메뉴 건너뛰기




Volumn 36, Issue 11, 2004, Pages 1393-1402

Oxidative stress promotes τ dephosphorylation in neuronal cells: The roles of cdk5 and PP1

Author keywords

4 HNE; 4 hydroxy 2 nonenal; Alzheimer's disease; Cyclin dependent kinase 5; Free radicals; Hydrogen peroxide; I 2; N acetyl L cysteine; NAC; Oxidative stress; PP1; Protein phosphatase 1; protein phosphatase 1; protein phosphatase 1 inhibitor 2; Tau phosphorylation

Indexed keywords

ACETYLCYSTEINE; ANTIBODY; CYCLIN DEPENDENT KINASE 5; EPITOPE; HYDROGEN PEROXIDE; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN INHIBITOR; TAU PROTEIN;

EID: 2342466091     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.03.007     Document Type: Article
Times cited : (77)

References (52)
  • 3
    • 1642555537 scopus 로고    scopus 로고
    • Iron involvement in neural damage and microgliosis in models of neurodegenerative diseases
    • Shoham S., Youdim M.B. Iron involvement in neural damage and microgliosis in models of neurodegenerative diseases. Cell Mol. Biol. (Noisy-le-grand). 46:2000;743-760
    • (2000) Cell Mol. Biol. (Noisy-le-grand) , vol.46 , pp. 743-760
    • Shoham, S.1    Youdim, M.B.2
  • 4
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded
    • Julien J.P. Amyotrophic lateral sclerosis. unfolding the toxicity of the misfolded. Cell. 104:2001;581-591
    • (2001) Cell , vol.104 , pp. 581-591
    • Julien, J.P.1
  • 5
    • 0035370261 scopus 로고    scopus 로고
    • The significance of τ and and α-synuclein inclusions in neurodegenerative diseases
    • Goedert M. The significance of τ and and α-synuclein inclusions in neurodegenerative diseases. Curr. Opin. Genet. Dev. 11:2001;343-351
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 343-351
    • Goedert, M.1
  • 6
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield D.A., Kanski J. Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech. Ageing Dev. 122:2001;945-962
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 7
    • 0034829801 scopus 로고    scopus 로고
    • The molecular bases of Alzheimer's disease and other neurodegenerative disorders
    • Maccioni R.B., Munoz J.P., Barbeito L. The molecular bases of Alzheimer's disease and other neurodegenerative disorders. Arch. Med. Res. 32:2001;367-381
    • (2001) Arch. Med. Res. , vol.32 , pp. 367-381
    • MacCioni, R.B.1    Munoz, J.P.2    Barbeito, L.3
  • 9
    • 0022260427 scopus 로고
    • Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils. Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide
    • Ohno Y., Gallin J.I. Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils. Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide. J. Biol. Chem. 260:1985;8438-8446
    • (1985) J. Biol. Chem. , vol.260 , pp. 8438-8446
    • Ohno, Y.1    Gallin, J.I.2
  • 12
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 13
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman M.S., Ragan C.I., Iversen L.L. Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid- mediated cell death. Proc. Natl. Acad. Sci. USA. 91:1994;1470-1474
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 14
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris M.E., Hensley K., Butterfield D.A., Leedle R.A., Carney J.M. Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 131:1995;193-202
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 15
    • 0028971093 scopus 로고
    • Beta-amyloid-induced toxicity in rat hippocampal cells: In vitro evidence for the involvement of free radicals
    • Manelli A.M., Puttfarcken P.S. Beta-amyloid-induced toxicity in rat hippocampal cells: in vitro evidence for the involvement of free radicals. Brain Res. Bull. 38:1995;569-576
    • (1995) Brain Res. Bull. , vol.38 , pp. 569-576
    • Manelli, A.M.1    Puttfarcken, P.S.2
  • 16
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson M.P., Goodman Y. Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res. 676:1995;219-224
