메뉴 건너뛰기




Volumn 1025, Issue 1-2, 2004, Pages 29-34

EPR evidence of hydroxyl radical generation as an initiator of lipid peroxidation in amyloid β-protein-stimulated PC12 cells

Author keywords

Amyloid protein; Electron paramagnetic resonance; Hydroxyl radical; Lipid peroxidation; Lipid radical; Spin trapping

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; HYDROGEN; HYDROXYL RADICAL;

EID: 5344268096     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2004.07.067     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0037363169 scopus 로고    scopus 로고
    • Identification of the hydroxyl radical and other reactive oxygen species in human neutrophil granulocytes exposed to a fragment of the amyloid beta peptide
    • J.M. Andersen, O. Myhre, H. Aarnes, T.A. Vestad, and F. Fonnum Identification of the hydroxyl radical and other reactive oxygen species in human neutrophil granulocytes exposed to a fragment of the amyloid beta peptide Free Radic. Res. 37 2003 269 279
    • (2003) Free Radic. Res. , vol.37 , pp. 269-279
    • Andersen, J.M.1    Myhre, O.2    Aarnes, H.3    Vestad, T.A.4    Fonnum, F.5
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • C. Behl, J.B. Davis, R. Lesley, and D. Schubert Hydrogen peroxide mediates amyloid beta 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
  • 4
    • 0030921729 scopus 로고    scopus 로고
    • Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: Relevance to Alzheimer's disease
    • D.A. Butterfield, K. Hensley, P. Cole, R. Subramaniam, M. Aksenov, M. Aksenova, P.M. Bummer, B.E. Haley, and J.M. Carney Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer's disease J. Neurochem. 68 1997 2451 2457
    • (1997) J. Neurochem. , vol.68 , pp. 2451-2457
    • Butterfield, D.A.1    Hensley, K.2    Cole, P.3    Subramaniam, R.4    Aksenov, M.5    Aksenova, M.6    Bummer, P.M.7    Haley, B.E.8    Carney, J.M.9
  • 5
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid beta protein precursor
    • X.D. Cai, T.E. Golde, and S.G. Younkin Release of excess amyloid beta protein from a mutant amyloid beta protein precursor Science 259 1993 514 516
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.D.1    Golde, T.E.2    Younkin, S.G.3
  • 8
    • 0022870203 scopus 로고
    • A search for oxygen-centered free radicals in the lipoxygenase/linoleic acid system
    • H.D. Connor, V. Fischer, and R.P. Mason A search for oxygen-centered free radicals in the lipoxygenase/linoleic acid system Biochem. Biophys. Res. Commun. 141 1986 614 621
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 614-621
    • Connor, H.D.1    Fischer, V.2    Mason, R.P.3
  • 9
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • J.R. Connor, B.S. Snyder, J.L. Beard, R.E. Fine, and E.J. Mufson Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease J. Neurosci. Res. 31 1992 327 335
    • (1992) J. Neurosci. Res. , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 10
    • 0033515564 scopus 로고    scopus 로고
    • Amyloid beta peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalyzed oxidation of hydroxylamines to nitroxides
    • S.I. Dikalov, M.P. Vitek, K.R. Maples, and R.P. Mason Amyloid beta peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalyzed oxidation of hydroxylamines to nitroxides J. Biol. Chem. 274 1999 9392 9399
    • (1999) J. Biol. Chem. , vol.274 , pp. 9392-9399
    • Dikalov, S.I.1    Vitek, M.P.2    Maples, K.R.3    Mason, R.P.4
  • 11
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study
    • P.F. Good, D.P. Perl, L.M. Bierer, and J. Schmeidler Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: a laser microprobe (LAMMA) study Ann. Neurol. 31 1992 286 292
    • (1992) Ann. Neurol. , vol.31 , pp. 286-292
    • Good, P.F.1    Perl, D.P.2    Bierer, L.M.3    Schmeidler, J.4
  • 12
    • 0027959041 scopus 로고
    • Nordihydroguaiaretic acid protects hippocampal neurons against amyloid beta-peptide toxicity, and attenuates free radical and calcium accumulation
    • Y. Goodman, M.R. Steiner, S.M. Steiner, and M.P. Mattson Nordihydroguaiaretic acid protects hippocampal neurons against amyloid beta-peptide toxicity, and attenuates free radical and calcium accumulation Brain Res. 654 1994 171 176
    • (1994) Brain Res. , vol.654 , pp. 171-176
    • Goodman, Y.1    Steiner, M.R.2    Steiner, S.M.3    Mattson, M.P.4
  • 13
    • 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?
    • B. Halliwell 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., Suppl. , vol.126 , pp. 23-33
    • Halliwell, B.1
  • 22
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • R.J. Mark, M.A. Lovell, W.R. Markesbery, K. Uchida, and M.P. Mattson A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide J. Neurochem. 68 1997 255 264
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 23
    • 0033600301 scopus 로고    scopus 로고
    • Molecular basis of the neurodegenerative disorders
    • J.B. Martin Molecular basis of the neurodegenerative disorders N. Engl. J. Med. 340 1999 1970 1980
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1970-1980
    • Martin, J.B.1
  • 24
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • M.P. Mattson, and Y. Goodman 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
  • 25
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • M.P. Mattson, B. Cheng, D. Davis, K. Bryant, I. Lieberburg, and R.E. Rydel beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity J. Neurosci. 12 1992 376 389
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 26
    • 0031664973 scopus 로고    scopus 로고
    • Measurement of lipid peroxidation
    • K. Moore, and L.J. Roberts II Measurement of lipid peroxidation Free Radic. Res. 28 1998 659 671
    • (1998) Free Radic. Res. , vol.28 , pp. 659-671
    • Moore, K.1    Roberts II, L.J.2
  • 27
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • G. Multhaup, A. Schlicksupp, L. Hesse, D. Beher, T. Ruppert, C.L. Masters, and K. Beyreuther 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
  • 28
    • 0345035452 scopus 로고    scopus 로고
    • Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein
    • F.H. Ruiz, M. Gonzalez, M. Bodini, C. Opazo, and N.C. Inestrosa Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein J. Neurochem. 73 1999 1288 1292
    • (1999) J. Neurochem. , vol.73 , pp. 1288-1292
    • Ruiz, F.H.1    Gonzalez, M.2    Bodini, M.3    Opazo, C.4    Inestrosa, N.C.5
  • 29
    • 0031066614 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis
    • M.A. Smith, and G. Perry The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis J. Neuropathol. Exp. Neurol. 56 1997 217
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 217
    • Smith, M.A.1    Perry, G.2
  • 31
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • B.A. Yankner, L.K. Duffy, and D.A. Kirschner Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides Science 250 1990 279 282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 32
    • 0033050773 scopus 로고    scopus 로고
    • Identification of a heparin binding site and the biological activities of the laminin alpha1 chain carboxy-terminal globular domain
    • I. Yoshida, K. Tashiro, A. Monji, I. Nagata, Y. Hayashi, Y. Mitsuyama, and N. Tashiro Identification of a heparin binding site and the biological activities of the laminin alpha1 chain carboxy-terminal globular domain J. Cell. Physiol. 179 1999 18 28
    • (1999) J. Cell. Physiol. , vol.179 , pp. 18-28
    • Yoshida, I.1    Tashiro, K.2    Monji, A.3    Nagata, I.4    Hayashi, Y.5    Mitsuyama, Y.6    Tashiro, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.