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Volumn 25, Issue 3, 2005, Pages 672-679

Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-β1-42

Author keywords

Alzheimer's disease; Amyloid ; Copper; Cytochrome oxidase; Mitochondria; Tg2576

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; COPPER; CYTOCHROME C OXIDASE;

EID: 19944433571     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4276-04.2005     Document Type: Article
Times cited : (300)

References (46)
  • 1
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandalheerlhavarada HK, Biswas G, Robin M-A, Avadhani NG (2003) Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 161:41-54.
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandalheerlhavarada, H.K.1    Biswas, G.2    Robin, M.-A.3    Avadhani, N.G.4
  • 2
    • 0034057202 scopus 로고    scopus 로고
    • Improved recovery of highly enriched mitochondrial fractions from small brain tissue samples
    • Anderson MF, Sims NR (2000) Improved recovery of highly enriched mitochondrial fractions from small brain tissue samples. Brain Res Protoc 5:95-101.
    • (2000) Brain Res Protoc , vol.5 , pp. 95-101
    • Anderson, M.F.1    Sims, N.R.2
  • 5
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G, Lomakin A, Teplow DB (2001) Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276:35176-35184.
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 6
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid β-protein oligomerization
    • Bitan G, Vollers SS, Teplow DB (2003a) Elucidation of primary structure elements controlling early amyloid β-protein oligomerization. J Biol Chem 278:34882-34889.
    • (2003) J Biol Chem , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 8
    • 0032810909 scopus 로고    scopus 로고
    • β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari L, Clark JB, Bates TE (1999) β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett 457:131-134.
    • (1999) FEBS Lett , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 9
    • 0036272650 scopus 로고    scopus 로고
    • β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA (2002a) β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 80:91-100.
    • (2002) J Neurochem , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 14
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain CC, Ali F, Volitakis I, Cherny RA, Norton RS, Beyreuther K, Barrow CJ, Masters CL, Bush AI, Barnham KJ (2001) Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J Biol Chem 276:20466-20473.
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 15
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WBJ, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J Biol Chem 277:32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.J.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 18
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • Fancy DA, Kodadek T (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light. Proc Natl Acad Sci USA 96:6020-6024.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 19
    • 0033045848 scopus 로고    scopus 로고
    • In vitro peroxidase oxidation induces stable dimers of beta-amyloid (1-42) through dityrosine bridge formation
    • Galeazzi L, Ronchi P, Franceschi C, Giunta S (1999) In vitro peroxidase oxidation induces stable dimers of beta-amyloid (1-42) through dityrosine bridge formation. Amyloid 6:7-13.
    • (1999) Amyloid , vol.6 , pp. 7-13
    • Galeazzi, L.1    Ronchi, P.2    Franceschi, C.3    Giunta, S.4
  • 21
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 22
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19:8876-8884.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 23
    • 0023860708 scopus 로고
    • The iron(III)-adriamycin complex inhibits cytochrome c oxidase before its inactivation
    • Hasinoff BB, Davey P (1988) The iron(III)-adriamycin complex inhibits cytochrome c oxidase before its inactivation. Biochem J 250:827-834.
    • (1988) Biochem J , vol.250 , pp. 827-834
    • Hasinoff, B.B.1    Davey, P.2
  • 24
    • 0022523469 scopus 로고
    • Neocortical metabolic abnormalities precede non-memory cognitive deficits in early Alzheimer's type dementia
    • Haxby J, Grady C, Duara R, Schlageter N, Berg G, Rapoport SI (1986) Neocortical metabolic abnormalities precede non-memory cognitive deficits in early Alzheimer's type dementia. Arch Neurol 43:882-885.
    • (1986) Arch Neurol , vol.43 , pp. 882-885
    • Haxby, J.1    Grady, C.2    Duara, R.3    Schlageter, N.4    Berg, G.5    Rapoport, S.I.6
  • 28
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Hartmann T, Pantel J, Schroder J, Zerfass R, Forstl H, Sandbrink R, Masters CL, Beyreuther K (1996) Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem 271:22908-22914.
    • (1996) J Biol Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 30
    • 0242362596 scopus 로고    scopus 로고
    • β-Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
    • Klug G, Losic D, Subasinghe SS, Aguilar M-I, Martin LL, Small DH (2003) β-Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH. Eur J Biochem 270:4282-4293.
    • (2003) Eur J Biochem , vol.270 , pp. 4282-4293
    • Klug, G.1    Losic, D.2    Subasinghe, S.S.3    Aguilar, M.-I.4    Martin, L.L.5    Small, D.H.6
  • 34
    • 0022480081 scopus 로고
    • Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress
    • Martins RN, Harper CG, Stokes GB, Masters CL (1986) Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress. J Neurochem 46:1042-1045.
    • (1986) J Neurochem , vol.46 , pp. 1042-1045
    • Martins, R.N.1    Harper, C.G.2    Stokes, G.B.3    Masters, C.L.4
  • 35
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer I, Zierz S, Moller HJ (2000) A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients. Neurobiol Aging 21:455-462.
    • (2000) Neurobiol Aging , vol.21 , pp. 455-462
    • Maurer, I.1    Zierz, S.2    Moller, H.J.3
  • 38
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Naslund J, Haroutunian V, Mohs R, Davis KL, Davies P, Greenard P, Buxbaum JD (2000) Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283:1571-1577.
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greenard, P.6    Buxbaum, J.D.7
  • 39
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Aβ peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • Parks JK, Smith TS, Trimmer PA, Bennett JPJ, Parker WDJ (2001) Neurotoxic Aβ peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro. J Neurochem 76:1050-1056.
    • (2001) J Neurochem , vol.76 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.J.4    Parker, W.D.J.5
  • 40
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson JL (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346-356.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, J.L.1
  • 41
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991) Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Euro J Pharmacol 207:367-368.
    • (1991) Euro J Pharmacol , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 42
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 43
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce IA, Kim YL, Jun AS, Wallace DC (1996) Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Methods Enzymol 264:484-509.
    • (1996) Methods Enzymol , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 44
    • 0022653494 scopus 로고
    • Computer prediction of peptide maps: Assignment of polypeptides to human and mouse mitochondrial DNA genes by analysis of two-dimensional-proteolytic digest gels
    • Wallace DC, Yang J, Ye J, Lott MT, Oliver NA, McCarthy J (1986) Computer prediction of peptide maps: assignment of polypeptides to human and mouse mitochondrial DNA genes by analysis of two-dimensional-proteolytic digest gels. Am J Hum Genet 38:461-481.
    • (1986) Am J Hum Genet , vol.38 , pp. 461-481
    • Wallace, D.C.1    Yang, J.2    Ye, J.3    Lott, M.T.4    Oliver, N.A.5    McCarthy, J.6
  • 45


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.