메뉴 건너뛰기




Volumn 86, Issue 8, 2004, Pages 553-559

Oxidative modification of neurofilament-L by the Cu,Zn-superoxide dismutase and hydrogen peroxide system

Author keywords

Copper; Hydrogen peroxide; Modification; Neurofilament L

Indexed keywords

ANSERINE; CARNOSINE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; HYDROGEN PEROXIDE; SCAVENGER;

EID: 4544350547     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.07.006     Document Type: Article
Times cited : (21)

References (48)
  • 2
    • 0027406083 scopus 로고
    • Motor neurons and neurofilaments in sickness and in health
    • Brady S.T. Motor neurons and neurofilaments in sickness and in health Cell 73 1993 1 3
    • (1993) Cell , vol.73 , pp. 1-3
    • Brady, S.T.1
  • 3
    • 0022909139 scopus 로고
    • Differential turnover of phosphate groups on neurofilament subunits in mammalian neurons in vivo
    • Nixon R.A., and Lewis S.E. Differential turnover of phosphate groups on neurofilament subunits in mammalian neurons in vivo J. Biol. Chem. 261 1986 16298 16301
    • (1986) J. Biol. Chem. , vol.261 , pp. 16298-16301
    • Nixon, R.A.1    Lewis, S.E.2
  • 4
    • 0026764101 scopus 로고
    • Dynamics of neuronal intermediate filaments: A developmental perspective
    • Nixon R.A., and Shea T.B. Dynamics of neuronal intermediate filaments: a developmental perspective Cell Motil Cytoskeleton 22 1992 81 91
    • (1992) Cell Motil Cytoskeleton , vol.22 , pp. 81-91
    • Nixon, R.A.1    Shea, T.B.2
  • 6
    • 0023255221 scopus 로고
    • The Lewy body in Parkinson's disease
    • Forno L.S. The Lewy body in Parkinson's disease Adv. Neurol. 45 1987 35 43
    • (1987) Adv. Neurol. , vol.45 , pp. 35-43
    • Forno, L.S.1
  • 7
    • 0024512326 scopus 로고
    • The significance of the Lewy body in the diagnosis of idiopathic Parkinson's disease
    • Gibb W.R.G., and Lees A.J. The significance of the Lewy body in the diagnosis of idiopathic Parkinson's disease Neuropathol. Appl. Neurobiol. 15 1989 27 44
    • (1989) Neuropathol. Appl. Neurobiol. , vol.15 , pp. 27-44
    • Gibb, W.R.G.1    Lees, A.J.2
  • 8
    • 1842289165 scopus 로고    scopus 로고
    • Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L
    • Crow J.P., Ye Y.Z., Strong M., Kirk M., Barnes S., and Beckman J.S. Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L J. Neurochem. 69 1997 1945 1953
    • (1997) J. Neurochem. , vol.69 , pp. 1945-1953
    • Crow, J.P.1    Ye, Y.Z.2    Strong, M.3    Kirk, M.4    Barnes, S.5    Beckman, J.S.6
  • 9
    • 0033611619 scopus 로고    scopus 로고
    • Release of copper ions from the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants
    • Eum W.S., and Kang J.H. Release of copper ions from the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants Mol. Cells 9 1999 110 114
    • (1999) Mol. Cells , vol.9 , pp. 110-114
    • Eum, W.S.1    Kang, J.H.2
  • 11
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames B.N., Shigenaga M.K., and Hagen T.M. Oxidants, antioxidants, and the degenerative diseases of aging Proc. Natl. Acad. Sci. USA 90 1993 7915 7922
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 12
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress J. Biol. Chem. 272 1997 20313 20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 13
    • 0028012335 scopus 로고
    • Glutathione peroxidase compensates for the hypersensitivity of Cu,Zn-superoxide dismutase overproducers to oxidant stress
    • Amstad P., Moret R., and Cerutti P. Glutathione peroxidase compensates for the hypersensitivity of Cu,Zn-superoxide dismutase overproducers to oxidant stress J. Biol. Chem. 269 1994 1606 1609
    • (1994) J. Biol. Chem. , vol.269 , pp. 1606-1609
    • Amstad, P.1    Moret, R.2    Cerutti, P.3
  • 14
    • 0022684839 scopus 로고
    • Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elory-Stein O., Bernstein Y., and Groner Y. Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation EMBO J. 5 1986 615 622
    • (1986) EMBO J. , vol.5 , pp. 615-622
    • Elory-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 15
    • 0023848325 scopus 로고
    • Impaired neurotransmitter uptake in PC12 cells overexpressing human Cu/Zn-superoxide dismutase-implication for gene dosage effects in Down syndrome
    • Elory-Stein O., and Groner Y. Impaired neurotransmitter uptake in PC12 cells overexpressing human Cu/Zn-superoxide dismutase-implication for gene dosage effects in Down syndrome Cell 52 1988 259 267
    • (1988) Cell , vol.52 , pp. 259-267
    • Elory-Stein, O.1    Groner, Y.2
  • 17
    • 0027456505 scopus 로고
    • Enzyme function of copper, zinc superoxide dismutase as a free radical generator
