메뉴 건너뛰기




Volumn 99, Issue 1, 2006, Pages 226-236

Copper-dependent inhibition of cytochrome c oxidase by Aβ 1-42 requires reduced methionine at residue 35 of the Aβ peptide

Author keywords

Alzheimer's disease; Amyloid ; Copper; Cytochrome c oxidase; Methionine 35; Mitochondria

Indexed keywords

ALANINE; AMYLOID BETA PROTEIN[1-42]; CATALASE; COPPER; CYTOCHROME C OXIDASE; DODECYL SULFATE SODIUM; HYDROGEN PEROXIDE; METHIONINE; SULFOXIDE; SULFUR; TYROSINE; VALINE;

EID: 33748684352     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.04050.x     Document Type: Article
Times cited : (45)

References (50)
  • 1
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer β-amyloid peptide 1-42: A membrane-disrupting peptide
    • Ambroggio E. E., Kim D. H., Separovic F., Barrow C. J., Barnham K. J., Bagatolli L. A. and Fidelio G. D. (2005) Surface behavior and lipid interaction of Alzheimer β-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys. J. 88, 2706-2713.
    • (2005) Biophys. J. , vol.88 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3    Barrow, C.J.4    Barnham, K.J.5    Bagatolli, L.A.6    Fidelio, G.D.7
  • 2
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada H. K., Biswas G., Robin M.-A. and Avadhani N. G. (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
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.-A.3    Avadhani, N.G.4
  • 4
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β1-42
    • Atwood C. S., Scarpa R. C., Huang X., Moir R. D., Jones W. D., Fairlie D. P., Tanzi R. E. and Bush A. I. (2000) Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β1-42. J. Neurochem. 75, 1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 5
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β
    • Atwood C. S., Perry G., Zeng H. et al. (2004) Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β. Biochemistry 43, 560-568.
    • (2004) Biochemistry , vol.43 , pp. 560-568
    • Atwood, C.S.1    Perry, G.2    Zeng, H.3
  • 6
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation
    • Barnham K. J., Ciccotosto G. D., Tickler A. K. et al. (2003) Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278, 42 959-42 965.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42959-42965
    • Barnham, K.J.1    Ciccotosto, G.D.2    Tickler, A.K.3
  • 7
    • 9444284334 scopus 로고    scopus 로고
    • Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid
    • Barnham K. J., Haeffner F., Ciccotosto G. D. et al. (2004) Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid. FASEB J. 18, 1427-1429.
    • (2004) FASEB J. , vol.18 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3
  • 8
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J. B., Lesley R. and Schubert D. (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77, 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 9
    • 2942672221 scopus 로고    scopus 로고
    • Rapid photochemical cross-linking - A new tool for studies of metastable, amyloidogenic protein assemblies
    • Bitan G. and Teplow D. B. (2004) Rapid photochemical cross-linking - a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 37, 357-364.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 10
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan G., Lomakin A. and Teplow D. B. (2001) Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35 176-35 184.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 11
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid β-protein oligomerization
    • Bitan G., Vollers S. S. and Teplow D. B. (2003a) Elucidation of primary structure elements controlling early amyloid β-protein oligomerization. J. Biol. Chem. 278, 34 882-34 889.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 13
    • 12844266117 scopus 로고    scopus 로고
    • The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity
    • Butterfield D. A. and Boyd-Kimball D. (2005) The critical role of methionine 35 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim. Biophys. Acta 1703, 149-156.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 149-156
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 14
    • 0032810909 scopus 로고    scopus 로고
    • β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari L., Clark J. B. and Bates T. E. (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
  • 15
    • 0036272650 scopus 로고    scopus 로고
    • Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley C. S., Canevari L., Land J. M., Clark J. B. and Sharpe M. A. (2002) 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
  • 18
    • 0035943058 scopus 로고    scopus 로고
    • Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD
    • Cottrell D. A., Blakely E. L., Johnson M. A., Ince P. G. and Turnbull D. M. (2001) Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD. Neurology 57, 260-264.
    • (2001) Neurology , vol.57 , pp. 260-264
    • Cottrell, D.A.1    Blakely, E.L.2    Johnson, M.A.3    Ince, P.G.4    Turnbull, D.M.5
  • 21
    • 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 C. C., Ali F., Volitakis I., Cherny R. A., Norton R. S., Beyreuther K., Barrow C. J., Masters C. L., Bush A. I. and Barnham K. J. (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, 20 466-20 473.
    • (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
  • 22
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky S. T. and Scheff S. W. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol. 27, 457-464.
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 24
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • Fancy D. A. and 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
  • 25
    • 19944373389 scopus 로고    scopus 로고
    • Nicastrin, presenilin, APH-1 and PEN-2 form active γ-secretase complexes in mitochondria
    • Hansson C. A., Frykman S., Farmery M. R. et al. (2004) Nicastrin, presenilin, APH-1 and PEN-2 form active γ-secretase complexes in mitochondria. J. Biol. Chem. 279, 51 654-51 660.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51654-51660
    • Hansson, C.A.1    Frykman, S.2    Farmery, M.R.3
  • 26
