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Volumn 1842, Issue 4, 2014, Pages 646-653

Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation

Author keywords

Alzheimer's disease; Amyloid protein; Seeding effect

Indexed keywords

ACTIN; AMYLIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PROTEIN; CASEIN; FIBROIN; SERICIN; THIOFLAVINE;

EID: 84893485687     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2014.01.002     Document Type: Article
Times cited : (64)

References (41)
  • 1
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 1993, 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 2
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:1125-1129.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 3
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H., Nakakuki K. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab. Invest. 1996, 74:374-383.
    • (1996) Lab. Invest. , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 6
    • 84865336939 scopus 로고    scopus 로고
    • Cross-seeding effects of amyloid β-protein and α-synuclein
    • Ono K., Takahashi R., Ikeda T., Yamada M. Cross-seeding effects of amyloid β-protein and α-synuclein. J. Neurochem. 2012, 122:883-890.
    • (2012) J. Neurochem. , vol.122 , pp. 883-890
    • Ono, K.1    Takahashi, R.2    Ikeda, T.3    Yamada, M.4
  • 7
    • 2342444028 scopus 로고    scopus 로고
    • Seeding specificity in amyloid growth induced by heterologous fibrils
    • O'Nuallain B., Williams A.D., Westermark P., Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils. J. Biol. Chem. 2004, 279:17490-17499.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 8
    • 33644666997 scopus 로고    scopus 로고
    • Amyloid fibril formation of α-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases
    • Yagi H., Kusaka E., Hongo K., Mizobata T., Kawata Y. Amyloid fibril formation of α-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases. J. Biol. Chem. 2005, 280:38609-38616.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38609-38616
    • Yagi, H.1    Kusaka, E.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 9
    • 79957636327 scopus 로고    scopus 로고
    • Induction of intracellular tau aggregation is promoted by α-synuclein seeds and provides novel insights into the hyperphosphorylation of tau
    • Waxman E.A., Giasson B.I. Induction of intracellular tau aggregation is promoted by α-synuclein seeds and provides novel insights into the hyperphosphorylation of tau. J. Neurosci. 2011, 31:7604-7618.
    • (2011) J. Neurosci. , vol.31 , pp. 7604-7618
    • Waxman, E.A.1    Giasson, B.I.2
  • 11
    • 0025190584 scopus 로고
    • Human-milk proteins: analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods
    • Kunz C., Lonnerdal B. Human-milk proteins: analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods. Am. J. Clin. Nutr. 1990, 51:37-46.
    • (1990) Am. J. Clin. Nutr. , vol.51 , pp. 37-46
    • Kunz, C.1    Lonnerdal, B.2
  • 12
    • 41149181268 scopus 로고    scopus 로고
    • Amyloid fibril formation by bovine milk αs2-casein occurs under physiological conditions yet is prevented by its natural counterpart, αs1-casein
    • Thorn D.C., Ecroyd H., Sunde M., Poon S., Carver J.A. Amyloid fibril formation by bovine milk αs2-casein occurs under physiological conditions yet is prevented by its natural counterpart, αs1-casein. Biochemistry 2008, 47:3926-3936.
    • (2008) Biochemistry , vol.47 , pp. 3926-3936
    • Thorn, D.C.1    Ecroyd, H.2    Sunde, M.3    Poon, S.4    Carver, J.A.5
  • 15
    • 0035660088 scopus 로고    scopus 로고
    • The natural silk spinning process. A nucleation-dependent aggregation mechanism?
    • Li G., Zhou P., Shao Z., Xie X., Chen X., Wang H., Chunyu L., Yu T. The natural silk spinning process. A nucleation-dependent aggregation mechanism?. Eur. J. Biochem. 2001, 268:6600-6606.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6600-6606
    • Li, G.1    Zhou, P.2    Shao, Z.3    Xie, X.4    Chen, X.5    Wang, H.6    Chunyu, L.7    Yu, T.8
  • 17
    • 33745498234 scopus 로고    scopus 로고
    • Physical-chemical properties of actin in different structural states. New ideas about its folding-unfolding pathways
    • Povarova O.I., Kuznetsova I.M., Turoverov K.K. Physical-chemical properties of actin in different structural states. New ideas about its folding-unfolding pathways. Tsitologiia 2005, 47:953-977.
    • (2005) Tsitologiia , vol.47 , pp. 953-977
    • Povarova, O.I.1    Kuznetsova, I.M.2    Turoverov, K.K.3
  • 18
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • Westermark P., Andersson A., Westermark G.T. Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiol. Rev. 2011, 91:795-826.
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 19
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K., Yoshiike Y., Takashima A., Hasegawa K., Naiki H., Yamada M. Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease. J. Neurochem. 2003, 87:172-181.
