메뉴 건너뛰기




Volumn 60, Issue 16, 2012, Pages 4144-4155

Methionine oxidation enhances κ-casein amyloid fibril formation

Author keywords

amyloid fibril; casein proteins; methionine; oxidation

Indexed keywords

ALZHEIMER'S DISEASE; AMORPHOUS AGGREGATION; AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; CASEIN MICELLES; CELLULAR TOXICITIES; DISORDERED STRUCTURES; EXTRACELLULAR; FIBRIL FORMATION; IN-VITRO; METHIONINE; METHIONINE OXIDATION; METHIONINE RESIDUES; MILK PROTEIN; OXIDIZING ENVIRONMENTS; PHYSIOLOGICAL CONDITION; PROTEIN MISFOLDING; PROTEIN OXIDATION; SURFACE HYDROPHOBICITY; TARGET PROTEINS;

EID: 84860336481     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf205168t     Document Type: Article
Times cited : (29)

References (40)
  • 1
    • 0002772383 scopus 로고
    • Chemistry of caseins
    • Fox, P. F. Ed. Elsevier Applied Science: London
    • Swaisgood, H. E. Chemistry of caseins. In Advanced Dairy Chemistry-1: Proteins; Fox, P. F., Ed. Elsevier Applied Science: London, 1992; pp 139-201.
    • (1992) Advanced Dairy Chemistry-1: Proteins , pp. 139-201
    • Swaisgood, H.E.1
  • 2
    • 27144501029 scopus 로고    scopus 로고
    • Milk proteins: General and historical aspects
    • 3rd ed. Fox, P. F. McSweeney, P. L. H. Klumer Academic: New York, Vol. -Proteins
    • Fox, P. F.; McSweeney, P. L. H. Milk proteins: General and historical aspects. In Advanced Dairy Chemistry, 3rd ed.; Fox, P. F., McSweeney, P. L. H., Eds.; Klumer Academic: New York, 2003; Vol. 1 -Proteins, pp 1-48.
    • (2003) Advanced Dairy Chemistry , vol.1 , pp. 1-48
    • Fox, P.F.1    McSweeney, P.L.H.2
  • 4
    • 59649108278 scopus 로고    scopus 로고
    • Unraveling the mysteries of protein folding and misfolding
    • Ecroyd, H.; Carver, J. A. Unraveling the mysteries of protein folding and misfolding IUBMB Life 2008, 60, 769-74
    • (2008) IUBMB Life , vol.60 , pp. 769-774
    • Ecroyd, H.1    Carver, J.A.2
  • 5
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T.; Fu, S.; Stocker, R.; Davies, M. J. Biochemistry and pathology of radical-mediated protein oxidation Biochem. J. 1997, 324, 1-18 (Pubitemid 27229359)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 6
    • 0032902974 scopus 로고    scopus 로고
    • Oxidative alterations in Alzheimer's disease
    • Markesbery, W. R.; Carney, J. M. Oxidative alterations in Alzheimer's disease Brain Pathol. 1999, 9, 133-46 (Pubitemid 29056524)
    • (1999) Brain Pathology , vol.9 , Issue.1 , pp. 133-146
    • Markesbery, W.R.1    Carney, J.M.2
  • 7
    • 0015411260 scopus 로고
    • Corpora amylacea of the bovine mammary gland. Histochemical and electron microscopic evidence for their amyloid nature
    • Reid, I. M. Corpora amylacea of the bovine mammary gland. Histochemical and electron microscopic evidence for their amyloid nature J. Comp. Pathol. 1972, 82, 409-13
    • (1972) J. Comp. Pathol. , vol.82 , pp. 409-413
    • Reid, I.M.1
  • 8
    • 0022036350 scopus 로고
    • Prevalence and ultrastructural characteristics of bovine mammary corpora amylacea during the lactation cycle
    • Nickerson, S. C.; Sordillo, L. M.; Boddie, N. T.; Saxton, A. M. Prevalence and ultrastructural characteristics of bovine mammary corpora amylacea during the lactation cycle J. Dairy Sci. 1985, 68, 709-17
    • (1985) J. Dairy Sci. , vol.68 , pp. 709-717
    • Nickerson, S.C.1    Sordillo, L.M.2    Boddie, N.T.3    Saxton, A.M.4
  • 9
    • 0031731462 scopus 로고    scopus 로고
    • Proteic composition of corpora amylacea in the bovine mammary gland
    • DOI 10.1016/S0040-8166(98)80040-2
    • Claudon, C.; Francin, M.; Marchal, E.; Straczeck, J.; Laurent, F.; Nabet, P. Proteic composition of corpora amylacea in the bovine mammary gland Tissue Cell 1998, 30, 589-95 (Pubitemid 28512878)
    • (1998) Tissue and Cell , vol.30 , Issue.5 , pp. 589-595
    • Claudon, C.1    Francin, M.2    Marchal, E.3    Straczeck, J.4    Laurent, F.5    Nabet, P.6
  • 10
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine κ-casein: Reduction and conversion to fibrillar (amyloid) structures
    • DOI 10.1023/A:1025020503769
