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Volumn 289, Issue 40, 2014, Pages 27766-27775

Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid ß peptide

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GLYCOPROTEINS; NEURODEGENERATIVE DISEASES;

EID: 84907482249     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.574947     Document Type: Article
Times cited : (53)

References (46)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G., and Wong, C. W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 2
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aß oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aß oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci. 15, 349-357
    • (2012) Nat Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 4
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid ß oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid ß oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 6
    • 84890125654 scopus 로고    scopus 로고
    • Inhibiting and reversing amyloid-ß peptide (1-40) fibril formation with gramicidin S and engineered analogues
    • Luo, J., Otero, J. M., Yu, C.-H., Wärmländer, S. K., Gräslund, A., Overhand, M., and Abrahams, J. P. (2013) Inhibiting and reversing amyloid-ß peptide (1-40) fibril formation with gramicidin S and engineered analogues. Chemistry 19, 17338-17348
    • (2013) Chemistry , vol.19 , pp. 17338-17348
    • Luo, J.1    Otero, J.M.2    Yu, C.-H.3    Wärmländer, S.K.4    Gräslund, A.5    Overhand, M.6    Abrahams, J.P.7
  • 7
    • 84897623980 scopus 로고    scopus 로고
    • Cyclic peptides as inhibitors of amyloid fibrillation
    • Luo, J., and Abrahams, J. P. (2014) Cyclic peptides as inhibitors of amyloid fibrillation. Chemistry 20, 2410-2419
    • (2014) Chemistry , vol.20 , pp. 2410-2419
    • Luo, J.1    Abrahams, J.P.2
  • 8
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a ß-hairpin in monomeric Alzheimer's amyloid-ß peptide inhibits amyloid formation
    • Hoyer, W., Grönwall, C., Jonsson, A., Ståhl, S., and Härd, T. (2008) Stabilization of a ß-hairpin in monomeric Alzheimer's amyloid-ß peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. U.S.A. 105, 5099-5104
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5099-5104
    • Hoyer, W.1    Grönwall, C.2    Jonsson, A.3    Ståhl, S.4    Härd, T.5
  • 10
    • 9444229933 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone
    • Santhoshkumar, P., and Sharma, K. K. (2004) Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone. Mol. Cell Biochem. 267, 147-155
    • (2004) Mol. Cell Biochem. , vol.267 , pp. 147-155
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 12
    • 33646190092 scopus 로고    scopus 로고
    • Small heat shock protein HspB8: Its distribution in Alzheimer's disease brains and its inhibition of amyloid-ß protein aggregation and cerebrovascular amyloid-ß toxicity
    • Wilhelmus, M. M., Boelens, W. C., Otte-Höller, I., Kamps, B., Kusters, B., Maat-Schieman, M. L., de Waal, R. M., and Verbeek, M. M. (2006) Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-ß protein aggregation and cerebrovascular amyloid-ß toxicity. Acta Neuropathol. 111, 139-149
    • (2006) Acta Neuropathol. , vol.111 , pp. 139-149
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Höller, I.3    Kamps, B.4    Kusters, B.5    Maat-Schieman, M.L.6    De Waal, R.M.7    Verbeek, M.M.8
  • 13
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid ß-(l-42) aggregation in vitro
    • Evans, C. G., Wisén, S., and Gestwicki,J. E. (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid ß-(l-42) aggregation in vitro. J. Biol. Chem. 281, 33182-33191
    • (2006) J. Biol. Chem. , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisén, S.2    Gestwicki, J.E.3
  • 15
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon, A. C., Ferreon, J. C., Wright, P. E., and Deniz, A. A. (2013) Modulation of allostery by protein intrinsic disorder. Nature 498, 390 -394
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 16
    • 0033430085 scopus 로고    scopus 로고
    • Amyloid-ß binds catalase with high affinity and inhibits hydrogen peroxide breakdown
    • Milton, N. G. (1999) Amyloid-ß binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem. J. 344, 293-296
    • (1999) Biochem. J. , vol.344 , pp. 293-296