    • (2003) J. Neurochem. , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 21
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 2004, 278:313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 22
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M. The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. J. Biol. Chem. 2001, 276:14059-14066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.5
  • 24
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999, 309:274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 25
    • 57749112087 scopus 로고    scopus 로고
    • Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity
    • Ono K., Condron M.M., Ho L., Wang J., Zhao W., Pasinetti G.M., Teplow D.B. Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity. J. Biol. Chem. 2008, 283:32176-32187.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32176-32187
    • Ono, K.1    Condron, M.M.2    Ho, L.3    Wang, J.4    Zhao, W.5    Pasinetti, G.M.6    Teplow, D.B.7
  • 26
    • 77955819967 scopus 로고    scopus 로고
    • Kinetics of amyloid β monomer-to-oligomer exchange by NMR relaxation
    • Fawzi N.L., Ying J., Torchia D.A., Clore G.M. Kinetics of amyloid β monomer-to-oligomer exchange by NMR relaxation. J. Am. Chem. Soc. 2010, 132:9948-9951.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9948-9951
    • Fawzi, N.L.1    Ying, J.2    Torchia, D.A.3    Clore, G.M.4
  • 28
    • 0033598697 scopus 로고    scopus 로고
    • Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro
    • Hasegawa K., Yamaguchi I., Omata S., Gejyo F., Naiki H. Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 1999, 38:15514-15521.
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5
  • 29
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood S.J., Wetzel R., Martin J.D., Hurle M.R. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 1995, 34:724-730.
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 30
    • 0033755865 scopus 로고    scopus 로고
    • Effect of amino-acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions
    • McLaurin J., Fraser P.E. Effect of amino-acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions. Eur. J. Biochem. 2000, 267:6353-6361.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6353-6361
    • McLaurin, J.1    Fraser, P.E.2
  • 31
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain
    • Snow A.D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mizutani A., Arai M., Schreier W.A., Morgan D.G. An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain. Neuron 1994, 12:219-234.
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 34
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower J.H., Chu Y., Hauser R.A., Freeman T.B., Olanow C.W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 2008, 14:504-506.
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 35
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Munch C., O'Brien J., Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:3548-3553.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3548-3553
    • Munch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 36
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren P.H., Lauckner J.E., Kachirskaia I., Heuser J.E., Melki R., Kopito R.R. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 2009, 11:219-225.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 37
    • 78049285236 scopus 로고    scopus 로고
    • Prion-like aggregates: infectious agents in human disease
    • Westermark G.T., Westermark P. Prion-like aggregates: infectious agents in human disease. Trends Mol. Med. 2010, 16:501-507.
    • (2010) Trends Mol. Med. , vol.16 , pp. 501-507
    • Westermark, G.T.1    Westermark, P.2
  • 39
    • 0024202160 scopus 로고
    • Systemic amyloid deposition in old age and dementia of Alzheimer type: the relationship of brain amyloid to other amyloid
    • Yamada M., Tsukagoshi H., Otomo E., Hayakawa M. Systemic amyloid deposition in old age and dementia of Alzheimer type: the relationship of brain amyloid to other amyloid. Acta Neuropathol. 1988, 77:136-141.
    • (1988) Acta Neuropathol. , vol.77 , pp. 136-141
    • Yamada, M.1    Tsukagoshi, H.2    Otomo, E.3    Hayakawa, M.4
  • 40
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: not only pathological agents but also ordered nanomaterials
    • Cherny I., Gazit E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew. Chem. Int. Ed. Engl. 2008, 47:4062-4069.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 41
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles T.P., Buehler M.J. Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 2011, 6:469-479.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 469-479
    • Knowles, T.P.1    Buehler, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.