    • Farrell, H. M., Jr.; Cooke, P. H.; Wickham, E. D.; Piotrowski, E. G.; Hoagland, P. D. Environmental influences on bovine kappa-casein: Reduction and conversion to fibrillar (amyloid) structures J. Prot. Chem. 2003, 22, 259-73 (Pubitemid 37048484)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.3 , pp. 259-273
    • Farrell Jr., H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.G.4    Hoagland, P.D.5
  • 12
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human α-synuclein in vitro
    • DOI 10.1016/S0014-5793(02)02638-8, PII S0014579302026388
    • Uversky, V. N.; Yamin, G.; Souillac, P. O.; Goers, J.; Glaser, C. B.; Fink, A. L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro FEBS Lett. 2002, 517, 239-44 (Pubitemid 34327667)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , 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
  • 15
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt, W. Oxidation of methionyl residues in proteins: Tools, targets, and reversal Free Radical Biol. Med. 1995, 18, 93-105
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 16
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid aβ-(1-42) peptide of Alzheimer's disease
    • DOI 10.1074/jbc.C200338200
    • Hou, L.; Kang, I.; Marchant, R. E.; Zagorski, M. G. Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease J. Biol. Chem. 2002, 277, 40173-6 (Pubitemid 35215584)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 17
    • 33751112217 scopus 로고    scopus 로고
    • Oxidation inhibits amyloid fibril formation of transthyretin
    • DOI 10.1111/j.1742-4658.2006.05532.x
    • Maleknia, S. D.; Reixach, N.; Buxbaum, J. N. Oxidation inhibits amyloid fibril formation of transthyretin FEBS J. 2006, 273, 5400-6 (Pubitemid 44772396)
    • (2006) FEBS Journal , vol.273 , Issue.23 , pp. 5400-5406
    • Maleknia, S.D.1    Reixach, N.2    Buxbaum, J.N.3
  • 18
    • 52249123646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits assembly and promotes disassembly of apolipoprotein C-II amyloid fibrils
    • Binger, K. J.; Griffin, M. D.; Howlett, G. J. Methionine oxidation inhibits assembly and promotes disassembly of apolipoprotein C-II amyloid fibrils Biochemistry 2008, 47, 10208-17
    • (2008) Biochemistry , vol.47 , pp. 10208-10217
    • Binger, K.J.1    Griffin, M.D.2    Howlett, G.J.3
  • 19
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Vorm, O.; Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 1996, 68, 850-8
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 20
    • 44049105911 scopus 로고    scopus 로고
    • Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein
    • Ecroyd, H.; Koudelka, T.; Thorn, D. C.; Williams, D. M.; Devlin, G.; Hoffmann, P.; Carver, J. A. Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein J. Biol. Chem. 2008, 283, 9012-22
    • (2008) J. Biol. Chem. , vol.283 , pp. 9012-9022
    • Ecroyd, H.1    Koudelka, T.2    Thorn, D.C.3    Williams, D.M.4    Devlin, G.5    Hoffmann, P.6    Carver, J.A.7
  • 21
    • 78149466716 scopus 로고    scopus 로고
    • AlphaB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide
    • Dehle, F. C.; Ecroyd, H.; Musgrave, I. F.; Carver, J. A. alphaB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide Cell Stress Chaperones 2010, 15, 1013-26
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.C.1    Ecroyd, H.2    Musgrave, I.F.3    Carver, J.A.4
  • 22
    • 69349098271 scopus 로고    scopus 로고
    • (-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway
    • Hudson, S. A.; Ecroyd, H.; Dehle, F. C.; Musgrave, I. F.; Carver, J. A. (-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway J. Mol. Biol. 2009, 392, 689-700
    • (2009) J. Mol. Biol. , vol.392 , pp. 689-700
    • Hudson, S.A.1    Ecroyd, H.2    Dehle, F.C.3    Musgrave, I.F.4    Carver, J.A.5
  • 23
    • 0026683462 scopus 로고
    • The multimeric structure and disulfide-bonding pattern of bovine kappa-casein
    • Rasmussen, L. K.; Hojrup, P.; Petersen, T. E. The multimeric structure and disulfide-bonding pattern of bovine kappa-casein Eur. J. Biochem. 1992, 207, 215-22
    • (1992) Eur. J. Biochem. , vol.207 , pp. 215-222
    • Rasmussen, L.K.1    Hojrup, P.2    Petersen, T.E.3
