메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Characterization of Oligomers of Heterogeneous Size as Precursors of Amyloid Fibril Nucleation of an SH3 Domain: An Experimental Kinetics Study

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PROTEIN; FODRIN; MONOMER; OLIGOMER; POLYPEPTIDE; PROTEIN SH3; SODIUM CHLORIDE; THIOFLAVINE;

EID: 84870260214     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049690     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM, (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 18544379580 scopus 로고    scopus 로고
    • Actin polymerization machinery: the finish line of signaling networks, the starting point of cellular movement
    • Disanza A, Steffen A, Hertzog M, Frittoli E, Rottner K, et al. (2005) Actin polymerization machinery: the finish line of signaling networks, the starting point of cellular movement. Cell Mol Life Sci 62: 955-970.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 955-970
    • Disanza, A.1    Steffen, A.2    Hertzog, M.3    Frittoli, E.4    Rottner, K.5
  • 3
    • 33947613349 scopus 로고
    • Theory of Linear and Helical Aggregations of Macromolecules
    • Oosawa F, Kasai M, (1962) Theory of Linear and Helical Aggregations of Macromolecules. J Mol Biol 4: 10-&.
    • (1962) J Mol Biol , vol.4 , pp. 10
    • Oosawa, F.1    Kasai, M.2
  • 4
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ, (2007) Non-native protein aggregation kinetics. Biotechnol Bioeng 98: 927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 5
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature
    • Morris AM, Watzky MA, Finke RG, (2009) Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. Biochim Biophys Acta 1794: 375-397.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 6
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews JM, Roberts CJ, (2007) A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111: 7897-7913.
    • (2007) J Phys Chem B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 7
    • 55749087363 scopus 로고    scopus 로고
    • Direct characterization of amyloidogenic oligomers by single-molecule fluorescence
    • Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, et al. (2008) Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proc Natl Acad Sci U S A 105: 14424-14429.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14424-14429
    • Orte, A.1    Birkett, N.R.2    Clarke, R.W.3    Devlin, G.L.4    Dobson, C.M.5
  • 8
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, et al. (2003) Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100: 330-335.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5
  • 9
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 10
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation
    • Modler AJ, Gast K, Lutsch G, Damaschun G, (2003) Assembly of amyloid protofibrils via critical oligomers- A novel pathway of amyloid formation. J Mol Biol 325: 135-148.
    • (2003) J Mol Biol , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 11
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    • Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM, (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. J Mol Biol 356: 189-208.
    • (2006) J Mol Biol , vol.356 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 12
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, et al. (2000) Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys J 79: 1053-1065.
    • (2000) Biophys J , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5
  • 13
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
    • Plakoutsi G, Taddei N, Stefani M, Chiti F, (2004) Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation. J Biol Chem 279: 14111-14119.
    • (2004) J Biol Chem , vol.279 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 14
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ, (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-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
  • 15
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, Cherny RA, Fraser FW, Fuller SJ, Smith MJ, et al. (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 46: 860-866.
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5
  • 16
    • 85109083933 scopus 로고    scopus 로고
    • Alpha-synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma
    • El-Agnaf OM, Salem SA, Paleologou KE, Cooper LJ, Fullwood NJ, et al. (2003) Alpha-synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma. Faseb J 17: 1945-1947.
    • (2003) Faseb J , vol.17 , pp. 1945-1947
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Cooper, L.J.4    Fullwood, N.J.5
  • 17
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation
    • Schaffar G, Breuer P, Boteva R, Behrends C, Tzvetkov N, et al. (2004) Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell 15: 95-105.
    • (2004) Mol Cell , vol.15 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3    Behrends, C.4    Tzvetkov, N.5
  • 18
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates
    • Sousa MM, Cardoso I, Fernandes R, Guimaraes A, Saraiva MJ, (2001) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am J Pathol 159: 1993-2000.
    • (2001) Am J Pathol , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 19
    • 14844323613 scopus 로고    scopus 로고
    • Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity?
    • Malisauskas M, Ostman J, Darinskas A, Zamotin V, Liutkevicius E, et al. (2005) Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity? J Biol Chem 280: 6269-6275.
    • (2005) J Biol Chem , vol.280 , pp. 6269-6275
    • Malisauskas, M.1    Ostman, J.2    Darinskas, A.3    Zamotin, V.4    Liutkevicius, E.5
  • 20
    • 3843148352 scopus 로고    scopus 로고
    • Prefibrillar amyloid protein aggregates share common features of cytotoxicity
    • Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, et al. (2004) Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 279: 31374-31382.
    • (2004) J Biol Chem , vol.279 , pp. 31374-31382
    • Bucciantini, M.1    Calloni, G.2    Chiti, F.3    Formigli, L.4    Nosi, D.5
  • 21
    • 30744477442 scopus 로고    scopus 로고
    • A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation
    • Morel B, Casares S, Conejero-Lara F, (2006) A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation. J Mol Biol 356: 453-468.
    • (2006) J Mol Biol , vol.356 , pp. 453-468
    • Morel, B.1    Casares, S.2    Conejero-Lara, F.3
  • 22
    • 59849130063 scopus 로고    scopus 로고
    • A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state
    • Varela L, Morel B, Azuaga AI, Conejero-Lara F, (2009) A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state. FEBS Lett 583: 801-806.
    • (2009) FEBS Lett , vol.583 , pp. 801-806
    • Varela, L.1    Morel, B.2    Azuaga, A.I.3    Conejero-Lara, F.4
  • 23
    • 78649807663 scopus 로고    scopus 로고
    • Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology
    • Morel B, Varela L, Azuaga AI, Conejero-Lara F, (2010) Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology. Biophys J 99: 3801-3810.