    • (1995) Brain Res. , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 17
    • 0029150526 scopus 로고
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons
    • 2+ concentration, and neurotoxicity and increase antioxidant enzyme activities in hippocampal neurons. J. Neurochem. 65:1995;1740-1751
    • (1995) J. Neurochem. , vol.65 , pp. 1740-1751
    • Mattson, M.P.1    Lovell, M.A.2    Furukawa, K.3    Markesberry, W.R.4
  • 18
  • 19
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce τ phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B.A. Beta-amyloid fibrils induce τ phosphorylation and loss of microtubule binding. Neuron. 14:1995;879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 20
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of τ protein kinase I/glycogen synthase kinase-3 β
    • Takashima A., Noguchi K., Michel G., Mercken M., Hoshi M., Ishiguro K., Imahori K. Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of τ protein kinase I/glycogen synthase kinase-3 β Neurosci. Lett. 203:1996;33-36
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 21
    • 0032859938 scopus 로고    scopus 로고
    • Inhibition of τ phosphorylating protein kinase cdk5 prevents β-amyloid-induced neuronal death
    • Alvarez A., Toro R., Caceres A., Maccioni R.B. Inhibition of τ phosphorylating protein kinase cdk5 prevents β-amyloid-induced neuronal death. FEBS Lett. 459:1999;421-426
    • (1999) FEBS Lett. , vol.459 , pp. 421-426
    • Alvarez, A.1    Toro, R.2    Caceres, A.3    MacCioni, R.B.4
  • 22
    • 0035298135 scopus 로고    scopus 로고
    • A Cdk5-p35 stable complex is involved in the β-amyloid-induced deregulation of Cdk5 activity in hippocampal neurons
    • Alvarez A., Munoz J.P., Maccioni R.B. A Cdk5-p35 stable complex is involved in the β-amyloid-induced deregulation of Cdk5 activity in hippocampal neurons. Exp. Cell Res. 264:2001;266-274
    • (2001) Exp. Cell Res. , vol.264 , pp. 266-274
    • Alvarez, A.1    Munoz, J.P.2    MacCioni, R.B.3
  • 24
    • 0035968240 scopus 로고    scopus 로고
    • Neuronal Cdc2-like protein kinase (Cdk5/p25) is associated with protein phosphatase 1 and phosphorylates inhibitor-2
    • Agarwal-Mawal A., Paudel H.K. Neuronal Cdc2-like protein kinase (Cdk5/p25) is associated with protein phosphatase 1 and phosphorylates inhibitor-2. J. Biol. Chem. 276:2001;23712-23718
    • (2001) J. Biol. Chem. , vol.276 , pp. 23712-23718
    • Agarwal-Mawal, A.1    Paudel, H.K.2
  • 25
    • 0030986545 scopus 로고    scopus 로고
    • Beta-amyloid and ionophore A23187 evoke and τ hyperphosphorylation by distinct intracellular pathways: Differential involvement of the calpain/protein kinase C system
    • Shea T.B., Prabhakar S., Ekinci F.J. Beta-amyloid and ionophore A23187 evoke and τ hyperphosphorylation by distinct intracellular pathways: differential involvement of the calpain/protein kinase C system. J. Neurosci. Res. 49:1997;759-768
    • (1997) J. Neurosci. Res. , vol.49 , pp. 759-768
    • Shea, T.B.1    Prabhakar, S.2    Ekinci, F.J.3
  • 26
    • 0032528162 scopus 로고    scopus 로고
    • Calcineurin inhibition prevents calpain-mediated proteolysis of τ in differentiated PC12 cells
    • Xie H.Q., Johnson G.V. Calcineurin inhibition prevents calpain-mediated proteolysis of τ in differentiated PC12 cells. J. Neurosci. Res. 53:1998;153-164
    • (1998) J. Neurosci. Res. , vol.53 , pp. 153-164
    • Xie, H.Q.1    Johnson, G.V.2
  • 27
    • 0033597936 scopus 로고    scopus 로고
    • Transient increases in intracellular calcium result in prolonged site-selective increases in τ phosphorylation through a glycogen synthase kinase 3 β-dependent pathway
    • Hartigan J.A., Johnson G.V. Transient increases in intracellular calcium result in prolonged site-selective increases in τ phosphorylation through a glycogen synthase kinase 3 β-dependent pathway. J. Biol. Chem. 274:1999;21395-21401
