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Volumn 54, Issue 13, 2015, Pages 2193-2204

Biophysical Comparison of Soluble Amyloid-β(1-42) Protofibrils, Oligomers, and Protofilaments

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; DYNAMIC LIGHT SCATTERING; GLYCOPROTEINS; LIGHT SCATTERING; NEURODEGENERATIVE DISEASES; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 84926669639     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500957g     Document Type: Article
Times cited : (41)

References (48)
  • 1
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease
    • Masters, C. L. and Selkoe, D. J. (2012) Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease Cold Spring Harbor Perspect. Med. 2, a006262
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. a006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 2
    • 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
  • 3
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants
    • Suzuki, N., Cheung, T. T., Cai, X. D., Odaka, A., Otvos, L., Jr., Eckman, C., Golde, T. E., and Younkin, S. G. (1994) An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants Science 264, 1336 - 1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos, L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 5
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. (1997) Amyloid, the presenilins and Alzheimer's disease Trends Neurosci. 20, 154 - 159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 6
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T., Berger, E. P., and Lansbury, P. T., Jr. (1993) The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease Biochemistry 32, 4693 - 4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 7
    • 0028915895 scopus 로고
    • Amyloid β protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ42(43)
    • Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Jr., Younkin, L. H., Suzuki, N., and Younkin, S. G. (1995) Amyloid β protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ42(43) J. Biol. Chem. 270, 7013 - 7016
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3    Long, K.E.4    Otvos, L.5    Younkin, L.H.6    Suzuki, N.7    Younkin, S.G.8
  • 9
    • 34548812551 scopus 로고    scopus 로고
    • The role of amyloid β peptide 42 in Alzheimer's disease
    • Findeis, M. A. (2007) The role of amyloid β peptide 42 in Alzheimer's disease Pharmacol. Ther. 116, 266 - 286
    • (2007) Pharmacol. Ther. , vol.116 , pp. 266-286
    • Findeis, M.A.1
  • 10
    • 77955919746 scopus 로고    scopus 로고
    • Biomarkers in translational research of Alzheimer's disease
    • Tarawneh, R. and Holtzman, D. M. (2010) Biomarkers in translational research of Alzheimer's disease Neuropharmacology 59, 310 - 322
    • (2010) Neuropharmacology , vol.59 , pp. 310-322
    • Tarawneh, R.1    Holtzman, D.M.2
  • 11
    • 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
  • 12
    • 84901635545 scopus 로고    scopus 로고
    • Simultaneous measurement of a range of particle sizes during Aβ1-42 fibrillogenesis quantified using fluorescence correlation spectroscopy
    • Mittag, J. J., Milani, S., Walsh, D. M., Radler, J. O., and McManus, J. J. (2014) Simultaneous measurement of a range of particle sizes during Aβ1-42 fibrillogenesis quantified using fluorescence correlation spectroscopy Biochem. Biophys. Res. Commun. 448, 195 - 199
    • (2014) Biochem. Biophys. Res. Commun. , vol.448 , pp. 19-199
    • Mittag, J.J.1    Milani, S.2    Walsh, D.M.3    Radler, J.O.4    McManus, J.J.5
  • 13
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Aβ amyloid peptides: An in vitro model for a possible early event in Alzheimer's disease
    • Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T., Jr. (1999) Assembly of Aβ amyloid peptides: An in vitro model for a possible early event in Alzheimer's disease Biochemistry 38, 8972 - 8980
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 14
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate J. Biol. Chem. 272, 22364 - 22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 16
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J. D., Lieber, C. M., and Lansbury, P. T., Jr. (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein Chem. Biol. 4, 951 - 959
