From the Polymorphism of Amyloid Fibrils to their Assembly Mechanism and Cytotoxicity

Advances in Protein Chemistry

Volumn 73, Issue , 2006, Pages 217-233

  Kreplak, Laurent ^a   Aebi, Ueli ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; OLIGOMER;

CYTOTOXICITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN POLYMORPHISM; REVIEW;

AMYLOID; HUMANS; LIPIDS; NEURONS; PROTEIN STRUCTURE, QUATERNARY;

EID: 33845637320     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(06)73007-8     Document Type: Review

References (77)

1. Antzutkin O.N., Leapman R.D., Balbach J.J., and Tycko R. Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41 (2002) 15436-15450
2. Arispe N., Rojas E., and Pollard H.B. Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. USA 90 (1993) 567-571
3. Bauer H.H., Aebi U., Haner M., Hermann R., Muller M., and Merkle H.P. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol. 115 (1995) 1-15
4. Bennhold H. Eine specifische amyloidfärbung mit kongorot. Münch. Med. Wochenschr. 44 (1922) 1537-1538
5. Benzinger T.L., Gregory D.M., Burkoth T.S., Miller-Auer H., Lynn D.G., Botto R.E., and Meredith S.C. Propagating structure of Alzheimer's beta-amyloid (10-35) is parallel beta-sheet with residues in exact register. Proc. Natl. Acad. Sci. USA 95 (1998) 13407-13412
6. Blackley H.K., Sanders G.H., Davies M.C., Roberts C.J., Tendler S.J., and Wilkinson M.J. In-situ atomic force microscopy study of beta-amyloid fibrillization. J. Mol. Biol. 298 (2000) 833-840
7. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
8. Cardoso I., Goldsbury C.S., Muller S.A., Olivieri V., Wirtz S., Damas A.M., Aebi U., and Saraiva M.J. Transthyretin fibrillogenesis entails the assembly of monomers: A molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317 (2002) 683-695
9. Chothia C. Coiling of beta-pleated sheets. J. Mol. Biol. 163 (1983) 107-117
10. Cohen A.S., and Calkins E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183 (1959) 1202-1203
11. Conway K.A., Harper J.D., and Lansbury P.T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4 (1998) 1318-1320
12. Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273 (1998) 9443-9449
13. Demuro A., Mina E., Kayed R., Milton S.C., Parker I., and Glabe C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280 (2005) 17294-17300
14. Divry P., and Florkin M. On the optical properties of amyloid. C. R. Soc. Biol. 97 (1927) 1808-1810
15. Eanes E.D., and Glenner G.G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16 (1968) 673-677
16. Flock D., Colacino S., Colombo G., and Di Nola A. Misfolding of the amyloid beta-protein: A molecular dynamics study. Proteins 62 (2006) 183-192
17. Goldsbury C.S., Cooper G.J., Goldie K.N., Muller S.A., Saafi E.L., Gruijters W.T., Misur M.P., Engel A., Aebi U., and Kistler J. Polymorphic fibrillar assembly of human amylin. J. Struct. Biol. 119 (1997) 17-27
18. Goldsbury C., Kistler J., Aebi U., Arvinte T., and Cooper G.J. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285 (1999) 33-39
19. Goldsbury C., Goldie K., Pellaud J., Seelig J., Frey P., Muller S.A., Kistler J., Cooper G.J., and Aebi U. Amyloid fibril formation from full-length and fragments of amylin. J. Struct. Biol. 130 (2000) 352-362
20. Goldsbury C.S., Wirtz S., Muller S.A., Sunderji S., Wicki P., Aebi U., and Frey P. Studies on the in vitro assembly of A beta 1-40: Implications for the search for A beta fibril formation inhibitors. J. Struct. Biol. 130 (2000) 217-231
21. Goldsbury C., Aebi U., and Frey P. Visualizing the growth of Alzheimer's A beta amyloid-like fibrils. Trends Mol. Med. 7 (2001) 582
22. Goldsbury C., Frey P., Olivieri V., Aebi U., and Muller S.A. Multiple assembly pathways underlie amyloid-beta fibril polymorphisms. J. Mol. Biol. 352 (2005) 282-298
23. Green J.D., Goldsbury C., Mini T., Sunderji S., Frey P., Kistler J., Cooper G., and Aebi U. Full-length rat amylin forms fibrils following substitution of single residues from human amylin. J. Mol. Biol. 326 (2003) 1147-1156
24. Green J.D., Goldsbury C., Kistler J., Cooper G.J., and Aebi U. Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation. J. Biol. Chem. 279 (2004) 12206-12212
