메뉴 건너뛰기




Volumn 47, Issue 38, 2008, Pages 10208-10217

Methionine oxidation inhibits assembly and promotes disassembly of apolipoprotein C-II amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL OXYGEN DEMAND; DISSOCIATION; GLYCOPROTEINS; HYDROGEN; HYDROGEN PEROXIDE; NONMETALS; SELF ASSEMBLED MONOLAYERS; SYSTEM STABILITY;

EID: 52249123646     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8009339     Document Type: Article
Times cited : (38)

References (56)
  • 2
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt, W. (1995) Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radical Biol. Med. 18, 93-105.
    • (1995) Free Radical Biol. Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 3
    • 0037063326 scopus 로고    scopus 로고
    • Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: HCBS1
    • Jung, S., Hansel, A., Kasperczyk, H., Hoshi, T., and Heinemann, S. H. (2002) Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett. 527, 91-94.
    • (2002) FEBS Lett , vol.527 , pp. 91-94
    • Jung, S.1    Hansel, A.2    Kasperczyk, H.3    Hoshi, T.4    Heinemann, S.H.5
  • 4
    • 0032770232 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)
    • Kuschel, L., Hansel, A., Schonherr, R., Weissbach, H., Brot, N., Hoshi, T., and Heinemann, S. H. (1999) Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett. 456, 17-21.
    • (1999) FEBS Lett , vol.456 , pp. 17-21
    • Kuschel, L.1    Hansel, A.2    Schonherr, R.3    Weissbach, H.4    Brot, N.5    Hoshi, T.6    Heinemann, S.H.7
  • 5
    • 34249692347 scopus 로고    scopus 로고
    • Methionine sulfoxide reduction and the aging process
    • Koc, A., and Gladyshev, V. N. (2007) Methionine sulfoxide reduction and the aging process. Ann. N. Y. Acad. Sci. 1100, 383-386.
    • (2007) Ann. N. Y. Acad. Sci , vol.1100 , pp. 383-386
    • Koc, A.1    Gladyshev, V.N.2
  • 8
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity
    • Taggart, C., Cervantes-Laurean, D., Kim, G., McElvaney, N. G., Wehr, N., Moss, J., and Levine, R. L. (2000) Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity. J. Biol. Chem. 275, 27258-27265.
    • (2000) J. Biol. Chem , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3    McElvaney, N.G.4    Wehr, N.5    Moss, J.6    Levine, R.L.7
  • 9
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • Butterfield, D. A., Drake, J., Pocernich, C., and Castegna, A. (2001) Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 7, 548-554.
    • (2001) Trends Mol. Med , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 10
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 12
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape
    • Dobson, C. M. (2002) Getting out of shape. Nature 418, 729-730.
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 13
    • 0026771089 scopus 로고
    • Amyloidosis
    • Sipe, J. D. (1992) Amyloidosis. Annu. Rev. Biochem. 61, 947-975.
    • (1992) Annu. Rev. Biochem , vol.61 , pp. 947-975
    • Sipe, J.D.1
  • 14
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. (2003) Folding proteins in fatal ways. Nature 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 15
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (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
  • 16
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 17
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, L., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, L.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 18
    • 0034233474 scopus 로고    scopus 로고
    • Oxidative processes in Alzheimer's disease: The role of abeta-metal interactions
    • Lynch, T., Cherny, R. A., and Bush, A. I. (2000) Oxidative processes in Alzheimer's disease: the role of abeta-metal interactions. Exp. Gerontol. 35, 445-451.
    • (2000) Exp. Gerontol , vol.35 , pp. 445-451
    • Lynch, T.1    Cherny, R.A.2    Bush, A.I.3
  • 19
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radical Biol. Med. 23, 134-147.
    • (1997) Free Radical Biol. Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 20
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid beta peptide
    • Smith, D. G., Cappai, R., and Barnham, K. J. (2007) The redox chemistry of the Alzheimer's disease amyloid beta peptide. Biochim. Biophys. Acta 1768, 1976-1990.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 22
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita, S. P., Aksenov, M. Y., Lovell, M. A., and Markesbery, W. R. (1999) Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 73, 1660-1666.