    • Milton, N.G.1
  • 17
    • 0036272650 scopus 로고    scopus 로고
    • ß-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) ß-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
    • 84879778288 scopus 로고    scopus 로고
    • Human lysozyme inhibits the in vitro aggregation of Aß peptides, which in vivo are associated with Alzheimer's disease
    • Luo, J., Wärmländer, S. K. T. S., Gräslund, A., and Abrahams, J. P. (2013) Human lysozyme inhibits the in vitro aggregation of Aß peptides, which in vivo are associated with Alzheimer's disease. Chem. Commun. (Camb)49, 6507-6509
    • (2013) Chem. Commun. (Camb) , vol.49 , pp. 6507-6509
    • Luo, J.1    Wärmländer, S.K.T.S.2    Gräslund, A.3    Abrahams, J.P.4
  • 20
    • 84865007775 scopus 로고    scopus 로고
    • Human serum albumin can regulate amyloid-ß peptide fiber growth in the brain interstitium: Implications for Alzheimer disease
    • Stanyon, H. F., and Viles, J. H. (2012) Human serum albumin can regulate amyloid-ß peptide fiber growth in the brain interstitium: implications for Alzheimer disease. J. Biol. Chem. 287, 28163-28168
    • (2012) J. Biol. Chem. , vol.287 , pp. 28163-28168
    • Stanyon, H.F.1    Viles, J.H.2
  • 22
    • 84902128757 scopus 로고    scopus 로고
    • Endogenous polyamines reduce the toxicity of soluble A ß peptide aggregates associated with Alzheimer's disease
    • Luo, J., Mohammed, I., Wärmländer, S. K., Hiruma, Y., Gräslund, A., and Abrahams, J. P. (2014) Endogenous polyamines reduce the toxicity of soluble A ß peptide aggregates associated with Alzheimer's disease. Biomacromolecules 15, 1985-1991
    • (2014) Biomacromolecules , vol.15 , pp. 1985-1991
    • Luo, J.1    Mohammed, I.2    Wärmländer, S.K.3    Hiruma, Y.4    Gräslund, A.5    Abrahams, J.P.6
  • 25
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • Sluzky, V., Tamada, J. A., Klibanov, A.M., and Langer, R. (1991) Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc. Natl. Acad. Sci. U.S.A. 88, 9377-9381
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 26
    • 84894481810 scopus 로고    scopus 로고
    • The presence of an air-water interface affects formation and elongation of a-synuclein fibrils
    • Campioni, S., Carret, G., Jordens, S., Nicoud, L., Mezzenga, R., and Riek, R. (2014) The presence of an air-water interface affects formation and elongation of a-synuclein fibrils. J. Am. Chem. Soc. 136, 2866 -2875
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 2866-2875
    • Campioni, S.1    Carret, G.2    Jordens, S.3    Nicoud, L.4    Mezzenga, R.5    Riek, R.6
  • 28
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C. G. (2008) Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283, 29639-29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 29
    • 84900336916 scopus 로고    scopus 로고
    • Structural basis for protein antiaggregation activity of the trigger factor chaperone
    • Saio, T., Guan, X., Rossi, P., Economou, A., and Kalodimos, C. G. (2014) Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science 344, 1250494-1250511
    • (2014) Science , vol.344 , pp. 1250494-1250511
    • Saio, T.1    Guan, X.2    Rossi, P.3    Economou, A.4    Kalodimos, C.G.5
  • 31
    • 0026610829 scopus 로고
    • Conformational aspects of the Cu2+ binding to α-lactalbumin: Characterization and stability of the Cu-bound state
    • Van Dael, H., Tieghem, E., Haezebrouck, P., and Van Cauwelaert, F. (1992) Conformational aspects of the Cu2+ binding to α-lactalbumin: characterization and stability of the Cu-bound state. Biophys. Chem. 42, 235-242
    • (1992) Biophys. Chem. , vol.42 , pp. 235-242
    • Van Dael, H.1    Tieghem, E.2    Haezebrouck, P.3    Van Cauwelaert, F.4
  • 32
    • 84860160388 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic investigations of ß-lactoglobulin upon interaction with copper ion
    • Divsalar, A., Damavandi, S. E., Saboury, A. A., Seyedarabi, A., and Moosavi-Movahedi, A. A. (2012) Calorimetric and spectroscopic investigations of ß-lactoglobulin upon interaction with copper ion. J. Dairy Res. 79, 209-215
    • (2012) J. Dairy Res. , vol.79 , pp. 209-215
    • Divsalar, A.1    Damavandi, S.E.2    Saboury, A.A.3    Seyedarabi, A.4    Moosavi-Movahedi, A.A.5
  • 34
    • 0032983691 scopus 로고    scopus 로고
    • Activities of key glycolytic enzymes in the brains of patients with Alzheimer's disease
