Tapia R. Preferential stimulation of glutamate release by 4-aminopyridine in rat striatum in vivo. Neurochem. Int. 28 (1996) 35-40
    • (1996) Neurochem. Int. , vol.28 , pp. 35-40
    • Morales-Villagran, A.1    Tapia, R.2
  • 21
    • 0029895780 scopus 로고    scopus 로고
    • Evidence disputing the link between seizure activity and high extracellular glutamate
    • Obrenovitch T.P., Urenjak J., and Zilkha E. Evidence disputing the link between seizure activity and high extracellular glutamate. J. Neurochem. 66 (1996) 2446-2454
    • (1996) J. Neurochem. , vol.66 , pp. 2446-2454
    • Obrenovitch, T.P.1    Urenjak, J.2    Zilkha, E.3
  • 22
    • 0034665175 scopus 로고    scopus 로고
    • Roles of molecular chaperones in the nervous system
    • Ohtsuka K., and Suzuki T. Roles of molecular chaperones in the nervous system. Brain Res. Bull. 53 (2000) 141-146
    • (2000) Brain Res. Bull. , vol.53 , pp. 141-146
    • Ohtsuka, K.1    Suzuki, T.2
  • 23
    • 0344026342 scopus 로고    scopus 로고
    • Relationships among seizures, extracellular amino acid changes, and neurodegeneration induced by 4-aminopyridine in rat hippocampus: a microdialysis and electroencephalographic study
    • Peña F., and Tapia R. Relationships among seizures, extracellular amino acid changes, and neurodegeneration induced by 4-aminopyridine in rat hippocampus: a microdialysis and electroencephalographic study. J. Neurochem. 72 (1999) 2006-2014
    • (1999) J. Neurochem. , vol.72 , pp. 2006-2014
    • Peña, F.1    Tapia, R.2
  • 24
    • 0034669136 scopus 로고    scopus 로고
    • Seizures and neurodegeneration induced by 4-aminopyridine in rat hippocampus in vivo: role of glutamate- and GABA-mediated neurotransmission and of ion channels
    • Peña F., and Tapia R. Seizures and neurodegeneration induced by 4-aminopyridine in rat hippocampus in vivo: role of glutamate- and GABA-mediated neurotransmission and of ion channels. Neuroscience 101 (2000) 547-561
    • (2000) Neuroscience , vol.101 , pp. 547-561
    • Peña, F.1    Tapia, R.2
  • 25
    • 0345269737 scopus 로고    scopus 로고
    • Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons
    • Rao S.D., Yin H.Z., and Weiss J.H. Disruption of glial glutamate transport by reactive oxygen species produced in motor neurons. J. Neurosci. 23 (2003) 2627-2633
    • (2003) J. Neurosci. , vol.23 , pp. 2627-2633
    • Rao, S.D.1    Yin, H.Z.2    Weiss, J.H.3
  • 28
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • Rothstein J.D., Martin L.J., and Kuncl R.W. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N. Engl. J. Med. 326 (1992) 1464-1468
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 29
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein J.D., Van Kammen M., Levey A.I., Martin L.J., and Kuncl R.W. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Neurol. 38 (1995) 73-84
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 30
    • 0028329940 scopus 로고
    • Decrease of glutamate decarboxylase activity after in vivo cortical infusion of gamma-aminobutyric acid
    • Salazar P., Montiel T., Brailowsky S., and Tapia R. Decrease of glutamate decarboxylase activity after in vivo cortical infusion of gamma-aminobutyric acid. Neurochem. Int. 24 (1994) 363-368
    • (1994) Neurochem. Int. , vol.24 , pp. 363-368
    • Salazar, P.1    Montiel, T.2    Brailowsky, S.3    Tapia, R.4
  • 31
    • 0035947131 scopus 로고    scopus 로고
    • EAAT1 and EAAT2 immunoreactivity in transgenic mice with a G93A mutant SOD1 gene
    • Sasaki S., Warita H., Abe K., Komori T., and Iwata M. EAAT1 and EAAT2 immunoreactivity in transgenic mice with a G93A mutant SOD1 gene. NeuroReport 12 (2001) 1359-1362
    • (2001) NeuroReport , vol.12 , pp. 1359-1362
    • Sasaki, S.1    Warita, H.2    Abe, K.3    Komori, T.4    Iwata, M.5
  • 32
    • 0029067210 scopus 로고