    • (2010) Biophys J , vol.99 , pp. 3801-3810
    • Morel, B.1    Varela, L.2    Azuaga, A.I.3    Conejero-Lara, F.4
  • 24
    • 0033551492 scopus 로고    scopus 로고
    • The native state conformational ensemble of the SH3 domain from alpha-spectrin
    • Sadqi M, Casares S, Abril MA, Lopez-Mayorga O, Conejero-Lara F, et al. (1999) The native state conformational ensemble of the SH3 domain from alpha-spectrin. Biochemistry 38: 8899-8906.
    • (1999) Biochemistry , vol.38 , pp. 8899-8906
    • Sadqi, M.1    Casares, S.2    Abril, M.A.3    Lopez-Mayorga, O.4    Conejero-Lara, F.5
  • 25
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 26
    • 0031160370 scopus 로고    scopus 로고
    • 1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure
    • Blanco FJ, Ortiz AR, Serrano L, (1997) 1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure. J Biomol NMR 9: 347-357.
    • (1997) J Biomol NMR , vol.9 , pp. 347-357
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 27
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson BA, (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278: 313-352.
    • (2004) Methods Mol Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 28
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB, (1996) On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci U S A 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
  • 29
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad A, Uversky VN, Hong D, Fink AL, (2005) Early events in the fibrillation of monomeric insulin. J Biol Chem 280: 42669-42675.
    • (2005) J Biol Chem , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 30
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
    • Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, et al. (2005) Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol 351: 850-864.
    • (2005) J Mol Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5
  • 31
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT 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 Jr., P.T.2
  • 33
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F, (1999) Analysis of protein aggregation kinetics. Methods Enzymol 309: 256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 34
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization
    • Li Y, Roberts CJ, (2009) Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization. J Phys Chem B 113: 7020-7032.
    • (2009) J Phys Chem B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 35
    • 80052304480 scopus 로고    scopus 로고
    • Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides
    • Vitalis A, Pappu RV, (2011) Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides. Biophys Chem 159: 14-23.
    • (2011) Biophys Chem , vol.159 , pp. 14-23
    • Vitalis, A.1    Pappu, R.V.2
  • 36
    • 33745757474 scopus 로고    scopus 로고
    • The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration"
    • Powers ET, Powers DL, (2006) The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". Biophys J 91: 122-132.
    • (2006) Biophys J , vol.91 , pp. 122-132
    • Powers, E.T.1    Powers, D.L.2
  • 37
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: structure and assembly
    • Serpell LC, (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 1502: 16-30.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 38
    • 13844281065 scopus 로고    scopus 로고
    • Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations
    • Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, et al. (2005) Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. J Mol Biol 346: 773-788.
    • (2005) J Mol Biol , vol.346 , pp. 773-788
    • Dumoulin, M.1    Canet, D.2    Last, A.M.3    Pardon, E.4    Archer, D.B.5
  • 39
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky VN, Fink AL, (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698: 131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 40
    • 33744937549 scopus 로고    scopus 로고
    • Sulfates Dramatically Stabilize a Salt-Dependent Type of Glucagon Fibrils
    • Pedersen JS, Flink JM, Dikov D, Otzen DE, (2006) Sulfates Dramatically Stabilize a Salt-Dependent Type of Glucagon Fibrils. Biophys J 90: 4181-4194.
    • (2006) Biophys J , vol.90 , pp. 4181-4194
    • Pedersen, J.S.1    Flink, J.M.2    Dikov, D.3    Otzen, D.E.4
  • 41
    • 35148899284 scopus 로고    scopus 로고
    • Effect of Different Salt Ions on the Propensity of Aggregation and on the Structure of Alzheimer's A[beta](1-40) Amyloid Fibrils
    • Klement K, Wieligmann K, Meinhardt J, Hortschansky P, Richter W, et al. (2007) Effect of Different Salt Ions on the Propensity of Aggregation and on the Structure of Alzheimer's A[beta](1-40) Amyloid Fibrils. J Mol Biol 373: 1321-1333.
    • (2007) J Mol Biol , vol.373 , pp. 1321-1333
    • Klement, K.1    Wieligmann, K.2    Meinhardt, J.3    Hortschansky, P.4    Richter, W.5
  • 42
    • 1542533563 scopus 로고    scopus 로고
    • Role of Protein-Water Interactions and Electrostatics in α-Synuclein Fibril Formation
    • Munishkina LA, Henriques J, Uversky VN, Fink AL, (2004) Role of Protein-Water Interactions and Electrostatics in α-Synuclein Fibril Formation. Biochemistry 43: 3289-3300.
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Uversky, V.N.3    Fink, A.L.4
  • 43
    • 13444269021 scopus 로고    scopus 로고
    • Critical Balance of Electrostatic and Hydrophobic Interactions Is Required for Beta2-Microglobulin Amyloid Fibril Growth and Stability
    • Raman B, Chatani E, Kihara M, Ban T, Sakai M, et al. (2005) Critical Balance of Electrostatic and Hydrophobic Interactions Is Required for Beta2-Microglobulin Amyloid Fibril Growth and Stability. Biochemistry 44: 1288-1299.
    • (2005) Biochemistry , vol.44 , pp. 1288-1299
    • Raman, B.1    Chatani, E.2    Kihara, M.3    Ban, T.4    Sakai, M.5
  • 44
    • 77956138054 scopus 로고    scopus 로고
    • Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein
    • Jain S, Udgaonkar JB, (2010) Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein. Biochemistry 49: 7615-7624.
    • (2010) Biochemistry , vol.49 , pp. 7615-7624
    • Jain, S.1    Udgaonkar, J.B.2
  • 45
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL, (1996) How Hofmeister ion interactions affect protein stability. Biophys J 71: 2056-2063.
    • (1996) Biophys J , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.