    • Bigl, M., Brückner, M. K., Arendt, T., Bigi, V., and Eschrich, K. (1999) Activities of key glycolytic enzymes in the brains of patients with Alzheimer's disease. J. Neural Transm. 106, 499-511
    • (1999) J. Neural Transm. , vol.106 , pp. 499-511
    • Bigl, M.1    Brückner, M.K.2    Arendt, T.3    Bigi, V.4    Eschrich, K.5
  • 35
    • 84904975199 scopus 로고    scopus 로고
    • Serum levels of albumin-amyloid ß complexes are decreased in Alzheimer's disease
    • Yamamoto, K., Shimada, H., Koh, H., Ataka, S., and Mild, T. (2014) Serum levels of albumin-amyloid ß complexes are decreased in Alzheimer's disease. Geriatr. Gerontol. Int. 14, 716-723
    • (2014) Geriatr. Gerontol. Int. , vol.14 , pp. 716-723
    • Yamamoto, K.1    Shimada, H.2    Koh, H.3    Ataka, S.4    Mild, T.5
  • 38
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., and Wilson, M. R. (2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 21, 2312-2322
    • (2007) FASEB J. , vol.21 , pp. 2312-2322
    • Yerbury, J.J.1    Poon, S.2    Meehan, S.3    Thompson, B.4    Kumita, J.R.5    Dobson, C.M.6    Wilson, M.R.7
  • 39
    • 63249134826 scopus 로고    scopus 로고
    • α2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species
    • Yerbury, J. J., Kumita, J. R., Meehan, S., Dobson, C. M., and Wilson, M. R. (2009) α2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species. J Biol. Chem. 284, 4246-4254
    • (2009) J Biol. Chem. , vol.284 , pp. 4246-4254
    • Yerbury, J.J.1    Kumita, J.R.2    Meehan, S.3    Dobson, C.M.4    Wilson, M.R.5
  • 41
    • 56949083650 scopus 로고    scopus 로고
    • Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Aß fibrils and protofibrils
    • Arimon, M., Grimminger, V., Sanz, F., and Lashuel, H. A. (2008) Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Aß fibrils and protofibrils.J. Mol. Biol. 384, 1157-1173
    • (2008) J. Mol. Biol. , vol.384 , pp. 1157-1173
    • Arimon, M.1    Grimminger, V.2    Sanz, F.3    Lashuel, H.A.4
  • 42
    • 78651245383 scopus 로고    scopus 로고
    • Stoichiometry and affinity of the human serum albumin-Alzheimer's Aß peptide interactions
    • Milojevic, J., and Melacini, G. (2011) Stoichiometry and affinity of the human serum albumin-Alzheimer's Aß peptide interactions. Biophys. J. 100, 183-192
    • (2011) Biophys. J. , vol.100 , pp. 183-192
    • Milojevic, J.1    Melacini, G.2
  • 43
    • 72249108028 scopus 로고    scopus 로고
    • Human serum albumin inhibits Aß fibrillization through a "monomer-competitor" mechanism
    • Milojevic, J., Raditsis, A., and Melacini, G. (2009) Human serum albumin inhibits Aß fibrillization through a "monomer-competitor" mechanism. Biophys. J. 97, 2585-2594.
    • (2009) Biophys. J. , vol.97 , pp. 2585-2594
    • Milojevic, J.1    Raditsis, A.2    Melacini, G.3
  • 44
    • 84865336939 scopus 로고    scopus 로고
    • Cross-seeding effects of amyloid ß-protein and α-synuclein
    • Ono, K., Takahashi, R., Ikeda, T., and Yamada, M. (2012) Cross-seeding effects of amyloid ß-protein and α-synuclein.J. Neurochem. 122, 883- 890
    • (2012) J. Neurochem. , vol.122 , pp. 883-890
    • Ono, K.1    Takahashi, R.2    Ikeda, T.3    Yamada, M.4
  • 45
    • 77953068390 scopus 로고    scopus 로고
    • Synergistic Interactions between Aß, Tau, and α-synuclein: Acceleration of neuropathology and cognitive decline
    • Clinton, L. K., Blurton-Jones, M., Myczek, K., Trojanowski, J. Q., and LaFerla, F. M. (2010) Synergistic Interactions between Aß, Tau, and α-synuclein: acceleration of neuropathology and cognitive decline.J. Neurosci. 30, 7281-7289
    • (2010) J. Neurosci. , vol.30 , pp. 7281-7289
    • Clinton, L.K.1    Blurton-Jones, M.2    Myczek, K.3    Trojanowski, J.Q.4    LaFerla, F.M.5
  • 46
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between Aß peptide and α synuclein: Molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease
    • Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L., and Mandal, R. (2006) Interaction between Aß peptide and α synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease. Neurochem. Res. 31, 1153-1162
    • (2006) Neurochem. Res. , vol.31 , pp. 1153-1162
    • Mandal, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandal, R.5


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