    • CSF and plasma amino acid levels in motor neuron disease: elevation of CSF glutamate in a subset of patients
    • Shaw P.J., Forrest V., Ince P.G., Richardson J.P., and Wastell H.J. CSF and plasma amino acid levels in motor neuron disease: elevation of CSF glutamate in a subset of patients. Neurodegeneration 4 (1995) 209-216
    • (1995) Neurodegeneration , vol.4 , pp. 209-216
    • Shaw, P.J.1    Forrest, V.2    Ince, P.G.3    Richardson, J.P.4    Wastell, H.J.5
  • 33
    • 0026721889 scopus 로고
    • Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress
    • Sloviter R.S., and Lowenstein D.H. Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress. J. Neurosci. 12 (1992) 3004-3009
    • (1992) J. Neurosci. , vol.12 , pp. 3004-3009
    • Sloviter, R.S.1    Lowenstein, D.H.2
  • 34
    • 0037081113 scopus 로고    scopus 로고
    • Glutamate levels in cerebrospinal fluid in amyotrophic lateral sclerosis: a reappraisal using a new HPLC method with coulometric detection in a large cohort of patients
    • Spreux-Varoquaux O., Bensimon G., Lacomblez L., Salachas F., Pradat P.F., Le Forestier N., Marouan A., Dib M., and Meininger V. Glutamate levels in cerebrospinal fluid in amyotrophic lateral sclerosis: a reappraisal using a new HPLC method with coulometric detection in a large cohort of patients. J. Neurol. Sci. 193 (2002) 73-78
    • (2002) J. Neurol. Sci. , vol.193 , pp. 73-78
    • Spreux-Varoquaux, O.1    Bensimon, G.2    Lacomblez, L.3    Salachas, F.4    Pradat, P.F.5    Le Forestier, N.6    Marouan, A.7    Dib, M.8    Meininger, V.9
  • 35
    • 0032966046 scopus 로고    scopus 로고
    • On the relationship between extracellular glutamate, hyperexcitation and neurodegeneration, in vivo
    • Tapia R., Medina-Ceja L., and Peña F. On the relationship between extracellular glutamate, hyperexcitation and neurodegeneration, in vivo. Neurochem. Int. 34 (1999) 23-31
    • (1999) Neurochem. Int. , vol.34 , pp. 23-31
    • Tapia, R.1    Medina-Ceja, L.2    Peña, F.3
  • 36
    • 0027314311 scopus 로고
    • A comparison of induced heat-shock protein in neurons destined to survive and those destined to die after transient ischemia in rats
    • Tomioka C., Nishioka K., and Kogure K. A comparison of induced heat-shock protein in neurons destined to survive and those destined to die after transient ischemia in rats. Brain Res. 612 (1993) 216-220
    • (1993) Brain Res. , vol.612 , pp. 216-220
    • Tomioka, C.1    Nishioka, K.2    Kogure, K.3
  • 38
    • 0033366461 scopus 로고    scopus 로고
    • SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter
    • Trotti D., Rolfs A., Danbolt N.C., Brown Jr. R.H., and Hediger M.A. SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nat. Neurosci. 2 (1999) 427-433
    • (1999) Nat. Neurosci. , vol.2 , pp. 427-433
    • Trotti, D.1    Rolfs, A.2    Danbolt, N.C.3    Brown Jr., R.H.4    Hediger, M.A.5
  • 40
    • 14944385595 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice
    • Vijayvergiya C., Beal M.F., Buck J., and Manfredi G. Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci. 25 (2005) 2463-2470
    • (2005) J. Neurosci. , vol.25 , pp. 2463-2470
    • Vijayvergiya, C.1    Beal, M.F.2    Buck, J.3    Manfredi, G.4
  • 41
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra A., Trotti D., Tromba C., Floridi S., and Racagni G. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14 (1994) 2924-2932
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1    Trotti, D.2    Tromba, C.3    Floridi, S.4    Racagni, G.5
  • 42
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P.C., Pardo C.A., Borchelt D.R., Lee M.K., Copeland N.G., Jenkins N.A., Sisodia S.S., Cleveland D.W., and Price D.L. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14 (1995) 1105-1116
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.