메뉴 건너뛰기




Volumn 69, Issue 1, 2006, Pages 37-47

HSP70 induction and oxidative stress protection mediated by a subtoxic dose of NMDA in the retinoic acid-differentiated C6 glioma cell line

Author keywords

Antioxidant enzymes; C6 glioma; HSP70; NMDA; Retinoic acid

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; DIZOCILPINE; GLUTAMIC ACID; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HEAT SHOCK PROTEIN 70; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; RETINOIC ACID;

EID: 31844454669     PISSN: 03619230     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainresbull.2005.10.011     Document Type: Article
Times cited : (16)

References (63)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • L. Packer Academic Press New York
    • H. Aebi Catalase in vitro L. Packer Methods in Enzymology vol. 105 1984 Academic Press New York 121 126
    • (1984) Methods in Enzymology , vol.105 , pp. 121-126
    • Aebi, H.1
  • 4
    • 0009760791 scopus 로고    scopus 로고
    • Heat shock protein hsp70 overexpression confers resistance against nitric oxide
    • K. Bellman, M. Jaattela, D. Wissing, V. Burkart, and H. Kolb Heat shock protein hsp70 overexpression confers resistance against nitric oxide FEBS Lett. 391 1996 185 188
    • (1996) FEBS Lett. , vol.391 , pp. 185-188
    • Bellman, K.1    Jaattela, M.2    Wissing, D.3    Burkart, V.4    Kolb, H.5
  • 5
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • L. Packer Academic Press New York
    • J.A. Beuge, and A.D. Aust Microsomal lipid peroxidation L. Packer Methods in Enzymology vol. 52 1978 Academic Press New York 302 310
    • (1978) Methods in Enzymology , vol.52 , pp. 302-310
    • Beuge, J.A.1    Aust, A.D.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0034304391 scopus 로고    scopus 로고
    • NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders: Role of oxidant/antioxidant balance
    • V. Calabrese, T.E. Bates, and A.M. Stella NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders: role of oxidant/antioxidant balance Neurochem. Res. 25 2000 1315 1341
    • (2000) Neurochem. Res. , vol.25 , pp. 1315-1341
    • Calabrese, V.1    Bates, T.E.2    Stella, A.M.3
  • 8
    • 0036212575 scopus 로고    scopus 로고
    • Regional distribution of heme oxygenase, HSP70 and glutathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance
    • V. Calabrese, G. Scapagnini, A. Ravagna, R.G. Fariello, A.M.G. Stella, and N.G. Abraham Regional distribution of heme oxygenase, HSP70 and glutathione in brain: relevance for endogenous oxidant/antioxidant balance and stress tolerance J. Neurosci. Res. 68 2002 65 75
    • (2002) J. Neurosci. Res. , vol.68 , pp. 65-75
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Fariello, R.G.4    Stella, A.M.G.5    Abraham, N.G.6
  • 9
    • 0029129811 scopus 로고
    • Characterization of excitoprotective actions of N-methyl-d-aspartate in cultured cerebellar granule neurons
    • P. Damschroder-Williams, R.P. Irwin, S.Z. Lin, and S.M. Paul Characterization of excitoprotective actions of N-methyl-d-aspartate in cultured cerebellar granule neurons J. Neurochem. 65 1995 1069 1076
    • (1995) J. Neurochem. , vol.65 , pp. 1069-1076
    • Damschroder-Williams, P.1    Irwin, R.P.2    Lin, S.Z.3    Paul, S.M.4
  • 10
    • 0032974143 scopus 로고    scopus 로고
    • The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells
    • R. Dringen, L. Kussmaul, J.M. Gutterer, J. Hirrlinger, and B. Hamprecht The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells J. Neurochem. 72 1999 2523 2530
    • (1999) J. Neurochem. , vol.72 , pp. 2523-2530
    • Dringen, R.1    Kussmaul, L.2    Gutterer, J.M.3    Hirrlinger, J.4    Hamprecht, B.5
  • 11
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Droge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 12
    • 0031692606 scopus 로고    scopus 로고
    • Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of rat during postnatal development
    • S.M. D'Souza, and I.R. Brown Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of rat during postnatal development Cell Stress Chaperones 3 1998 188 199
    • (1998) Cell Stress Chaperones , vol.3 , pp. 188-199
    • D'Souza, S.M.1    Brown, I.R.2
  • 13
    • 0036902430 scopus 로고    scopus 로고
    • Induction of heat shock proteins (HSPs) by sodium arsenite in cultured astrocytes and reduction of hydrogen peroxide-induced cell death
    • B. Fauconneau, V. Petegnief, C. Sanfeliu, A. Piriou, and A.M. Planas Induction of heat shock proteins (HSPs) by sodium arsenite in cultured astrocytes and reduction of hydrogen peroxide-induced cell death J. Neurochem. 83 2002 1338 1348
    • (2002) J. Neurochem. , vol.83 , pp. 1338-1348
    • Fauconneau, B.1    Petegnief, V.2    Sanfeliu, C.3    Piriou, A.4    Planas, A.M.5
  • 14
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • L. Packer Academic Press New York
    • L. Flohe, and W.A. Gunzler Assays of glutathione peroxidase L. Packer Methods in Enzymology vol. 105 1984 Academic Press New York 114 121
    • (1984) Methods in Enzymology , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 15
    • 0034801245 scopus 로고    scopus 로고
    • Stress proteins in oligodendrocytes: Differential effects of heat shock and oxidative stress
    • O. Goldbaum, and C. Richter-Landsberg Stress proteins in oligodendrocytes: differential effects of heat shock and oxidative stress J. Neurochem. 78 2001 1233 1242
    • (2001) J. Neurochem. , vol.78 , pp. 1233-1242
    • Goldbaum, O.1    Richter-Landsberg, C.2
  • 16
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • I. Guzhova, K. Kislyakova, O. Moskaliova, I. Fridlanskaya, M. Tytell, M. Cheetham, and B. Margulis In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance Brain Res. 914 2001 66 73
    • (2001) Brain Res. , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 17
    • 84996120592 scopus 로고
    • Oxidant and the central nervous system: Somefundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke?
    • B. Halliwell Oxidant and the central nervous system: somefundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke? Acta Neurol. Scand. Suppl. 126 1989 23 33
    • (1989) Acta Neurol. Scand. Suppl. , vol.126 , pp. 23-33
    • Halliwell, B.1
  • 18
    • 0030707678 scopus 로고    scopus 로고
    • Protection against glutamate-induced cytotoxicity in C6 glial cells by thiol antioxidants
    • D. Han, C.K. Sen, S. Roy, M.S. Kobayashi, H.J. Tritschler, and L. Packer Protection against glutamate-induced cytotoxicity in C6 glial cells by thiol antioxidants Am. J. Physiol. 273 1997 1771 1778
    • (1997) Am. J. Physiol. , vol.273 , pp. 1771-1778
    • Han, D.1    Sen, C.K.2    Roy, S.3    Kobayashi, M.S.4    Tritschler, H.J.5    Packer, L.6
  • 19
    • 2942614914 scopus 로고    scopus 로고
    • NMDA and AMP a receptors mediated intracellular calcium increase in rat cortical astrocytes
    • B. Hu, S.G. Sun, and E.T. Tong NMDA and AMP A receptors mediated intracellular calcium increase in rat cortical astrocytes Acta Pharmacol. Sin. 25 2004 714 720
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 714-720
    • Hu, B.1    Sun, S.G.2    Tong, E.T.3
  • 20
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • M. Jaattela, D. Wissing, K. Kokholm, T. Kallunki, and M. Egebald Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases EMBO J. 17 1998 6124 6134
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egebald, M.5
  • 23
    • 12244274982 scopus 로고    scopus 로고
    • Creatine enhances survival of glutamate treated neuronal/glial cells, modulates Ras/NF-kappaB signaling and increases the generation of reactive oxygen species