25. Green J.D., Kreplak L., Goldsbury C., Li Blatter X., Stolz M., Cooper G.S., Seelig A., Kistler J., and Aebi U. Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. J. Mol. Biol. 342 (2004) 877-887
26. Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297 (2002) 353-356
27. Harper J.D., Wong S.S., Lieber C.M., and Lansbury P.T. Observation of metastable A beta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4 (1997) 119-125
28. Harper J.D., Wong S.S., Lieber C.M., and Lansbury Jr. P.T. Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease. Biochemistry 38 (1999) 8972-8980
29. Hartley D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., Teplow D.B., and Selkoe D.J. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 8876-8884
30. Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., and Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. USA 102 (2005) 15871-15876
31. Herrmann H., and Aebi U. Intermediate filament assembly: Temperature sensitivity and polymorphism. Cell. Mol. Life Sci. 55 (1999) 1416-1431
32. Hertel C., Terzi E., Hauser N., Jakob-Rotne R., Seelig J., and Kemp J.A. Inhibition of the electrostatic interaction between beta-amyloid peptide and membranes prevents beta-amyloid-induced toxicity. Proc. Natl. Acad. Sci. USA 94 (1997) 9412-9416
33. Higham C.E., Jaikaran E.T., Fraser P.E., Gross M., and Clark A. Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils. FEBS Lett. 470 (2000) 55-60
34. Hirakura Y., and Kagan B.L. Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid 8 (2001) 94-100
35. Hiramatsu H., Goto Y., Naiki H., and Kitagawa T. Core structure of amyloid fibril proposed from IR-microscope linear dichroism. J. Am. Chem. Soc. 126 (2004) 3008-3009
36. Hirota-Nakaoka N., Hasegawa K., Naiki H., and Goto Y. Dissolution of beta2-microglobulin amyloid fibrils by dimethylsulfoxide. J. Biochem. (Tokyo) 134 (2003) 159-164
37. Hoyer W., Antony T., Cherny D., Heim G., Jovin T.M., and Subramaniam V. Dependence of alpha-synuclein aggregate morphology on solution conditions. J. Mol. Biol. 322 (2002) 383-393
38. Huff M.E., Balch W.E., and Kelly J.W. Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr. Opin. Struct. Biol. 13 (2003) 674-682
39. Jansen R., Dzwolak W., and Winter R. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88 (2005) 1344-1353
40. Jimenez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., and Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18 (1999) 815-821
41. Jones E.M., and Surewicz W.K. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121 (2005) 63-72
42. Kad N.M., Myers S.L., Smith D.P., Smith D.A., Radford S.E., and Thomson N.H. Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330 (2003) 785-797
43. Kajava A.V., Aebi U., and Steven A.C. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348 (2005) 247-252
44. Kayed R., Sokolov Y., Edmonds B., McIntire T.M., Milton S.C., Hall J.E., and Glabe C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279 (2004) 46363-46366
45. Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6 (1996) 11-17
46. Khurana R., Coleman C., Ionescu-Zanetti C., Carter S.A., Krishna V., Grover R.K., Roy R., and Singh S. Mechanism of thioflavin T binding to amyloid fibrils. J. Struct. Biol. 151 (2005) 229-238
47. Krebs M.R., Bromley E.H., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: Localisation and implications. J. Struct. Biol. 149 (2005) 30-37
48. Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., Morgan T.E., Rozovsky I., Trommer B., Viola K.L., Wals P., Zhang C., et al. Diffusible, nonfibrillar ligands derived from A beta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA 95 (1998) 6448-6453
49. Lashuel H.A., Lai Z., and Kelly J.W. Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37 (1998) 17851-17864
50. Lashuel H.A., Petre B.M., Wall J., Simon M., Nowak R.J., Walz T., and Lansbury Jr. P.T. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002) 1089-1102
51. LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