  • 24
    • 0027685785 scopus 로고
    • Review and update of casein chemistry
    • Swaisgood, H. E. Review and update of casein chemistry J. Dairy Sci. 1993, 76, 3054-61
    • (1993) J. Dairy Sci. , vol.76 , pp. 3054-3061
    • Swaisgood, H.E.1
  • 27
    • 0021892809 scopus 로고
    • A 1H-n.m.r. study of casein micelles
    • Griffin, M. C.; Roberts, G. C. A 1H-n.m.r. study of casein micelles Biochem. J. 1985, 228, 273-6
    • (1985) Biochem. J. , vol.228 , pp. 273-276
    • Griffin, M.C.1    Roberts, G.C.2
  • 28
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • Wishart, D. S.; Bigam, C. G.; Holm, A.; Hodges, R. S.; Sykes, B. D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects J. Biomol. NMR 1995, 5, 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 29
    • 17544379500 scopus 로고    scopus 로고
    • Haligramides A and B, two new cytotoxic hexapeptides from the marine sponge Haliclona nigra
    • DOI 10.1021/np000051+
    • Rashid, M. A.; Gustafson, K. R.; Boswell, J. L.; Boyd, M. R. Haligramides A and B, two new cytotoxic hexapeptides from the marine sponge Haliclona nigra J. Nat. Prod. 2000, 63, 956-9 (Pubitemid 30624480)
    • (2000) Journal of Natural Products , vol.63 , Issue.7 , pp. 956-959
    • Boyd, M.R.1
  • 30
    • 0034938628 scopus 로고    scopus 로고
    • Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins
    • Kim, Y. H.; Berry, A. H.; Spencer, D. S.; Stites, W. E. Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins Protein Eng. 2001, 14, 343-7 (Pubitemid 32655950)
    • (2001) Protein Engineering , vol.14 , Issue.5 , pp. 343-347
    • Kim, Y.H.1    Berry, A.H.2    Spencer, D.S.3    Stites, W.E.4
  • 32
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: A structural and kinetic spectroscopic study
    • DOI 10.1016/S0022-2836(02)00144-4
    • Carver, J. A.; Lindner, R. A.; Lyon, C.; Canet, D.; Hernandez, H.; Dobson, C. M.; Redfield, C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: A structural and kinetic spectroscopic study J. Mol. Biol. 2002, 318, 815-27 (Pubitemid 34729371)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.3 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 35
    • 67649836543 scopus 로고    scopus 로고
    • s- and β-caseins and its effect on chaperone activity: A structural and functional investigation
    • s- and β-caseins and its effect on chaperone activity: A structural and functional investigation J. Agric. Food Chem. 2009, 57, 5956-64
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 5956-5964
    • Koudelka, T.1    Hoffmann, P.2    Carver, J.A.3
  • 37
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
    • DOI 10.1074/jbc.M010907200
    • Uversky, V. N.; Li, J.; Fink, A. L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation J. Biol. Chem. 2001, 276, 10737-44 (Pubitemid 38089246)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 38
    • 77954710921 scopus 로고    scopus 로고
    • The dissociated form of kappa-casein is the precursor to its amyloid fibril formation
    • Ecroyd, H.; Thorn, D. C.; Liu, Y.; Carver, J. A. The dissociated form of kappa-casein is the precursor to its amyloid fibril formation Biochem. J. 2010, 429, 251-60
    • (2010) Biochem. J. , vol.429 , pp. 251-260
    • Ecroyd, H.1    Thorn, D.C.2    Liu, Y.3    Carver, J.A.4
  • 39
    • 0027661562 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized kappa-casein structure
    • Kumosinski, T. F.; Brown, E. M.; Farrell, H. M., Jr. Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized kappa-casein structure J. Dairy Sci. 1993, 76, 2507-20
    • (1993) J. Dairy Sci. , vol.76 , pp. 2507-2520
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell, Jr.H.M.3
  • 40
    • 0033830240 scopus 로고    scopus 로고
    • Beta-amyloid peptides are cytotoxic to astrocytes in culture: A role for oxidative stress
    • Brera, B.; Serrano, A.; de Ceballos, M. L. Beta-amyloid peptides are cytotoxic to astrocytes in culture: A role for oxidative stress Neurobiol. Dis. 2000, 7, 395-405
    • (2000) Neurobiol. Dis. , vol.7 , pp. 395-405
    • Brera, B.1    Serrano, A.2    De Ceballos, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.