    • Yim M.B., Chock P.B., and Stadtman E.R. Enzyme function of copper, zinc superoxide dismutase as a free radical generator J. Biol. Chem. 268 1993 4099 4105
    • (1993) J. Biol. Chem. , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 18
    • 0031588551 scopus 로고    scopus 로고
    • Peroxidative activity of human Cu,Zn-superoxide dismutase
    • Kim S.M., and Kang J.H. Peroxidative activity of human Cu,Zn-superoxide dismutase Mol. Cells 7 1997 120 124
    • (1997) Mol. Cells , vol.7 , pp. 120-124
    • Kim, S.M.1    Kang, J.H.2
  • 19
    • 0031592750 scopus 로고    scopus 로고
    • Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction
    • Kang J.H., and Kim S.M. Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction Mol. Cells 7 1997 553 558
    • (1997) Mol. Cells , vol.7 , pp. 553-558
    • Kang, J.H.1    Kim, S.M.2
  • 21
    • 0029939471 scopus 로고    scopus 로고
    • A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide
    • Yim M.B., Kang J.H., Yim H.-S., Kawk H.-S., Chock P.B., and Stadtman E.R. A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide Proc. Natl. Acad. Sci. USA 93 1996 5709 5714
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5709-5714
    • Yim, M.B.1    Kang, J.H.2    Yim, H.-S.3    Kawk, H.-S.4    Chock, P.B.5    Stadtman, E.R.6
  • 23
    • 0242382769 scopus 로고    scopus 로고
    • Oxidative modification of neurofilament-L by copper-catalyzed reaction
    • Kim N.H., and Kang J.H. Oxidative modification of neurofilament-L by copper-catalyzed reaction J. Biochem. Mol. Biol. 36 2003 488 492
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 488-492
    • Kim, N.H.1    Kang, J.H.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 26
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions Annu. Rev. Biochem. 62 1993 797 821
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 27
    • 0344158770 scopus 로고
    • Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain
    • Kohen R., Yamamoto Y., Cundy K.C., and Ames B.N. Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain Proc. Natl. Acad. Sci. USA 85 1988 3175 3179
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3175-3179
    • Kohen, R.1    Yamamoto, Y.2    Cundy, K.C.3    Ames, B.N.4
  • 28
    • 0023757196 scopus 로고
    • Detection, characterisation, and quantification of carnosine and other histidyl derivatives in cardiac and skeletal muscle
    • O'Dowd J.J., Robins D.J., and Miller D.J. Detection, characterisation, and quantification of carnosine and other histidyl derivatives in cardiac and skeletal muscle Biochem. Biophys. Acta 967 1988 241 249
    • (1988) Biochem. Biophys. Acta , vol.967 , pp. 241-249
    • O'Dowd, J.J.1    Robins, D.J.2    Miller, D.J.3
  • 29
    • 0024990775 scopus 로고
    • Muscle buffering capacity and dipeptide content in the thoroughbred horse, greyhound dog and man
    • Harris R.C., Marlin D.J., Dunnett M., Snow D.H., and Hultman E. Muscle buffering capacity and dipeptide content in the thoroughbred horse, greyhound dog and man Comp. Biochem. Physiol. A 97 1990 249 251
    • (1990) Comp. Biochem. Physiol. a , vol.97 , pp. 249-251
    • Harris, R.C.1    Marlin, D.J.2    Dunnett, M.3    Snow, D.H.4    Hultman, E.5
  • 30
    • 0001688322 scopus 로고
    • The significance of carnosine and anserine in striated skeletal muscle
    • Davey C.L. The significance of carnosine and anserine in striated skeletal muscle Arch. Biochem. Biophys. 89 1960 303 308
    • (1960) Arch. Biochem. Biophys. , vol.89 , pp. 303-308
    • Davey, C.L.1
  • 31
    • 0019364820 scopus 로고
    • Interactions among carnosine, anserine, ophidine and copper in biochemical adaptation
    • Brown C.E. Interactions among carnosine, anserine, ophidine and copper in biochemical adaptation J. Theor. Biol. 88 1981 245 256
    • (1981) J. Theor. Biol. , vol.88 , pp. 245-256
    • Brown, C.E.1
  • 32
    • 0001302366 scopus 로고
    • EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides
    • Chan W.K.M., Decker E.A., Lee J.B., and Butterfield D.A. EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides J. Agric. Food. Chem. 42 1994 1407 1410
    • (1994) J. Agric. Food. Chem. , vol.42 , pp. 1407-1410
    • Chan, W.K.M.1    Decker, E.A.2    Lee, J.B.3    Butterfield, D.A.4
  • 33
    • 84996120592 scopus 로고
    • Oxidants and the central nervous system: Some fundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke?
    • Halliwell B. Oxidants and the central nervous system: some fundamental 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. , Issue.126 , pp. 23-33
    • Halliwell, B.1
  • 34
    • 84996111069 scopus 로고