    • E. Juraleva, T. Barbakadze, D. Mikeladze, and T. Kekelidze Creatine enhances survival of glutamate treated neuronal/glial cells, modulates Ras/NF-kappaB signaling and increases the generation of reactive oxygen species J. Neurosci. Res. 79 2004 224 230
    • (2004) J. Neurosci. Res. , vol.79 , pp. 224-230
    • Juraleva, E.1    Barbakadze, T.2    Mikeladze, D.3    Kekelidze, T.4
  • 24
    • 0037216148 scopus 로고    scopus 로고
    • Stress proteins and glial functions: Possible therapeutic targets for neurodegenerative disorders
    • Y. Kitamura, and Y. Nomura Stress proteins and glial functions: possible therapeutic targets for neurodegenerative disorders Pharmacol. Ther. 97 2003 35 53
    • (2003) Pharmacol. Ther. , vol.97 , pp. 35-53
    • Kitamura, Y.1    Nomura, Y.2
  • 25
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Y. Kobayashi, A. Kume, M. Li, M. Doyu, M. Hata, K. Ohtsuka, and G. Sobue Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract J. Biol. Chem. 275 2000 8772 8778
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 26
    • 0030597122 scopus 로고    scopus 로고
    • Expression of hsp70 mRNA is induced in the brain of transgenic mice overexpressing human CuZn-superoxide dismutase following transient global ischemia
    • T. Kondo, K. Murakami, J. Honkaniemi, F.R. Sharp, C.J. Epstein, and P.H. Chan Expression of hsp70 mRNA is induced in the brain of transgenic mice overexpressing human CuZn-superoxide dismutase following transient global ischemia Brain Res. 737 1996 321 326
    • (1996) Brain Res. , vol.737 , pp. 321-326
    • Kondo, T.1    Murakami, K.2    Honkaniemi, J.3    Sharp, F.R.4    Epstein, C.J.5    Chan, P.H.6
  • 27
    • 0017804313 scopus 로고
    • Generation of superoxide radical during autoxidation of hydroxylamine and an assay for superoxide dismutases
    • Y. Kono Generation of superoxide radical during autoxidation of hydroxylamine and an assay for superoxide dismutases Arch. Biochem. Biophys. 186 1978 189 195
    • (1978) Arch. Biochem. Biophys. , vol.186 , pp. 189-195
    • Kono, Y.1
  • 28
    • 0038334574 scopus 로고    scopus 로고
    • Functional NMDA receptors subtype 2B expressed in astrocytes after ischemia in vivo and anoxia in vitro
    • C. Krebs, H.B. Fernandes, C. Sheldon, L.A. Raymond, and K.G. Baimbridge Functional NMDA receptors subtype 2B expressed in astrocytes after ischemia in vivo and anoxia in vitro J. Neurosci. 23 2003 3364 3372
    • (2003) J. Neurosci. , vol.23 , pp. 3364-3372
    • Krebs, C.1    Fernandes, H.B.2    Sheldon, C.3    Raymond, L.A.4    Baimbridge, K.G.5
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0036795854 scopus 로고    scopus 로고
    • Pl6ink4a and retinoic acid modulate rhoA and GFAP expression during induction of a stellate phenotype in U343 MG-A astrocytoma cells
    • A. Langlois, S. Lee, D.S. Kim, P.B. Dirks, and J.T. Rutka pl6ink4a and retinoic acid modulate rhoA and GFAP expression during induction of a stellate phenotype in U343 MG-A astrocytoma cells Glia 40 2002 85 94
    • (2002) Glia , vol.40 , pp. 85-94
    • Langlois, A.1    Lee, S.2    Kim, D.S.3    Dirks, P.B.4    Rutka, J.T.5
  • 31
    • 0034954215 scopus 로고    scopus 로고
    • Differential neuroprotection from human heat shock protein 70 overexpression in in vitro and in vivo models of ischemia and ischemia-like conditions
    • J.E. Lee, M.A. Yenari, G.H. Sun, L. Xu, M.R. Emond, D. Cheng, G.K. Steinberg, and R.G. Giffard Differential neuroprotection from human heat shock protein 70 overexpression in in vitro and in vivo models of ischemia and ischemia-like conditions Exp. Neurol. 170 2001 129 139
    • (2001) Exp. Neurol. , vol.170 , pp. 129-139
    • Lee, J.E.1    Yenari, M.A.2    Sun, G.H.3    Xu, L.4    Emond, M.R.5    Cheng, D.6    Steinberg, G.K.7    Giffard, R.G.8
  • 32
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • P. Liang, and T.H. MacRae Molecular chaperones and the cytoskeleton J. Cell Sci. 110 1997 1431 1440