    • (1999) J. Neurochem , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 26
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar, A. P., Dubay, K. F., Zurdo, J., Chiti, F., Vendruscolo, M., and Dobson, C. M. (2005) Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350, 379-392.
    • (2005) J. Mol. Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 27
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease
    • Hou, L., Kang, I., Marchant, R. E., and Zagorski, M. G. (2002) Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 277, 40173-40176.
    • (2002) J. Biol. Chem , vol.277 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 28
    • 28244486826 scopus 로고    scopus 로고
    • Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
    • Breydo, L., Bocharova, O. V., Makarava, N., Salnikov, V. V., Anderson, M., and Baskakov, I. V. (2005) Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry 44, 15534-15543.
    • (2005) Biochemistry , vol.44 , pp. 15534-15543
    • Breydo, L.1    Bocharova, O.V.2    Makarava, N.3    Salnikov, V.V.4    Anderson, M.5    Baskakov, I.V.6
  • 29
    • 33751112217 scopus 로고    scopus 로고
    • Oxidation inhibits amyloid fibril formation of transthyretin
    • Maleknia, S. D., Reixach, N., and Buxbaum, J. N. (2006) Oxidation inhibits amyloid fibril formation of transthyretin. FEBS J. 273, 5400-5406.
    • (2006) FEBS J , vol.273 , pp. 5400-5406
    • Maleknia, S.D.1    Reixach, N.2    Buxbaum, J.N.3
  • 30
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro
    • Uversky, V. N., Yamin, G., Souillac, P. O., Goers, J., Glaser, C. B., and Fink, A. L. (2002) Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517, 239-244.
    • (2002) FEBS Lett , vol.517 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 31
    • 12944255705 scopus 로고    scopus 로고
    • Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease
    • Collinge, J., Beck, J., Campbell, T., Estibeiro, K., and Will, R. G. (1996) Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease. Lancet 348, 356.
    • (1996) Lancet , vol.348 , pp. 356
    • Collinge, J.1    Beck, J.2    Campbell, T.3    Estibeiro, K.4    Will, R.G.5
  • 33
    • 34548317095 scopus 로고    scopus 로고
    • Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126
    • Bergstrom, A. L., Chabry, J., Bastholm, L., and Heegaard, P. M. (2007) Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126. Biochim. Biophys. Acta 1774, 1118-1127.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1118-1127
    • Bergstrom, A.L.1    Chabry, J.2    Bastholm, L.3    Heegaard, P.M.4
  • 36
    • 0034682559 scopus 로고    scopus 로고
    • Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops
    • Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., and Howlett, G. J. (2000) Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops. Biochemistry 39, 8276-8283.
    • (2000) Biochemistry , vol.39 , pp. 8276-8283
    • Hatters, D.M.1    MacPhee, C.E.2    Lawrence, L.J.3    Sawyer, W.H.4    Howlett, G.J.5
  • 37
    • 39049110070 scopus 로고    scopus 로고
    • Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining
    • Binger, K. J., Pham, C. L., Wilson, L. M., Bailey, M. F., Lawrence, L. J., Schuck, P., and Howlett, G. J. (2008) Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining. J. Mol. Biol. 376, 1116-1129.
    • (2008) J. Mol. Biol , vol.376 , pp. 1116-1129
    • Binger, K.J.1    Pham, C.L.2    Wilson, L.M.3    Bailey, M.F.4    Lawrence, L.J.5    Schuck, P.6    Howlett, G.J.7
  • 38
    • 0030590244 scopus 로고    scopus 로고
    • Isolation and characterization of recombinant human apolipoprotein C-II expressed in Escherichia coli
    • Wang, C. S., Downs, D., Dashti, A., and Jackson, K. W. (1996) Isolation and characterization of recombinant human apolipoprotein C-II expressed in Escherichia coli. Biochim. Biophys. Acta 1302, 224-230.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 224-230
    • Wang, C.S.1    Downs, D.2    Dashti, A.3    Jackson, K.W.4
  • 40
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 41
    • 0037380769 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of flexible macromolecules: Self-association and tangling of amyloid fibrils
    • MacRaild, C. A., Hatters, D. M., Lawrence, L. J., and Howlett, G. J. (2003) Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils. Biophys. J. 84, 2562-2569.