    • 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. and Rapoport S. I. (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
  • 27
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai K., Aliev G., Nunomura A. et al. (2001) Mitochondrial abnormalities in Alzheimer's disease. J. Neurosci. 21, 3017-3023.
    • (2001) J. Neurosci. , vol.21 , pp. 3017-3023
    • Hirai, K.1    Aliev, G.2    Nunomura, A.3
  • 29
    • 18344414746 scopus 로고    scopus 로고
    • The A beta peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang X., Atwood C. S., Hartshorn M. A. et al. (1999a) The A beta peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38, 7609-7616.
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3
  • 30
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of Alzheimer Aβ neurotoxicity: Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang X., Cuajungco M. P., Atwood C. S. et al. (1999b) Cu(II) potentiation of Alzheimer Aβ neurotoxicity: Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274, 37 111-37 116.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37111-37116
    • Huang, X.1    Cuajungco, M.P.2    Atwood, C.S.3
  • 31
    • 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 C. L. and 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, 22 908-22 914.
    • (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
  • 32
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide
    • Kanski J., Aksenova M., Schoneich C. and Butterfield D. A. (2002) Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide. Free Radic. Biol. Med. 32, 1205-1211.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1205-1211
    • Kanski, J.1    Aksenova, M.2    Schoneich, C.3    Butterfield, D.A.4
  • 33
    • 0242362596 scopus 로고    scopus 로고
    • 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 S. S., Aguilar M.-I., Martin L. L. and Small D. H. (2003) b-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
  • 36
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M., Anekonda T. S., Henson E., Park B. S., Quinn J. and Reddy P. H. (2006) Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437-1449.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 37
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
    • Maurer I., Zierz S. and Moller H. J. (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
    • 2942631225 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid beta-protein fragment (31-35) on isolated brain mitochondria
    • Misiti F., Martorana G. E., Nocca G., Di Stasio E., Giardina B. and Clementi M. E. (2004) Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid beta-protein fragment (31-35) on isolated brain mitochondria. Neuroscience 126, 297-303.
    • (2004) Neuroscience , vol.126 , pp. 297-303
    • Misiti, F.1    Martorana, G.E.2    Nocca, G.3    Di Stasio, E.4    Giardina, B.5    Clementi, M.E.6
  • 39
    • 0032014429 scopus 로고    scopus 로고
    • Effects of β-amyloid peptides on the fluidity of membranes from frontal and parietal lobes of human brain. High potencies of Aβ 1-42 and Aβ 1-43
    • Muller W. E., Eckert G. P., Scheuer K., Cairns N. J., Maras A. and Gattaz W. F. (1998) Effects of β-amyloid peptides on the fluidity of membranes from frontal and parietal lobes of human brain. High potencies of Aβ 1-42 and Aβ 1-43. Amyloid 5, 10-15.
    • (1998) Amyloid , vol.5 , pp. 10-15
    • Muller, W.E.1    Eckert, G.P.2    Scheuer, K.3    Cairns, N.J.4    Maras, A.5    Gattaz, W.F.6
  • 40
    • 27544511750 scopus 로고    scopus 로고
    • Formation and stabilization model of the 42-mer Abeta radical: Implications for the long-lasting oxidative stress in Alzheimer's disease
    • Murakami K., Irie K., Ohigashi H., Hara H., Nagao M., Shimizu T. and Shirasawa T. (2005) Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease. J. Am. Chem. Soc. 127, 15 168-15 174.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15168-15174
    • Murakami, K.1    Irie, K.2    Ohigashi, H.3    Hara, H.4    Nagao, M.5    Shimizu, T.6    Shirasawa, T.7
  • 42
    • 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 J. K., Smith T. S., Trimmer P. A., Bennett J. P. J. and Parker W. D. J. (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
  • 43
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson J. L. (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
  • 44
    • 0037082115 scopus 로고    scopus 로고
    • Redox processes of methionine relevant to betaamyloid oxidation and Alzheimer's disease
    • Schoneich C. (2002) Redox processes of methionine relevant to betaamyloid oxidation and Alzheimer's disease. Arch. Biochem. Biophys. 397, 370-376.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 370-376
    • Schoneich, C.1
  • 45
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology
    • Seilheimer B., Bohrmann B., Bondolfi L., Muller F., Stuber D. and Dobeli H. (1997) The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119, 59-71.
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 46
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid beta-protein and the genetics of Alzheimer's disease
    • Selkoe D. J. (1996) Amyloid beta-protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271, 18 295-18 298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 48
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce I. A., Kim Y. L., Jun A. S. and Wallace D. C. (1996) Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Meth. Enzymol. 264, 484-509.
    • (1996) Meth. Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 49
    • 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 D. C., Yang J., Ye J., Lott M. T., Oliver N. A. and 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
  • 50
    • 0032530953 scopus 로고    scopus 로고
    • Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching?
    • Watson A. A., Fairlie D. P. and Craik D. J. (1998) Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching? Biochemistry 37, 12 700-12 706.
    • (1998) Biochemistry , vol.37 , pp. 12700-12706
    • Watson, A.A.1    Fairlie, D.P.2    Craik, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.