    • (1997) J. Cell Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 33
    • 0026772696 scopus 로고
    • Regulation of insulin-like growth factor 1 production in rat C6 glioma cells: Possible role as an autocrine/paracrine growth factor
    • W.L. Lowe Jr., T. Meyer, C.W. Karpen, and L.R. Lorentzen Regulation of insulin-like growth factor 1 production in rat C6 glioma cells: possible role as an autocrine/paracrine growth factor Endocrinology 130 1992 2683 2691
    • (1992) Endocrinology , vol.130 , pp. 2683-2691
    • Lowe Jr., W.L.1    Meyer, T.2    Karpen, C.W.3    Lorentzen, L.R.4
  • 34
    • 0027976087 scopus 로고
    • Vitamin E, ascorbate, glutathione, glutathione disulfide and enzymes of glutathione metabolism in chick astrocytes and neurons: Evidence that astrocytes play an important role in antioxidative processes in brain
    • T.K. Makar, M. Nedergaard, A. Preuss, A.S. Gelbard, A.S. Perumal, and A.J.L. Cooper Vitamin E, ascorbate, glutathione, glutathione disulfide and enzymes of glutathione metabolism in chick astrocytes and neurons: evidence that astrocytes play an important role in antioxidative processes in brain J. Neurochem. 62 1994 45 53
    • (1994) J. Neurochem. , vol.62 , pp. 45-53
    • Makar, T.K.1    Nedergaard, M.2    Preuss, A.3    Gelbard, A.S.4    Perumal, A.S.5    Cooper, A.J.L.6
  • 35
    • 0024326484 scopus 로고
    • Early and late passage C6 glial cell growth: Similarities with primary glial cells in culture
    • D. Mangoura, N. Sakellaridis, J. Jones, and A. Vernadakis Early and late passage C6 glial cell growth: similarities with primary glial cells in culture Neurochem. Res. 14 1989 941 947
    • (1989) Neurochem. Res. , vol.14 , pp. 941-947
    • Mangoura, D.1    Sakellaridis, N.2    Jones, J.3    Vernadakis, A.4
  • 36
    • 0026747874 scopus 로고
    • N-methyl-d-aspartate receptor-mediated neuroprotection in cerebellar granule cells requires new RNA and protein synthesis
    • A.M. Marini, and S.M. Paul N-methyl-d-aspartate receptor-mediated neuroprotection in cerebellar granule cells requires new RNA and protein synthesis Proc. Natl. Acad. Sci. U.S.A. 89 1992 6555 6559
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6555-6559
    • Marini, A.M.1    Paul, S.M.2
  • 37
    • 0035860435 scopus 로고    scopus 로고
    • Riluzole stimulates nerve growth factor, brain-derived neurotrophic factor and glial cell line-derived neurotrophic factor synthesis in cultured astrocytes
    • I. Mizuta, M. Ohita, K. Ohita, M. Nishimura, E. Mizuta, and S. Kuno Riluzole stimulates nerve growth factor, brain-derived neurotrophic factor and glial cell line-derived neurotrophic factor synthesis in cultured astrocytes Neurosci. Lett. 310 2001 117 120
    • (2001) Neurosci. Lett. , vol.310 , pp. 117-120
    • Mizuta, I.1    Ohita, M.2    Ohita, K.3    Nishimura, M.4    Mizuta, E.5    Kuno, S.6
  • 38
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • D.D. Mosser, A.W. Caron, L. Bourget, C. Denis-Larose, and B. Massie Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis Mol. Cell. Biol. 17 1997 5317 5327
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 39
    • 0030174253 scopus 로고    scopus 로고
    • Astrocyte survival and HSP70 heat shock protein induction following heat shock and acidosis
    • P. Narasimhan, R.A. Swanson, S.M. Sagar, and F.R. Sharp Astrocyte survival and HSP70 heat shock protein induction following heat shock and acidosis Glia 17 1998 147 159
    • (1998) Glia , vol.17 , pp. 147-159
    • Narasimhan, P.1    Swanson, R.A.2    Sagar, S.M.3    Sharp, F.R.4
  • 40
    • 0038579599 scopus 로고    scopus 로고
    • In vivo neuroprotective role of NMDA receptors against kainate-induced excitotoxicity in murine hippocampal pyramidal neurons
    • K. Ogita, H. Okuda, Y. Yamamoto, N. Nishiyama, and Y. Yoneda In vivo neuroprotective role of NMDA receptors against kainate-induced excitotoxicity in murine hippocampal pyramidal neurons J. Neurochem. 85 2003 1336 1346
