Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis

Neurology

Volumn 66, Issue 2 SUPPL. 1, 2006, Pages

  Glabe, Charles G ^a,b   Kayed, Rakez ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Kinexis Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CALCIUM; REACTIVE OXYGEN METABOLITE; AMYLOID BETA PROTEIN; BIOPOLYMER;

AMYLOIDOSIS; CALCIUM CELL LEVEL; CALCIUM HOMEOSTASIS; CELL DEATH; CELL FUNCTION; CONFERENCE PAPER; CONTROLLED STUDY; DEGENERATIVE DISEASE; HUMAN; HUMAN CELL; HUMAN TISSUE; INCLUSION BODY MYOSITIS; MEMBRANE PERMEABILITY; NEUROPATHOLOGY; OLIGOMERIZATION; OXIDATIVE STRESS; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; ALZHEIMER DISEASE; ANIMAL; ANTIBODY SPECIFICITY; CELL INCLUSION; CELL MEMBRANE PERMEABILITY; CHEMISTRY; DEMENTIA; DRUG DESIGN; HUNTINGTON CHOREA; IMMUNOLOGY; METABOLISM; MITOCHONDRION; MOUSE; PARKINSON DISEASE; PHYSIOLOGY; PROTEIN FOLDING; REVIEW; SOLUBILITY; TRANSGENIC MOUSE;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PROTEIN; AMYLOIDOSIS; ANIMALS; ANTIBODY SPECIFICITY; BIOPOLYMERS; CALCIUM; CELL MEMBRANE PERMEABILITY; DEMENTIA; DRUG DESIGN; HUMANS; HUNTINGTON DISEASE; INCLUSION BODIES; MICE; MICE, TRANSGENIC; MITOCHONDRIA; MYOSITIS, INCLUSION BODY; PARKINSON DISEASE; PROTEIN FOLDING; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33644861975     PISSN: 00283878     EISSN: None     Source Type: Journal    
DOI: 10.1212/01.wnl.0000192103.24796.42     Document Type: Conference Paper

References (53)