    • (1999) J. Biol. Chem. , vol.274 , pp. 21395-21401
    • Hartigan, J.A.1    Johnson, G.V.2
  • 28
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker G.A., Cowan W.M. Rat hippocampal neurons in dispersed cell culture. Brain Res. 126:1977;397-402
    • (1977) Brain Res. , vol.126 , pp. 397-402
    • Banker, G.A.1    Cowan, W.M.2
  • 29
    • 0000854861 scopus 로고
    • Growth of a rat neuroblastoma cell line in serum-free supplemented medium
    • Bottenstein J.E., Sato G.H. Growth of a rat neuroblastoma cell line in serum-free supplemented medium. Proc. Natl. Acad. Sci. USA. 76:1979;514-517
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 514-517
    • Bottenstein, J.E.1    Sato, G.H.2
  • 30
    • 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.M. 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
  • 31
    • 0016360218 scopus 로고
    • Maturation of the head of bacteriophage T4. IV. The proteins of the core of the tubular polyheads and in vitro cleavage of the head proteins
    • Laemmli U.K., Quittner S.F. Maturation of the head of bacteriophage T4. IV. The proteins of the core of the tubular polyheads and in vitro cleavage of the head proteins. Virology. 62:1974;483-499
    • (1974) Virology , vol.62 , pp. 483-499
    • Laemmli, U.K.1    Quittner, S.F.2
  • 32
    • 0034672554 scopus 로고    scopus 로고
    • Phosphorylated, but not native, τ protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal
    • Perez M., Cuadros R., Smith M.A., Perry G., Avila J. Phosphorylated, but not native, τ protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal. FEBS Lett. 486:2000;270-274
    • (2000) FEBS Lett. , vol.486 , pp. 270-274
    • Perez, M.1    Cuadros, R.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 34
    • 0035872474 scopus 로고    scopus 로고
    • Mechanisms by which metals promote events connected to neurodegenerative diseases
    • Campbell A., Smith M.A., Sayre L.M., Bondy S.C., Perry G. Mechanisms by which metals promote events connected to neurodegenerative diseases. Brain Res. Bull. 55:2001;125-132
    • (2001) Brain Res. Bull. , vol.55 , pp. 125-132
    • Campbell, A.1    Smith, M.A.2    Sayre, L.M.3    Bondy, S.C.4    Perry, G.5
  • 36
    • 0033836580 scopus 로고    scopus 로고
    • In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification
    • Takeda A., Smith M.A., Avila J., Nunomura A., Siedlak S.L., Zhu X., Perry G., Sayre L.M. In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification. J. Neurochem. 75:2000;1234-1241
    • (2000) J. Neurochem. , vol.75 , pp. 1234-1241
    • Takeda, A.1    Smith, M.A.2    Avila, J.3    Nunomura, A.4    Siedlak, S.L.5    Zhu, X.6    Perry, G.7    Sayre, L.M.8
  • 38
    • 0031944692 scopus 로고    scopus 로고
    • Evidence of oxidative stress and in vivo neurotoxicity of β-amyloid in a transgenic mouse model of Alzheimer's disease: A chronic oxidative paradigm for testing antioxidant therapies in vivo
    • Pappolla M.A., Chyan Y.J., Omar R.A., Hsiao K., Perry G., Smith M.A., Bozner P. Evidence of oxidative stress and in vivo neurotoxicity of β-amyloid in a transgenic mouse model of Alzheimer's disease: a chronic oxidative paradigm for testing antioxidant therapies in vivo. Am. J. Pathol. 152:1998;871-877
    • (1998) Am. J. Pathol. , vol.152 , pp. 871-877
    • Pappolla, M.A.1    Chyan, Y.J.2    Omar, R.A.3    Hsiao, K.4    Perry, G.5    Smith, M.A.6    Bozner, P.7
  • 40
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42)
    • Yatin S.M., Varadarajan S., Link C.D., Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid β-peptide (1-42). Neurobiol. Aging. 20:1999;325-330
    • (1999) Neurobiol. Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4
  • 41
    • 0030998758 scopus 로고    scopus 로고
    • Oxidative stress induces dephosphorylation of τ in rat brain primary neuronal cultures