    • (2003) J. Neurochem. , vol.85 , pp. 1336-1346
    • Ogita, K.1    Okuda, H.2    Yamamoto, Y.3    Nishiyama, N.4    Yoneda, Y.5
  • 41
    • 0142075876 scopus 로고    scopus 로고
    • Molecular chaperones, stress proteins and redox homeostasis
    • E. Papp, G. Nardai, C. Soti, and P. Csermely Molecular chaperones, stress proteins and redox homeostasis Biofactors 17 2003 249 257
    • (2003) Biofactors , vol.17 , pp. 249-257
    • Papp, E.1    Nardai, G.2    Soti, C.3    Csermely, P.4
  • 42
    • 0028829795 scopus 로고
    • NMDA receptors mediate heat shock protein induction in mouse brain following administration of the ibotenic acid analogue AMAA
    • A.M. Planas, I. Ferrer, and E. Rodriguez-Farre NMDA receptors mediate heat shock protein induction in mouse brain following administration of the ibotenic acid analogue AMAA Brain Res. 700 1995 289 294
    • (1995) Brain Res. , vol.700 , pp. 289-294
    • Planas, A.M.1    Ferrer, I.2    Rodriguez-Farre, E.3
  • 43
    • 0034889453 scopus 로고    scopus 로고
    • Preconditioning-induced neuroprotection is mediated by reactive oxygen species and activation of transcription factor nuclear factor-kappaB
    • A. Ravati, B. Ahlemeyer, A. Becker, S. Klumpp, and J. Krielglstein Preconditioning-induced neuroprotection is mediated by reactive oxygen species and activation of transcription factor nuclear factor-kappaB J. Neurochem. 78 2001 909 919
    • (2001) J. Neurochem. , vol.78 , pp. 909-919
    • Ravati, A.1    Ahlemeyer, B.2    Becker, A.3    Klumpp, S.4    Krielglstein, J.5
  • 44
    • 0034595546 scopus 로고    scopus 로고
    • Preconditioning-induced neuroprotection is mediated by reactive oxygen species
    • A. Ravati, B. Ahlemeyer, A. Becker, and J. Krieglstein Preconditioning-induced neuroprotection is mediated by reactive oxygen species Brain Res. 866 2000 23 32
    • (2000) Brain Res. , vol.866 , pp. 23-32
    • Ravati, A.1    Ahlemeyer, B.2    Becker, A.3    Krieglstein, J.4
  • 45
    • 0035805222 scopus 로고    scopus 로고
    • The influence of oxidative stress on catalase and MnSOD gene transcription in astrocytes
    • E. Rohrdanz, G. Schmuck, S. Ohler, and R. Kahl The influence of oxidative stress on catalase and MnSOD gene transcription in astrocytes Brain Res. 900 2001 128 136
    • (2001) Brain Res. , vol.900 , pp. 128-136
    • Rohrdanz, E.1    Schmuck, G.2    Ohler, S.3    Kahl, R.4
  • 47
    • 0042328211 scopus 로고    scopus 로고
    • Spinal heat shock protein (70) expression: Effect of spinal ischemia, hyperthermia (42°C)/hypothermia (27°C), NMDA receptor stimulation and potassium evoked depolarization on the induction
    • T. Sasara, D. Cizkova, R. Mestril, J. Galik, K. Sugahara, and M. Marsala Spinal heat shock protein (70) expression: effect of spinal ischemia, hyperthermia (42°C)/hypothermia (27°C), NMDA receptor stimulation and potassium evoked depolarization on the induction Neurochem. Int. 44 2004 53 64
    • (2004) Neurochem. Int. , vol.44 , pp. 53-64
    • Sasara, T.1    Cizkova, D.2    Mestril, R.3    Galik, J.4    Sugahara, K.5    Marsala, M.6
  • 48
    • 0034873185 scopus 로고    scopus 로고
    • Reactive oxygen species as intracellular messengers during cell growth and differentiation
    • H. Sauer, M. Wartenberg, and J. Hescheler Reactive oxygen species as intracellular messengers during cell growth and differentiation Cell Physiol. Biochem. 11 2001 173 186
    • (2001) Cell Physiol. Biochem. , vol.11 , pp. 173-186
    • Sauer, H.1    Wartenberg, M.2    Hescheler, J.3
  • 50
    • 0014428865 scopus 로고
    • Estimation of total, protein bound and non-protein sulfhydryl groups in tissue with Ellman's reagent
    • J. Sedlak, and R.H. Lindsay Estimation of total, protein bound and non-protein sulfhydryl groups in tissue with Ellman's reagent Anal. Biochem. 25 1968 192 205