    • (2003) Biophys. J , vol.84 , pp. 2562-2569
    • MacRaild, C.A.1    Hatters, D.M.2    Lawrence, L.J.3    Howlett, G.J.4
  • 42
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck, P., and Rossmanith, P. (2000) Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54, 328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 46
    • 25444522601 scopus 로고    scopus 로고
    • Thermodynamics of abeta(1-40) amyloid fibril elongation
    • O'Nuallain, B., Shivaprasad, S., Kheterpal, I., and Wetzel, R. (2005) Thermodynamics of abeta(1-40) amyloid fibril elongation. Biochemistry 44, 12709-12718.
    • (2005) Biochemistry , vol.44 , pp. 12709-12718
    • O'Nuallain, B.1    Shivaprasad, S.2    Kheterpal, I.3    Wetzel, R.4
  • 48
    • 33846014251 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state
    • Abdul Latif, A. R., Kono, R., Tachibana, H., and Akasaka, K. (2007) Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state. Biophys. J. 92, 323-329.
    • (2007) Biophys. J , vol.92 , pp. 323-329
    • Abdul Latif, A.R.1    Kono, R.2    Tachibana, H.3    Akasaka, K.4
  • 49
    • 1842519391 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide
    • Butterfield, D. A., and Bush, A. I. (2004) Alzheimer's amyloid beta-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol. Aging 25, 563-568.
    • (2004) Neurobiol. Aging , vol.25 , pp. 563-568
    • Butterfield, D.A.1    Bush, A.I.2
  • 50
    • 0027389112 scopus 로고
    • Modifications of transthyretin in amyloid fibrils: Analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation
    • Thylen, C., Wahlqvist, J., Haettner, E., Sandgren, O., Holmgren, G., and Lundgren, E. (1993) Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation. EMBO J. 12, 743-748.
    • (1993) EMBO J , vol.12 , pp. 743-748
    • Thylen, C.1    Wahlqvist, J.2    Haettner, E.3    Sandgren, O.4    Holmgren, G.5    Lundgren, E.6
  • 52
    • 33947390936 scopus 로고    scopus 로고
    • Attenuated cytotoxicity but enhanced betafibril of a mutant amyloid beta-peptide with a methionine to cysteine substitution
    • Dai, X. L., Sun, Y. X., and Jiang, Z. F. (2007) Attenuated cytotoxicity but enhanced betafibril of a mutant amyloid beta-peptide with a methionine to cysteine substitution. FEBS Lett. 581, 1269-1274.
    • (2007) FEBS Lett , vol.581 , pp. 1269-1274
    • Dai, X.L.1    Sun, Y.X.2    Jiang, Z.F.3
  • 53
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier, T. C. (2001) Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36, 1539-1550.
    • (2001) Exp. Gerontol , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 54
    • 1842504323 scopus 로고    scopus 로고
    • Redox-active metals, oxidative stress, and Alzheimer's disease pathology
    • Huang, X., Moir, R. D., Tanzi, R. E., Bush, A. L, and Rogers, J. T. (2004) Redox-active metals, oxidative stress, and Alzheimer's disease pathology. Ann. N.Y. Acad. Sci. 1012, 153-163.
    • (2004) Ann. N.Y. Acad. Sci , vol.1012 , pp. 153-163
    • Huang, X.1    Moir, R.D.2    Tanzi, R.E.3    Bush, A.L.4    Rogers, J.T.5
  • 55
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R., and Berlett, B. S. (1997) Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10, 485-494.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 56
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • BI8009339
    • Berlett, B. S., and Stadtman, E. R. (1997) Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272, 20313-20316. BI8009339
    • (1997) J. Biol. Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.