메뉴 건너뛰기




Volumn 1774, Issue 9, 2007, Pages 1118-1127

Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126

Author keywords

Apoptosis; Electroretinography; Oligomers; Oxidation; Prion peptide; Protofibrils

Indexed keywords

AMINO ACID; AMYLOID; METHIONINE; OLIGOMER; PRION PROTEIN; PROTEINASE K;

EID: 34548317095     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.06.016     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 0030478022 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of prion diseases
    • Prusiner S.B. Molecular biology and pathogenesis of prion diseases. Trends Biochem. Sci. 21 (1996) 482-487
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 482-487
    • Prusiner, S.B.1
  • 4
    • 0034711254 scopus 로고    scopus 로고
    • In vivo cytotoxicity of the prion protein fragment 106-126
    • Ettaiche M., Pichot R., Vincent J.P., and Chabry J. In vivo cytotoxicity of the prion protein fragment 106-126. J. Biol. Chem. 275 (2000) 36487-36490
    • (2000) J. Biol. Chem. , vol.275 , pp. 36487-36490
    • Ettaiche, M.1    Pichot, R.2    Vincent, J.P.3    Chabry, J.4
  • 7
    • 0037380980 scopus 로고    scopus 로고
    • Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic
    • Florio T., Paludi D., Villa V., Principe D.R., Corsaro A., Millo E., Damonte G., D'Arrigo C., Russo C., Schettini G., and Aceto A. Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J. Neurochem. 85 (2003) 62-72
    • (2003) J. Neurochem. , vol.85 , pp. 62-72
    • Florio, T.1    Paludi, D.2    Villa, V.3    Principe, D.R.4    Corsaro, A.5    Millo, E.6    Damonte, G.7    D'Arrigo, C.8    Russo, C.9    Schettini, G.10    Aceto, A.11
  • 8
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • Brown D.R., Schmidt B., and Kretzschmar H.A. Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380 (1996) 345-347
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 10
    • 0037439629 scopus 로고    scopus 로고
    • In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression
    • Chabry J., Ratsimanohatra C., Sponne I., Elena P.P., Vincent J.P., and Pillot T. In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. J. Neurosci. 23 (2003) 462-469
    • (2003) J. Neurosci. , vol.23 , pp. 462-469
    • Chabry, J.1    Ratsimanohatra, C.2    Sponne, I.3    Elena, P.P.4    Vincent, J.P.5    Pillot, T.6
  • 14
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R., Sokolov Y., Edmonds B., McIntire T.M., Milton S.C., Hall J.E., and Glabe C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279 (2004) 46363-46366
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 15
    • 11844286389 scopus 로고    scopus 로고
    • Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer
    • Masel J., Genoud N., and Aguzzi A. Efficient inhibition of prion replication by PrP-Fc(2) suggests that the prion is a PrP(Sc) oligomer. J. Mol. Biol. 345 (2005) 1243-1251
    • (2005) J. Mol. Biol. , vol.345 , pp. 1243-1251
    • Masel, J.1    Genoud, N.2    Aguzzi, A.3
  • 16
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V., Bocharova O.V., Bronstein I., and Baskakov I.V. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281 (2006) 13828-13836
    • (2006) J. Biol. Chem. , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 17
    • 0036167055 scopus 로고    scopus 로고
    • Structure and location of amyloid beta peptide chains and arrays in Alzheimer's disease: new findings require reevaluation of the amyloid hypothesis and of tests of the hypothesis
    • Rosenblum W.I. Structure and location of amyloid beta peptide chains and arrays in Alzheimer's disease: new findings require reevaluation of the amyloid hypothesis and of tests of the hypothesis. Neurobiol. Aging 23 (2002) 225-230
    • (2002) Neurobiol. Aging , vol.23 , pp. 225-230
    • Rosenblum, W.I.1
  • 19
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration
    • Walsh D.M., and Selkoe D.J. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11 (2004) 213-228
