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Volumn 22, Issue 5, 2009, Pages 403-413

Preparation of fluorescently-labeled amyloid-beta peptide assemblies: The effect of fluorophore conjugation on structure and function

Author keywords

AFM; Amyloid beta; Assembly; Cellular uptake; Fibril; Fluorescence; Neuro 2A cells; Oligomer

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); FLUORESCENT DYE; PEPTIDE FRAGMENT;

EID: 68949163262     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.948     Document Type: Conference Paper
Times cited : (59)

References (48)
  • 1
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers-what you see is not alwayswhat you get
    • Bitan G, Fradinger EA, Spring SM, Teplow DB. 2005. Neurotoxic protein oligomers-what you see is not alwayswhat you get. Amyloid 12: 88-95.
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 2
    • 0034595821 scopus 로고    scopus 로고
    • Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia
    • Brazil MI, Chung H, Maxfield FR. 2000. Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia. J. Biol. Chem. 275: 16941-16947.
    • (2000) J. Biol. Chem , vol.275 , pp. 16941-16947
    • Brazil, M.I.1    Chung, H.2    Maxfield, F.R.3
  • 3
    • 50949097728 scopus 로고    scopus 로고
    • Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake
    • Chafekar SM, Baas F, Scheper W. 2008. Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake. Biochim. Biophys. Acta 1782: 523-531.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 523-531
    • Chafekar, S.M.1    Baas, F.2    Scheper, W.3
  • 6
    • 33845406090 scopus 로고    scopus 로고
    • Preferential accumulation of Abeta(1-42) on gel phase domains of lipid bilayers: An AFM and fluorescence study
    • Choucair A, Chakrapani M, Chakravarthy B, Katsaras J, Johnston LJ. 2007. Preferential accumulation of Abeta(1-42) on gel phase domains of lipid bilayers: an AFM and fluorescence study. Biochim. Biophys. Acta 1768: 146-154.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 146-154
    • Choucair, A.1    Chakrapani, M.2    Chakravarthy, B.3    Katsaras, J.4    Johnston, L.J.5
  • 7
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid betapeptide by microglial cells
    • Chung H, Brazil MI, Soe TT, Maxfield FR. 1999. Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid betapeptide by microglial cells. J. Biol. Chem. 274: 32301-32308.
    • (1999) J. Biol. Chem , vol.274 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 9
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, LaDu MJ. 2002. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 277: 32046-32053.
    • (2002) J. Biol. Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 10
    • 34147115541 scopus 로고    scopus 로고
    • Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
    • El Khoury J, Toft M, Hickman SE, Means TK, Terada K, Geula C, Luster AD. 2007. Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease. Nat. Med. 13: 432-438.
    • (2007) Nat. Med , vol.13 , pp. 432-438
    • El Khoury, J.1    Toft, M.2    Hickman, S.E.3    Means, T.K.4    Terada, K.5    Geula, C.6    Luster, A.D.7
  • 11
    • 0037294045 scopus 로고    scopus 로고
    • Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates
    • Frost D, Gorman PM, Yip CM, Chakrabartty A. 2003. Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates. Eur. J. Biochem. 270: 654-663.
    • (2003) Eur. J. Biochem , vol.270 , pp. 654-663
    • Frost, D.1    Gorman, P.M.2    Yip, C.M.3    Chakrabartty, A.4
  • 13
  • 14
    • 34249041646 scopus 로고    scopus 로고
    • Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template
    • Ha C, Ryu J, Park CB. 2007. Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template. Biochemistry (Mosc). 46: 6118-6125.
    • (2007) Biochemistry (Mosc) , vol.46 , pp. 6118-6125
    • Ha, C.1    Ryu, J.2    Park, C.B.3
  • 15
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT. 1997. Observation of metastable Abeta 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
  • 16
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper JD, Wong SS, Lieber CM, Lansbury PT Jr. 1999. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry (Mosc). 38: 8972-8980.
    • (1999) Biochemistry (Mosc) , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 17
    • 51149120624 scopus 로고    scopus 로고
    • Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice
    • Hickman SE, Allison EK, El Khoury J. 2008. Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice. J. Neurosci. 28: 8354-8360.
    • (2008) J. Neurosci , vol.28 , pp. 8354-8360
    • Hickman, S.E.1    Allison, E.K.2    El Khoury, J.3
  • 20
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation
    • Kowalewski T, Holtzman DM. 1999. In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation. Proc. Natl. Acad. Sci. U.S.A. 96: 3688-3693.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 23
    • 0345862278 scopus 로고    scopus 로고
    • Effect of different anti-Abeta antibodies on Abeta fibrillogenesis as assessed by atomic force microscopy
    • Legleiter J, Czilli DL, Gitter B, DeMattos RB, Holtzman DM, Kowalewski T. 2004. Effect of different anti-Abeta antibodies on Abeta fibrillogenesis as assessed by atomic force microscopy. J. Mol. Biol. 335: 997-1006.
    • (2004) J. Mol. Biol , vol.335 , pp. 997-1006
    • Legleiter, J.1    Czilli, D.L.2    Gitter, B.3    DeMattos, R.B.4    Holtzman, D.M.5    Kowalewski, T.6
  • 24
    • 2942683736 scopus 로고    scopus 로고
    • Atomic force microscopy of beta-amyloid: Static and dynamic studies of nanostructure and its formation
    • Legleiter J, Kowalewski T. 2004. Atomic force microscopy of beta-amyloid: static and dynamic studies of nanostructure and its formation. Methods Mol. Biol. 242: 349-364.
    • (2004) Methods Mol. Biol , vol.242 , pp. 349-364
    • Legleiter, J.1    Kowalewski, T.2
  • 25
    • 0033812349 scopus 로고    scopus 로고
    • Estrogen enhances uptake of amyloid beta-protein by microglia derived from the human cortex
    • Li R, Shen Y, Yang LB, Lue LF, Finch C, Rogers J. 2000. Estrogen enhances uptake of amyloid beta-protein by microglia derived from the human cortex. J. Neurochem. 75: 1447-1454.
    • (2000) J. Neurochem , vol.75 , pp. 1447-1454
    • Li, R.1    Shen, Y.2    Yang, L.B.3    Lue, L.F.4    Finch, C.5    Rogers, J.6
  • 27
    • 34249293987 scopus 로고    scopus 로고
    • Abeta42 neurotoxicity in primary co-cultures: Effect of apoE isoform and Abeta conformation
    • Manelli AM, Bulfinch LC, Sullivan PM, LaDu MJ. 2007. Abeta42 neurotoxicity in primary co-cultures: effect of apoE isoform and Abeta conformation. Neurobiol. Aging 28: 1139-1147.
    • (2007) Neurobiol. Aging , vol.28 , pp. 1139-1147
    • Manelli, A.M.1    Bulfinch, L.C.2    Sullivan, P.M.3    LaDu, M.J.4
  • 28
    • 2542430828 scopus 로고    scopus 로고
    • ApoE and Abeta1-42 interactions: Effects of isoform and conformation on structure and function
    • Manelli AM, Stine WB, Van Eldik LJ, LaDu MJ. 2004. ApoE and Abeta1-42 interactions: effects of isoform and conformation on structure and function. J. Mol. Neurosci. 23: 235-246.
    • (2004) J. Mol. Neurosci , vol.23 , pp. 235-246
    • Manelli, A.M.1    Stine, W.B.2    Van Eldik, L.J.3    LaDu, M.J.4
  • 31
    • 67650741983 scopus 로고    scopus 로고
    • Nielsen HM, Veerhuis R, Holmqvist B, Janciauskiene S. 2008. Binding and uptake of Abeta1-42 by primary human astrocytes in vitro. Glia. This article is an Epub ahead of print. Published online: 5 December 2008, DOI. 10.1002/glia.20822
    • Nielsen HM, Veerhuis R, Holmqvist B, Janciauskiene S. 2008. Binding and uptake of Abeta1-42 by primary human astrocytes in vitro. Glia. This article is an Epub ahead of print. Published online: 5 December 2008, DOI. 10.1002/glia.20822
  • 32
    • 0035997230 scopus 로고    scopus 로고
    • Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy
    • Parbhu A, Lin H, Thimm J, Lal R. 2002. Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy. Peptides. 23: 1265-1270.
    • (2002) Peptides , vol.23 , pp. 1265-1270
    • Parbhu, A.1    Lin, H.2    Thimm, J.3    Lal, R.4
  • 33
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid beta-protein via a scavenger receptor
    • Paresce DM, Ghosh RN, Maxfield FR. 1996. Microglial cells internalize aggregates of the Alzheimer's disease amyloid beta-protein via a scavenger receptor. Neuron 17: 553-565.
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 34
    • 70049102020 scopus 로고    scopus 로고
    • Parvathy S, Rajadas J, Ryan H, Vaziri S, Anderson L, Murphy GM Jr. 2008. Abeta peptide conformation determines uptake and interleukin-1alpha expression by primary microglial cells. Neurobiol. Aging. This article is an Epub ahead of print. Published online: 11 Marc. 2008. DOI. 10.1016/j.neurobiolaging. 2008.01.011