    • Davis D.R., Anderton B.H., Brion J.P., Reynolds C.H., Hanger D.P. Oxidative stress induces dephosphorylation of τ in rat brain primary neuronal cultures. J. Neurochem. 68:1997;1590-1597
    • (1997) J. Neurochem. , vol.68 , pp. 1590-1597
    • Davis, D.R.1    Anderton, B.H.2    Brion, J.P.3    Reynolds, C.H.4    Hanger, D.P.5
  • 43
    • 0029123294 scopus 로고
    • The phosphorylation state of the microtubule-associated protein τ as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures
    • Davis D.R., Brion J.P., Couck A.M., Gallo J.M., Hanger D.P., Ladhani K., Lewis C., Miller C.C., Rupniak T., Smith C. The phosphorylation state of the microtubule-associated protein τ as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures. Biochem. J. 309:1995;941-949
    • (1995) Biochem. J. , vol.309 , pp. 941-949
    • Davis, D.R.1    Brion, J.P.2    Couck, A.M.3    Gallo, J.M.4    Hanger, D.P.5    Ladhani, K.6    Lewis, C.7    Miller, C.C.8    Rupniak, T.9    Smith, C.10
  • 44
    • 0029072567 scopus 로고
    • Modulation of the phosphorylation state of τ in situ: The roles of calcium and cyclic AMP
    • Fleming L.M., Johnson G.V. Modulation of the phosphorylation state of τ in situ: the roles of calcium and cyclic AMP. Biochem. J. 309:1995;41-47
    • (1995) Biochem. J. , vol.309 , pp. 41-47
    • Fleming, L.M.1    Johnson, G.V.2
  • 46
    • 0030033901 scopus 로고    scopus 로고
    • Changes in phosphorylation of τ during ischemia and reperfusion in the rabbit spinal cord
    • Shackelford D.A., Nelson K.E. Changes in phosphorylation of τ during ischemia and reperfusion in the rabbit spinal cord. J. Neurochem. 66:1996;286-295
    • (1996) J. Neurochem. , vol.66 , pp. 286-295
    • Shackelford, D.A.1    Nelson, K.E.2
  • 47
    • 0037357190 scopus 로고    scopus 로고
    • Iron induced oxidative stress modify and τ phosphorylation patterns in hippocampal cell cultures
    • Egana J.T., Zambrano C., Nuñez M.T., Gonzalez-Billault C., Maccioni R.B. Iron induced oxidative stress modify and τ phosphorylation patterns in hippocampal cell cultures. Biometals. 16:2003;215-223
    • (2003) Biometals , vol.16 , pp. 215-223
    • Egana, J.T.1    Zambrano, C.2    Nuñez, M.T.3    Gonzalez-Billault, C.4    MacCioni, R.B.5
  • 48
    • 0030576564 scopus 로고    scopus 로고
    • Increased τ immunoreactivity in oligodendrocytes following human stroke and head injury
    • Irving E.A., Nicoll J., Graham D.I., Dewar D. Increased τ immunoreactivity in oligodendrocytes following human stroke and head injury. Neurosci. Lett. 213:1996;189-192
    • (1996) Neurosci. Lett. , vol.213 , pp. 189-192
    • Irving, E.A.1    Nicoll, J.2    Graham, D.I.3    Dewar, D.4
  • 49
    • 0030065109 scopus 로고    scopus 로고
    • Heat shock induces rapid dephosphorylation of τ in both female and male rats followed by hyperphosphorylation only in female rats: Implications for Alzheimer's disease
    • Papasozomenos S.C. Heat shock induces rapid dephosphorylation of τ in both female and male rats followed by hyperphosphorylation only in female rats: implications for Alzheimer's disease. J. Neurochem. 66:1996;1140-1149
    • (1996) J. Neurochem. , vol.66 , pp. 1140-1149
    • Papasozomenos, S.C.1
  • 51
    • 17544393297 scopus 로고    scopus 로고
    • Tau dephosphorylation at tau-1 site correlates with its association to cell membrane
    • Arrasate M., Perez M., Avila J. Tau dephosphorylation at tau-1 site correlates with its association to cell membrane. Neurochem. Res. 25:2000;43-50
    • (2000) Neurochem. Res. , vol.25 , pp. 43-50
    • Arrasate, M.1    Perez, M.2    Avila, J.3
  • 52
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein τ
    • Liao H., Li Y., Brautigan D.L., Gundersen G.G. Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein τ J. Biol. Chem. 273:1998;21901-21908
    • (1998) J. Biol. Chem. , vol.273 , pp. 21901-21908
    • Liao, H.1    Li, Y.2    Brautigan, D.L.3    Gundersen, G.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.