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 17
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T. and Lansbury, P. T., Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055 - 1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 19
    • 0037076539 scopus 로고    scopus 로고
    • Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • Nichols, M. R., Moss, M. A., Reed, D. K., Lin, W. L., Mukhopadhyay, R., Hoh, J. H., and Rosenberry, T. L. (2002) Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41, 6115 - 6127
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 20
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine, W. B. J., Dahlgren, K. N., Krafft, G. A., and LaDu, M. J. (2003) In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis J. Biol. Chem. 278, 11612 - 11622
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.J.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 22
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass, C. and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide Nat. Rev. Mol. Cell Biol. 8, 101 - 112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 23
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ oligomers: A decade of discovery J. Neurochem. 101, 1172 - 1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 25
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande, A., Mina, E., Glabe, C., and Busciglio, J. (2006) Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons J. Neurosci. 26, 6011 - 6018
    • (2006) J. Neurosci. , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 26
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., and Selkoe, D. J. (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons J. Neurosci. 19, 8876 - 8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 27
    • 0042405095 scopus 로고    scopus 로고
    • Protofibrils of amyloid β-protein inhibit specific K+ currents in neocortical cultures
    • Ye, C. P., Selkoe, D. J., and Hartley, D. M. (2003) Protofibrils of amyloid β-protein inhibit specific K+ currents in neocortical cultures Neurobiol. Dis. 13, 177 - 190
    • (2003) Neurobiol. Dis. , vol.13 , pp. 177-190
    • Ye, C.P.1    Selkoe, D.J.2    Hartley, D.M.3
  • 28
    • 77956698237 scopus 로고    scopus 로고
    • Preparation and characterization of toxic Aβ aggregates for structural and functional studies in Alzheimer's disease research
    • Jan, A., Hartley, D. M., and Lashuel, H. A. (2010) Preparation and characterization of toxic Aβ aggregates for structural and functional studies in Alzheimer's disease research Nat. Protoc. 5, 1186 - 1209
    • (2010) Nat. Protoc. , vol.5 , pp. 1186-1209
    • Jan, A.1    Hartley, D.M.2    Lashuel, H.A.3
  • 31
    • 58649100263 scopus 로고    scopus 로고
    • Granular assembly of α-synuclein leading to the accelerated amyloid fibril formation with shear stress
    • Bhak, G., Lee, J. H., Hahn, J. S., and Paik, S. R. (2009) Granular assembly of α-synuclein leading to the accelerated amyloid fibril formation with shear stress PLoS One 4, e4177
    • (2009) PLoS One , vol.4 , pp. e4177
    • Bhak, G.1    Lee, J.H.2    Hahn, J.S.3    Paik, S.R.4
  • 32
    • 84859918496 scopus 로고    scopus 로고
    • Isolated amyloid-β(1-42) protofibrils, but not isolated fibrils, are robust stimulators of microglia
    • Paranjape, G. S., Gouwens, L. K., Osborn, D. C., and Nichols, M. R. (2012) Isolated amyloid-β(1-42) protofibrils, but not isolated fibrils, are robust stimulators of microglia ACS Chem. Neurosci. 3, 302 - 311
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 302-311
    • Paranjape, G.S.1    Gouwens, L.K.2    Osborn, D.C.3    Nichols, M.R.4
  • 33
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • Wyatt, P. J. (1993) Light scattering and the absolute characterization of macromolecules Anal. Chim. Acta 272, 1 - 40
    • (1993) Anal. Chim. Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 35
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 287, 252 - 260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 36
    • 84874650573 scopus 로고    scopus 로고
    • Amyloid-(1-42) protofibrils formed in modified artificial cerebrospinal fluid bind and activate microglia
