Prefibrillar amyloid aggregates could be generic toxins in higher organisms

Journal of Neuroscience

Volumn 26, Issue 31, 2006, Pages 8160-8167

  Baglioni, Serena ^a   Casamenti, Fiorella ^a   Bucciantini, Monica ^a,b   Luheshi, Leila M ^b   Taddei, Niccolò ^a,b   Chiti, Fabrizio ^a   Dobson, Christopher M ^b   Stefani, Massimo ^a,b  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Aggregate microinjection; Amyloid fibrils; Cell dysfunction; Neurodegenerative diseases; Protein aggregation; Protein misfolding

Indexed keywords

AMYLOID; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN; PROTEIN HYPF; TOXIN; UNCLASSIFIED DRUG; HYPF N PROTEIN, HUMAN; HYPF-N PROTEIN, HUMAN;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELL DEATH; CELL FUNCTION; CELL VIABILITY; CHOLINERGIC NERVE CELL; CONTROLLED STUDY; CYTOTOXICITY; HOMEOSTASIS; INFLAMMATION; MAGNOCELLULAR NUCLEUS; MALE; MEMBRANE PERMEABILITY; NONHUMAN; OLIVARY NUCLEUS; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; RAT; SRC HOMOLOGY DOMAIN; ANIMAL; BRAIN; CELL CULTURE; CHEMICALLY INDUCED DISORDER; DEGENERATIVE DISEASE; DOSE RESPONSE; DRUG EFFECT; NERVE CELL; PATHOLOGY; WISTAR RAT;

AMYLOID; ANIMALS; BRAIN; CELLS, CULTURED; DOSE-RESPONSE RELATIONSHIP, DRUG; MALE; NEURODEGENERATIVE DISEASES; NEURONS; PROTEINS; RATS; RATS, WISTAR; TOXINS, BIOLOGICAL;

EID: 33748210163     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4809-05.2006     Document Type: Article

References (38)

1. Brofman FC, Moechars D, Van Leuven F (2000) Acetylcholinesterase-positive fiber deafferentation and cell shrinkage in the septohippocampal pathway of aged amyloid precursor protein London mutant transgenic mice. Neurobiol Dis 7:152-168.
2. Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, Stefani M (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416:507-511.
3. Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, Dobson CM, Stefani M (2004) Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 279:31374-31382.
4. Bucciantini M, Rigacci S, Berti A, Pieri L, Cecchi C, Nosi D, Formigli L, Chiti F, Stefani M (2005) Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. FASEB J 19:437-439.
5. Carulla N, Caddy GL, Hall DR, Zurdo J, Gairi M, Felix M, Giralt E, Robinson CV, Dobson CM (2005) Molecular recycling within amyloid fibrils. Nature 436:584-588.
6. Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 10:2541-2547.
7. Cleary JP, Walsh DM, Hofmeister JJ, Shankar GM, Kuskowski MA, Selkoe DJ, Ashe KH (2005) Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat Neurosci 8:79-84.
8. Conway KA, Lee SJ, Rochet JC, Ding TT, Harper JD, Williamson RE, Lansbury Jr PT (2000) Acceleration of oligomerization not fibrillization is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease. Implication for pathogenesis and therapy. Proc Natl Acad Sci USA 97:571-576.
9. Dobson CM (2003) Protein folding and misfolding. Nature 426:884-890.
10. Fändrich M, Dobson CM (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 21:5682-5690.
11. Fezoui Y, Hartley DM, Walsh DM, Selkoe DJ, Osterhout JJ, Teplow DB (2000) A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils. Nat Struct Biol 7:1095-1099.
12. Giovannelli L, Scali C, Faussone-Pellegrini MS, Pepeu G, Casamenti F (1998) Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain. Neurochemistry 87:349-357.
13. Giovannini MG, Scali C, Prosperi C, Bellucci A, Vannucchi MG, Rosi S, Pepeu G, Casamenti F (2002) β-amyloid-induced inflammation and cholinergic hypofunction in the rat brain in vivo: involvement of the p38MAPK pathway. Neurobiol Dis 11:257-274.
14. Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426:895-899.
15. Goldberg MS, Lansbury PT (2000) Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat Cell Biol 2:E115-E119.
16. Gong Y, Chang L, Viola KL, Lacor PN, Lambert MP, Finch CE, Krafft GA, Klein WL (2003) Alzheimer's disease-affected brain: presence of oligomeric Aβ ligands (ADDSLs) suggest a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100:10417-10422.
17. Guijarro JL, Sunde M, Jones JA, Campbell ID, Dobson CM (1998) Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 95:4224-4228.
18. Hoshi M, Sato M, Matsumoto S, Noguchi A, Yasutake K, Yoshida N, Sato K (2003) Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. Proc Natl Acad Sci USA 100:6370-6375.
19. Huff ME, Balch WE, Kelly JW (2003) Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr Opin Struct Biol 13:674-682.
20. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG (2003) Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis. Science 300:486-489.
21. Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, Hall JE, Glabe CG (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279:46363-46366.
22. Kelly J (1998) Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8:101-106.
23. Kranenburg O, Kroon-Batenburg LM, Reijerkerk A, Wu YP, Voest EE, Gebbink MF (2003) Recombinant endostatin forms amyloid fibrils that bind and are cytotoxic to murine neuroblastoma cells in vitro. FEBS Lett 539:149-155.
24. Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M, Ashe KH (2006) A specific amyloid-β protein assembly in the brain impairs memory. Nature 440:352-357.
25. Merlini G, Westermark P (2004) The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies. J Intern Med 255:159-178.
26. Nilsberth C, Westlind-Danielsson A, Eckman CB, Condron MM, Axelman K, Forsell C, Stenh C, Luthman J, Teplow DB, Younkin SG, Naslund J, Lannfelt L (2001) The "arctic" APP mutation. (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nat Neurosci 4:887-893.
27. Paxinos G, Watson G (1998) The rat brain in stereotaxic coordinates. New York: Academic.
28. Relini A, Torrassa S, Rolandi R, Gliozzi A, Rosano C, Canale C, Bolognesi M, Plakoutsi G, Bucciantini M, Chiti F, Stefani M (2004) Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J Mol Biol 338:943-957.
29. Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426:900-904.
30. Selkoe DJ (2004) Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6:1054-1061.
31. Serpell LC, Sunde M, Benson MD, Tennent GA, Pepys MB, Fraser PE (2000) The protofilament substructure of amyloid fibrils. J Mol Biol 300:1033-1039.
32. Sirangelo I, Malmo C, Iannuzzi C, Mezzogiorno A, Bianco MR, Papa M, Irace G (2004) Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F. J Biol Chem 279:13183-13189.
33. Sitia R, Braakman I (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426:891-894.
34. Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81:678-699.
35. Tycko R (2004) Progress towards a molecular-level structural understanding of amyloid fibrils. Curr Opin Struct Biol 14:96-103.
36. Walsh DM, Selkoe DJ (2004) Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 11:213-228.
37. Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416:535-539.
38. Wogulis M, Wright S, Cunningham D, Chilcote T, Powell K, Rydel RE (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 25:1071-1080.