    • (2004) Protein Pept. Lett. , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 20
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury Jr. P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 571-576
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury Jr., P.T.6
  • 21
    • 15744402739 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments
    • Cole N.B., Murphy D.D., Lebowitz J., Di Noto L., Levine R.L., and Nussbaum R.L. Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments. J. Biol. Chem. 280 (2005) 9678-9690
    • (2005) J. Biol. Chem. , vol.280 , pp. 9678-9690
    • Cole, N.B.1    Murphy, D.D.2    Lebowitz, J.3    Di Noto, L.4    Levine, R.L.5    Nussbaum, R.L.6
  • 22
    • 9144274018 scopus 로고    scopus 로고
    • Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein
    • Hokenson M.J., Uversky V.N., Goers J., Yamin G., Munishkina L.A., and Fink A.L. Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein. Biochemistry 43 (2004) 4621-4633
    • (2004) Biochemistry , vol.43 , pp. 4621-4633
    • Hokenson, M.J.1    Uversky, V.N.2    Goers, J.3    Yamin, G.4    Munishkina, L.A.5    Fink, A.L.6
  • 23
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 24
    • 33947626638 scopus 로고    scopus 로고
    • Oxidative stress in neurodegenerative disorders
    • Butterfield D.A. Oxidative stress in neurodegenerative disorders. Antioxid. Redox Signal. 8 (2006) 1971-1973
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1971-1973
    • Butterfield, D.A.1
  • 28
    • 7544239102 scopus 로고    scopus 로고
    • Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers
    • Heegaard P.M., Pedersen H.G., Flink J., and Boas U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. FEBS Lett. 577 (2004) 127-133
    • (2004) FEBS Lett. , vol.577 , pp. 127-133
    • Heegaard, P.M.1    Pedersen, H.G.2    Flink, J.3    Boas, U.4
  • 29
    • 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. Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching?. Biochemistry 37 (1998) 12700-12706
    • (1998) Biochemistry , vol.37 , pp. 12700-12706
    • Watson, A.A.1    Fairlie, D.P.2    Craik, D.J.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. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517 (2002) 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
  • 33
    • 20744456278 scopus 로고    scopus 로고
    • Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro
    • Bergstrom A.L., Cordes H., Zsurger N., Heegaard P.M., Laursen H., and Chabry J. Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro. J. Biol. Chem. 280 (2005) 23114-23121
    • (2005) J. Biol. Chem. , vol.280 , pp. 23114-23121
    • Bergstrom, A.L.1    Cordes, H.2    Zsurger, N.3    Heegaard, P.M.4    Laursen, H.5    Chabry, J.6
  • 36
    • 0029964280 scopus 로고    scopus 로고
    • Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, A beta 25-35
    • Hope J., Shearman M.S., Baxter H.C., Chong A., Kelly S.M., and Price N.C. Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, A beta 25-35. Neurodegeneration 5 (1996) 1-11
    • (1996) Neurodegeneration , vol.5 , pp. 1-11
    • Hope, J.1    Shearman, M.S.2    Baxter, H.C.3    Chong, A.4    Kelly, S.M.5    Price, N.C.6
  • 40
    • 0033980694 scopus 로고    scopus 로고
    • Prion protein peptides: optimal toxicity and peptide blockade of toxicity
    • Brown D.R. Prion protein peptides: optimal toxicity and peptide blockade of toxicity. Mol. Cell. Neurosci. 15 (2000) 66-78
    • (2000) Mol. Cell. Neurosci. , vol.15 , pp. 66-78
    • Brown, D.R.1
  • 41
    • 0345598918 scopus 로고    scopus 로고
    • NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126
    • Kuwata K., Matumoto T., Cheng H., Nagayama K., James T.L., and Roder H. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14790-14795
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14790-14795
    • Kuwata, K.1    Matumoto, T.2    Cheng, H.3    Nagayama, K.4    James, T.L.5    Roder, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.