    • Paranjape, G. S., Terrill, S. E., Gouwens, L. K., Ruck, B. M., and Nichols, M. R. (2013) Amyloid-(1-42) protofibrils formed in modified artificial cerebrospinal fluid bind and activate microglia J. Neuroimmune Pharmacol. 8, 312 - 322
    • (2013) J. Neuroimmune Pharmacol. , vol.8 , pp. 312-322
    • Paranjape, G.S.1    Terrill, S.E.2    Gouwens, L.K.3    Ruck, B.M.4    Nichols, M.R.5
  • 37
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H. (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution Protein Sci. 2, 404 - 410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 38
    • 0345060507 scopus 로고    scopus 로고
    • Aβ protofibrils possess a stable core structure resistant to hydrogen exchange
    • Kheterpal, I., Lashuel, H. A., Hartley, D. M., Walz, T., Lansbury, P. T., Jr., and Wetzel, R. (2003) Aβ protofibrils possess a stable core structure resistant to hydrogen exchange Biochemistry 42, 14092 - 14098
    • (2003) Biochemistry , vol.42 , pp. 14092-14098
    • Kheterpal, I.1    Lashuel, H.A.2    Hartley, D.M.3    Walz, T.4    Lansbury, P.T.5    Wetzel, R.6
  • 39
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T., Jr. (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy Chem. Biol. 4, 119 - 125
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 41
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of amyloid β-protein for structural and functional studies
    • Teplow, D. B. (2006) Preparation of amyloid β-protein for structural and functional studies Methods Enzymol. 413, 20 - 33
    • (2006) Methods Enzymol. , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 42
    • 84922894999 scopus 로고    scopus 로고
    • Resting microglia react to Aβ42 fibrils but do not detect oligomers or oligomer-induced neuronal damage
    • Ferrera, D., Mazzaro, N., Canale, C., and Gasparini, L. (2014) Resting microglia react to Aβ42 fibrils but do not detect oligomers or oligomer-induced neuronal damage Neurobiol. Aging 35, 2444 - 2457
    • (2014) Neurobiol. Aging , vol.35 , pp. 2444-2457
    • Ferrera, D.1    Mazzaro, N.2    Canale, C.3    Gasparini, L.4
  • 44
    • 70349782469 scopus 로고    scopus 로고
    • Amyloid-β(1-42) fibrillar precursors are optimal for inducing tumor necrosis factor-α production in the THP-1 human monocytic cell line
    • Ajit, D., Udan, M. L., Paranjape, G., and Nichols, M. R. (2009) Amyloid-β(1-42) fibrillar precursors are optimal for inducing tumor necrosis factor-α production in the THP-1 human monocytic cell line Biochemistry 48, 9011 - 9021
    • (2009) Biochemistry , vol.48 , pp. 9011-9021
    • Ajit, D.1    Udan, M.L.2    Paranjape, G.3    Nichols, M.R.4
  • 45
    • 70049102020 scopus 로고    scopus 로고
    • Aβ peptide conformation determines uptake and interleukin-1α expression by primary microglial cells
    • Parvathy, S., Rajadas, J., Ryan, H., Vaziri, S., Anderson, L., and Murphy, G. M., Jr. (2009) Aβ peptide conformation determines uptake and interleukin-1α expression by primary microglial cells Neurobiol. Aging 30, 1792 - 1804
    • (2009) Neurobiol. Aging , vol.30 , pp. 1792-1804
    • Parvathy, S.1    Rajadas, J.2    Ryan, H.3    Vaziri, S.4    Anderson, L.5    Murphy, G.M.6
  • 46
    • 33646841989 scopus 로고    scopus 로고
    • β-Amyloid stimulates murine postnatal and adult microglia cultures in a unique manner
    • Floden, A. M. and Combs, C. K. (2006) β-Amyloid stimulates murine postnatal and adult microglia cultures in a unique manner J. Neurosci. 26, 4644 - 4648
    • (2006) J. Neurosci. , vol.26 , pp. 4644-4648
    • Floden, A.M.1    Combs, C.K.2
  • 47
    • 14744283139 scopus 로고    scopus 로고
    • Differential effects of oligomeric and fibrillar amyloid-β1-42 on astrocyte-mediated inflammation
    • White, J. A., Manelli, A. M., Holmberg, K. H., Van Eldik, L. J., and Ladu, M. J. (2005) Differential effects of oligomeric and fibrillar amyloid-β1-42 on astrocyte-mediated inflammation Neurobiol. Dis. 18, 459 - 465
    • (2005) Neurobiol. Dis. , vol.18 , pp. 459-465
    • White, J.A.1    Manelli, A.M.2    Holmberg, K.H.3    Van Eldik, L.J.4    Ladu, M.J.5


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