    • Parvathy S, Rajadas J, Ryan H, Vaziri S, Anderson L, Murphy GM Jr. 2008. Abeta peptide conformation determines uptake and interleukin-1alpha expression by primary microglial cells. Neurobiol. Aging. This article is an Epub ahead of print. Published online: 11 Marc. 2008. DOI. 10.1016/j.neurobiolaging. 2008.01.011
  • 35
    • 45249102680 scopus 로고    scopus 로고
    • Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders
    • Rahimi F, Shanmugam A, Bitan G. 2008. Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Curr. Alzheimer Res. 5: 319-341.
    • (2008) Curr. Alzheimer Res , vol.5 , pp. 319-341
    • Rahimi, F.1    Shanmugam, A.2    Bitan, G.3
  • 37
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • Saavedra L, Mohamed A, Ma V, Kar S, de Chaves EP. 2007. Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E. J. Biol. Chem. 282: 35722-35732.
    • (2007) J. Biol. Chem , vol.282 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    de Chaves, E.P.5
  • 38
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Abeta peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Abeta toxicity
    • Simakova O, Arispe NJ. 2007. The cell-selective neurotoxicity of the Alzheimer's Abeta peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Abeta toxicity. J. Neurosci. 27: 13719-13729.
    • (2007) J. Neurosci , vol.27 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 40
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine WB Jr, Dahlgren KN, Krafft GK, LaDu MJ. 2003. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278: 11612-11622.
    • (2003) J. Biol. Chem , vol.278 , pp. 11612-11622
    • Stine Jr, W.B.1    Dahlgren, K.N.2    Krafft, G.K.3    LaDu, M.J.4
  • 41
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of amyloid beta-protein for structural and functional studies
    • Teplow DB. 2006. Preparation of amyloid beta-protein for structural and functional studies. Methods Enzymol. 413: 20-33.
    • (2006) Methods Enzymol , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 43
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarandi M, Penke B. 2004. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J Pept Sci. 10: 229-248.
    • (2004) J Pept Sci , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 44
    • 0035877075 scopus 로고    scopus 로고
    • Antibody-mediated phagocytosis of the amyloid betapeptide in microglia is differentially modulated by C1q
    • Webster SD, Galvan MD, Ferran E, Garzon-Rodriguez W, Glabe CG, Tenner AJ. 2001. Antibody-mediated phagocytosis of the amyloid betapeptide in microglia is differentially modulated by C1q. J. Immunol. 166: 7496-7503.
    • (2001) J. Immunol , vol.166 , pp. 7496-7503
    • Webster, S.D.1    Galvan, M.D.2    Ferran, E.3    Garzon-Rodriguez, W.4    Glabe, C.G.5    Tenner, A.J.6
  • 45
    • 14744283139 scopus 로고    scopus 로고
    • Differential effects of oligomeric and fibrillar amyloid-beta1-42 on astrocyte-mediated inflammation
    • White JA, Manelli AM, Holmberg KH, Van Eldik LJ, LaDu MJ. 2005. Differential effects of oligomeric and fibrillar amyloid-beta1-42 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
  • 46
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-beta aggregation pathway with chemical chaperones
    • Yang DS, Yip CM, Huang TH, Chakrabartty A, Fraser PE. 1999. Manipulating the amyloid-beta aggregation pathway with chemical chaperones. J. Biol. Chem. 274: 32970-32974.
    • (1999) J. Biol. Chem , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.3    Chakrabartty, A.4    Fraser, P.E.5
  • 47
    • 64149132721 scopus 로고    scopus 로고
    • Amyloid beta -protein toxicity and the pathogenesis of Alzheimer's disease
    • Yankner BA, Lu T. 2008. Amyloid beta -protein toxicity and the pathogenesis of Alzheimer's disease. J. Biol. Chem. 284(8): 4755-4759.
    • (2008) J. Biol. Chem , vol.284 , Issue.8 , pp. 4755-4759
    • Yankner, B.A.1    Lu, T.2
  • 48
    • 0036019210 scopus 로고    scopus 로고
    • Abeta42-peptide assembly on lipid bilayers
    • Yip CM, Darabie AA, McLaurin J. 2002. Abeta42-peptide assembly on lipid bilayers. J. Mol. Biol. 318: 97-107.
    • (2002) J. Mol. Biol , vol.318 , pp. 97-107
    • Yip, C.M.1    Darabie, A.A.2    McLaurin, J.3


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