    • (1968) Anal. Biochem. , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 51
    • 0023236818 scopus 로고
    • Histochemical eveluation of glutathione in brain
    • A. Slivka, C. Mytilineou, and G. Cohen Histochemical eveluation of glutathione in brain Brain Res. 409 1987 275 284
    • (1987) Brain Res. , vol.409 , pp. 275-284
    • Slivka, A.1    Mytilineou, C.2    Cohen, G.3
  • 52
    • 1542718628 scopus 로고    scopus 로고
    • Heat shock proteins in the regulation of apoptosis: New strategies in tumor therapy: A comprehensive review
    • A.S. Sreedhar, and P. Csermely Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review Pharmacol. Ther. 101 2004 227 257
    • (2004) Pharmacol. Ther. , vol.101 , pp. 227-257
    • Sreedhar, A.S.1    Csermely, P.2
  • 53
    • 0036826902 scopus 로고    scopus 로고
    • Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase
    • V.C. Stewart, R. Stone, M.E. Gegg, M.A. Sharpe, R.D. Hurst, J.B. Clarke, and S.J. Heales Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase J. Neurochem. 83 2002 984 991
    • (2002) J. Neurochem. , vol.83 , pp. 984-991
    • Stewart, V.C.1    Stone, R.2    Gegg, M.E.3    Sharpe, M.A.4    Hurst, R.D.5    Clarke, J.B.6    Heales, S.J.7
  • 54
    • 0032030809 scopus 로고    scopus 로고
    • Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock and ethanol
    • C.Y. Su, K.Y. Chong, O.E. Owen, W.H. Dillmann, C. Chang, and C.C. Lai Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock and ethanol J. Mol. Cell Cardiol. 30 1998 587 598
    • (1998) J. Mol. Cell Cardiol. , vol.30 , pp. 587-598
    • Su, C.Y.1    Chong, K.Y.2    Owen, O.E.3    Dillmann, W.H.4    Chang, C.5    Lai, C.C.6
  • 55
    • 0030574089 scopus 로고    scopus 로고
    • Heat shock protects cultured astrocytes in a model of reperfusion injury
    • K. Takuma, T. Matsuda, Y. Kishida, S. Asano, Y.H. Seong, and A. Baba Heat shock protects cultured astrocytes in a model of reperfusion injury Brain Res. 735 1996 265 270
    • (1996) Brain Res. , vol.735 , pp. 265-270
    • Takuma, K.1    Matsuda, T.2    Kishida, Y.3    Asano, S.4    Seong, Y.H.5    Baba, A.6
  • 56
    • 0034693326 scopus 로고    scopus 로고
    • CV-2619 protects cultured astrocytes against reperfusion injury via nerve growth factor production
    • K. Takuma, T. Yoshida, E. Lee, K. Mori, T. Kishi, A. Baba, and T. Matsuda CV-2619 protects cultured astrocytes against reperfusion injury via nerve growth factor production Eur. J. Pharmacol. 406 2000 333 339
    • (2000) Eur. J. Pharmacol. , vol.406 , pp. 333-339
    • Takuma, K.1    Yoshida, T.2    Lee, E.3    Mori, K.4    Kishi, T.5    Baba, A.6    Matsuda, T.7
  • 60
    • 0033566709 scopus 로고    scopus 로고
    • Three-dimensional relationships between hippocampal synapses and astrocytes
    • R. Ventura, and K.M. Harris Three-dimensional relationships between hippocampal synapses and astrocytes J. Neurosci. 19 1999 6897 6906
    • (1999) J. Neurosci. , vol.19 , pp. 6897-6906
    • Ventura, R.1    Harris, K.M.2
  • 61
    • 0031054430 scopus 로고    scopus 로고
    • HSP70 protects murine astrocytes from glucose deprivation injury
    • L. Xu, and R.G. Giffard HSP70 protects murine astrocytes from glucose deprivation injury Neurosci. Lett. 224 1997 9 12
    • (1997) Neurosci. Lett. , vol.224 , pp. 9-12
    • Xu, L.1    Giffard, R.G.2
  • 62
    • 0344392801 scopus 로고    scopus 로고
    • Possible involvement of astrocytes in neuroprotection by cognitive enhancer T-588
    • A. Yamamuro, Y. Ago, K. Takuma, S. Maeda, Y. Sakai, A. Baba, and T. Matsuda Possible involvement of astrocytes in neuroprotection by cognitive enhancer T-588 Neurochem. Res. 28 2003 1779 1783
    • (2003) Neurochem. Res. , vol.28 , pp. 1779-1783
    • Yamamuro, A.1    Ago, Y.2    Takuma, K.3    Maeda, S.4    Sakai, Y.5    Baba, A.6    Matsuda, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.