    • Is Parkinson's disease a progressive siderosis of substantia nigra resulting in iron and melanin induced neurodegeneration?
    • Youdim M.B., Ben-Schachar D., and Riederer P. Is Parkinson's disease a progressive siderosis of substantia nigra resulting in iron and melanin induced neurodegeneration? Acta Neurol. Scand. Suppl. 126 1989 47 54
    • (1989) Acta Neurol. Scand. , Issue.126 , pp. 47-54
    • Youdim, M.B.1    Ben-Schachar, D.2    Riederer, P.3
  • 35
    • 0029751104 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Parkinson's disease
    • Jenner P., and Olanow C.W. Oxidative stress and the pathogenesis of Parkinson's disease Neurology 47 1996 S161 S170
    • (1996) Neurology , vol.47
    • Jenner, P.1    Olanow, C.W.2
  • 36
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheime's disease
    • Markesbery W.R., and Carney J.M. Oxidative alterations in Alzheime's disease Brain Pathol. 9 1999 133 146
    • (1999) Brain Pathol. , vol.9 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 37
    • 0023441198 scopus 로고
    • Ferritin and haemosiderin in free radical generation, lipid peroxidation and protein damage
    • O'Connell M.J., and Peters T.J. Ferritin and haemosiderin in free radical generation, lipid peroxidation and protein damage Chem. Phys. Lipids 45 1987 241 249
    • (1987) Chem. Phys. Lipids , vol.45 , pp. 241-249
    • O'Connell, M.J.1    Peters, T.J.2
  • 39
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • Multhaup G., Schlicksupp A., Hesse L., Beher D., Ruppert T., Masters C.L., and Beyreuther K. The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I) Science 271 1996 1406 1409
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 41
    • 0032786731 scopus 로고    scopus 로고
    • Oxidative stress indicators are elevated in de novo Parkinson's disease patients
    • Ilic T., Jovanovic M., Jovicic A., and Tomovic M. Oxidative stress indicators are elevated in de novo Parkinson's disease patients Funct. Neurol. 14 1999 141 147
    • (1999) Funct. Neurol. , vol.14 , pp. 141-147
    • Ilic, T.1    Jovanovic, M.2    Jovicic, A.3    Tomovic, M.4
  • 42
    • 0029015626 scopus 로고
    • Cu/Zn superoxide dismutase-like immunoreactivity is present in Lewy bodies from Parkinson disease: A light and electron microscopic immunocytochemical study
    • Nishiyama K., Murayama S., Shimizu J., Ohya Y., Kwak S., Asayama K., and Kanazawa I. Cu/Zn superoxide dismutase-like immunoreactivity is present in Lewy bodies from Parkinson disease: a light and electron microscopic immunocytochemical study Acta Neuropathol. (Berl) 89 1995 471 474
    • (1995) Acta Neuropathol. (Berl) , vol.89 , pp. 471-474
    • Nishiyama, K.1    Murayama, S.2    Shimizu, J.3    Ohya, Y.4    Kwak, S.5    Asayama, K.6    Kanazawa, I.7
  • 44
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay J.A., Chin S.M., and Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro Science 240 1988 640 642
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 45
    • 0024571329 scopus 로고
    • Site-specific oxidative DNA damage at polyguanosines produced by copper plus hydrogen peroxide
    • Sagripant J.L., and Kraemer K.H. Site-specific oxidative DNA damage at polyguanosines produced by copper plus hydrogen peroxide J. Biol. Chem. 264 1989 1729 1734
    • (1989) J. Biol. Chem. , vol.264 , pp. 1729-1734
    • Sagripant, J.L.1    Kraemer, K.H.2
  • 46
    • 0024788706 scopus 로고
    • Carnosine, homocarnosine and anserine: Could they act as antioxidants in vivo?
    • Aruoma O.I., Laughton M.J., and Halliwell B. Carnosine, homocarnosine and anserine: could they act as antioxidants in vivo? Biochem. J. 264 1989 863 869
    • (1989) Biochem. J. , vol.264 , pp. 863-869
    • Aruoma, O.I.1    Laughton, M.J.2    Halliwell, B.3
  • 47
    • 0023776655 scopus 로고
    • Antioxidative properties of histidine-containing dipeptides from skeletal muscles of vertebrates
    • Boldyrev A.A., Dupin A.M., Pindel E.V., and Severin S.E. Antioxidative properties of histidine-containing dipeptides from skeletal muscles of vertebrates Comp. Biochem. Physiol. B 89 1988 245 250
    • (1988) Comp. Biochem. Physiol. B , vol.89 , pp. 245-250
    • Boldyrev, A.A.1    Dupin, A.M.2    Pindel, E.V.3    Severin, S.E.4
  • 48
    • 33751392063 scopus 로고
    • Differences in the antioxidant mechanism of carnosine in the presence of copper and iron
    • Decker E.A., Crum A.D., and Calvert J.T. Differences in the antioxidant mechanism of carnosine in the presence of copper and iron J. Agric. Food Chem. 40 1992 756 759
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 756-759
    • Decker, E.A.1    Crum, A.D.2    Calvert, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.