1. Bossy-Wetzel E, Schwarzenbacher R, Lipton SA. Molecular pathways to neurodegeneration. Nat Med 2004;10:S2-S9.
2. Bates G. Huntingtin aggregation and toxicity in Huntington's disease. Lancet 2003;361:1642-1644.
3. Terry RD. The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J Neuropathol Exp Neurol 1996;55:1023-1025.
4. McLean CA, Cherny RA, Fraser FW, et al. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 1999;46:860-866.
5. Lue TF, Kuo YM, Roher AE, et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Path 1999;155:853-862.
6. Hsia AY, Masliah E, McConlogue L, et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci 1999;96:3228-3233.
7. Westerman MA, Cooper-Blacketer D, Mariash A, et al. The relationship between Abeta and memory in the Tg2576 mouse model of Alzheimer's disease. J Neurosci 2002;22:1858-1867.
8. Burdick D, Soreghan B, Kwon M, et al. Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 1992;267:546-554.
9. Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K. Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J Mol Biol 1991;218:149-163.
10. Soreghan B, Kosmoski J, Glabe C. Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation. J Biol Chem 1994;269:28551-28554.
11. Garzon-Rodriguez W, Sepulveda-Becerra M, Milton S, Glabe CG. Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations. J Biol Chem 1997;272:21037-21044.
12. Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 1997;272:22364-22372.
13. Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of meta-stable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 1997;4:119-125.
14. Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury Jr PT. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002;418:291.
15. Anguiano M, Nowak RJ, Lansbury Jr PT. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 2002;41:11338-11343.
16. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc Natl Acad Sci 1997;94: 7942-7947.
17. Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from Abeta 1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci 1998;95:6448-6453.
18. Bucciantini M, Giannoni E, Chiti F, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002;416:507-511.
19. Conway KA, Harper JD, Lansbury Jr. PT. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 2000;39:2552-2563.
20. Janson J, Ashley RH, Harrison D, McIntyre S, Butler PC. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 1999;48:491-498.
21. Goldsbury CS, Wirtz S, Muller SA, et al. Studies on the in vitro assembly of Aβ1-40: Implications for the search for Aβ fibril formation inhibitors. J Str Biol 2000;130:217-231.
22. Tseng BP, Esler WP, Clish CB, et al. Deposition of monomeric, not oligomeric, Abeta mediates growth of Alzheimer's disease amyloid plaques in human brain preparations. Biochemistry 1999;38:10424-10431.
23. Esler WP, Stimson ER, Jennings JM, et al. Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 2000;39:6288-6295.
24. Nichols MR, Moss MA, Reed DK, et al. Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy. Biochemistry 2002;41:6115-6127.
25. Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci U S A 2002;99:11884-11889.
26. Serio TR, Cashikar AG, Kowal AS, et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000;289:1317-1321.
27. Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999;24:329-332.
28. Fandrich M, Dobson CM. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. Embo J 2002; 21:5682-5690.
29. Kirschner DA, Abraham C, Selkoe DJ. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation Proc Natl Acad Sci U.S.A. 1986;83:503-507.
30. Kirschner DA, Inouye H, Duffy LK, Sinclair A, Lind M, Selkoe DJ. Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc Natl Acad Sci U.S.A. 1987;84: 6953-6957.
31. Benzinger TL, Gregory DM, Burkoth TS, et al. Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register. Proc Natl Acad Sci 1998;95:13407-13412.
32. Balbach JJ, Petkova AT, Oyler NA, et al. Supramolecular Structure in Full-Length Alzheimer's beta-Amyloid Fibrils: Evidence for a Parallel beta-Sheet Organization from Solid- State Nuclear Magnetic Resonance. Biophys J 2002;83:1205-1216.
33. Antzutkin ON, Balbach JJ, Leapman RD, Rizzo NW, Reed J, Tycko R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci U S A 2000;97:13045-13050.
34. Torok M, Milton S, Kayed R, et al. Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling. J Biol Chem 2002;277:40810-40815.
35. Der-Sarkissian A, Jao CC, Chen J, Langen R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J Biol Chem 2003;278:37530-37535.
36. Barghorn S, Davies P, Mandelkow E. Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. Biochemistry 2004;43:1694-1703.
37. Margittai M, Langen R. Template-assisted filament growth by parallel stacking of tau. Proc Natl Acad Sci U S A 2004;101:10278-10283.
38. Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005;307:262-265.
39. Klein WL, Krafft GA, Finch CE. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 2001; 24:219-224.
40. Walsh DM, Klyubin I, Fadeeva JV, Rowan MJ, Selkoe DJ. Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition. Biochem Soc Trans 2002;30:552-557.
41. Kirkitadze MD, Bitan G, Teplow DB. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J Neurosci Res 2002;69:567-577.
42. Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003;26:267-298.
43. Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300:486-489.
44. Armen RS, DeMarco ML, Alonso DO, Daggett V. Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc Natl Acad Sci U S A 2004;101: 11622-11627.
45. Armen RS, Alonso DO, Daggett V. Anatomy of an amyloidogenic intermediate: conversion of beta-sheet to alpha-sheet structure in transthyretin at acidic pH. Structure (Camb) 2004;12:1847-1863.
46. Pauling L, Corey RB. The pleated sheet, a new layer configuration of the polypeptide chains. Proc Natl Acad Sci U S A 1951;37:251-256.
47. Kagan BL, Hirakura Y, Azimov R, Azimova R, Lin MC. The channel hypothesis of Alzheimer's disease: current status. Peptides 2002;23: 1311-1315.
48. Bucciantini M, Calloni G, Chiti F, et al. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 2004; 279:31374-31382.
49. Kayed R, Sokolov Y, Edmonds B, et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein Mis-folding diseases. J Biol Chem 2004; 279: 46363-46366.
50. Green JD, Kreplak L, Goldsbury C, et al. Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. J Mol Biol 2004;342:877-887.
51. Mina EW, Demuro A, Kayed R, Milton S, Parker I, Glabe CG. Membrane disruption and elevated intracellular calcium as a common mechanism of amyloid oligomer-induced neurodegeneration. Neuroscience Abstracts 2004;449:20.
52. Relini A, Torrassa S, Rolandi R, et al. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J Mol Biol 2004;338:943-957.
53. Sparr E, Engel MF, Sakharov DV, et al. Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. FEBS Lett 2004;577:117-120.