52. Lin H., Bhatia R., and Lal R. Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology. FASEB J. 15 (2001) 2433-2444
53. Lorenzo A., and Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91 (1994) 12243-12247
54. Luhrs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Dobeli H., Schubert D., and Riek R. 3D structure of Alzheimer's amyloid-{beta}(1-42) fibrils. Proc. Natl. Acad. Sci. USA 102 (2005) 17342-17347
55. Maiti N.C., Apetri M.M., Zagorski M.G., Carey P.R., and Anderson V.E. Raman spectroscopic characterization of secondary structure in natively unfolded proteins: Alpha-synuclein. J. Am. Chem. Soc. 126 (2004) 2399-2408
56. Malisauskas M., Zamotin V., Jass J., Noppe W., Dobson C.M., and Morozova-Roche L.A. Amyloid protofilaments from the calcium-binding protein equine lysozyme: Formation of ring and linear structures depends on pH and metal ion concentration. J. Mol. Biol. 330 (2003) 879-890
57. Millonig R., Salvo H., and Aebi U. Probing actin polymerization by intermolecular cross-linking. J. Cell Biol. 106 (1988) 785-796
58. Mirzabekov T.A., Lin M.C., and Kagan B.L. Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271 (1996) 1988-1992
59. Nielsen E.H., Nybo M., and Svehag S.E. Electron microscopy of prefibrillar structures and amyloid fibrils. Methods Enzymol. 309 (1999) 491-496
60. Owen R.J., Heyes C.D., Knebel D., Rocker C., and Nienhaus G.U. An integrated instrumental setup for the combination of atomic force microscopy with optical spectroscopy. Biopolymers 82 (2005) 410-414
61. Petkova A.T., Ishii Y., Balbach J.J., Antzutkin O.N., Leapman R.D., Delaglio F., and Tycko R. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. USA 99 (2002) 16742-16747
62. Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
63. Quist A., Doudevski I., Lin H., Azimova R., Ng D., Frangione B., Kagan B., Ghiso J., and Lal R. Amyloid ion channels: A common structural link for protein-misfolding disease. Proc. Natl. Acad. Sci. USA 102 (2005) 10427-10432
64. Reichlin T., Wild A., Durrenberger M., Daniels A.U., Aebi U., Hunziker P.R., and Stolz M. Investigating native coronary artery endothelium in situ and in cell culture by scanning force microscopy. J. Struct. Biol. 152 (2005) 52-63
65. Relini A., Torrassa S., Rolandi R., Gliozzi A., Rosano C., Canale C., Bolognesi M., Plakoutsi G., Bucciantini M., Chiti F., and Stefani M. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J. Mol. Biol. 338 (2004) 943-957
66. Serpell L.C. Alzheimer's amyloid fibrils: Structure and assembly. Biochim. Biophys. Acta 1502 (2000) 16-30
67. Shirahama T., and Cohen A.S. High-resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33 (1967) 679-708
68. Sipe J.D., and Cohen A.S. Review: History of the amyloid fibril. J. Struct. Biol. 130 (2000) 88-98
69. Stolz M., Stoffler D., Aebi U., and Goldsbury C. Monitoring biomolecular interactions by time-lapse atomic force microscopy. J. Struct. Biol. 131 (2000) 171-180
70. Sunde M., Serpell L.C., Bartlam M., Fraser P.E., Pepys M.B., and Blake C.C. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273 (1997) 729-739
71. Terzi E., Holzemann G., and Seelig J. Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252 (1995) 633-642
72. Terzi E., Holzemann G., and Seelig J. Interaction of Alzheimer beta-amyloid peptide (1-40) with lipid membranes. Biochemistry 36 (1997) 14845-14852
73. Tomiyama T., Asano S., Suwa Y., Morita T., Kataoka K., Mori H., and Endo N. Rifampicin prevents the aggregation and neurotoxicity of amyloid beta protein in vitro. Biochem. Biophys. Res. Commun. 204 (1994) 76-83
74. Virchow R. Bav and Zussmmersetzying der Corporci Amalacca des Menschen. Vehr Phys Med. Geswurzlurg 2 (1851) 51-53
75. Walsh D.M., Lomakin A., Benedek G.B., Condron M.M., and Teplow D.B. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272 (1997) 22364-22372
76. Walsh D.M., Hartley D.M., Kusumoto Y., Fezoui Y., Condron M.M., Lomakin A., Benedek G.B., Selkoe D.J., and Teplow D.B. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274 (1999) 25945-25952
77. Wetzel R. Ideas of order for amyloid fibril structure. Structure (Camb.) 10 (2002) 1031-1036