Biological membranes as protein aggregation matrices and targets of amyloid toxicity

Methods in Molecular Biology

Volumn 648, Issue , 2010, Pages 231-243

  Bucciantini, Monica ^a   Cecchi, Cristina ^a  

^a NONE

Author keywords

Amyloid aggregates; Atomic force microscopy; Confocal laser microscopy; Electron microscopy; Flow cytometry; Loss of membrane integrity; Plasma membranes

Indexed keywords

AMYLOID BETA PROTEIN; PROTEIN AGGREGATE; AMYLOID;

ATOMIC FORCE MICROSCOPY; BIOMEMBRANE; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELLS BY BODY ANATOMY; CONFOCAL LASER SCANNING MICROSCOPY; CONTROLLED STUDY; FLOW CYTOMETRY; HUMAN; HUMAN CELL; IN VIVO STUDY; LIPID MEMBRANE; MEMBRANE STRUCTURE; NEUROTOXICITY; PROTEIN AGGREGATION; PROTEIN LIPID INTERACTION; PROTEIN MISFOLDING; PROTEIN UNFOLDING; TRANSMISSION ELECTRON MICROSCOPY; ARTICLE; CHEMISTRY; CONFOCAL MICROSCOPY; DRUG EFFECT; FLUORESCENT ANTIBODY TECHNIQUE; MEMBRANE; METHODOLOGY; MICROSCOPY; PROTEIN QUATERNARY STRUCTURE; TUMOR CELL LINE; ULTRASTRUCTURE;

AMYLOID; CELL LINE, TUMOR; FLOW CYTOMETRY; FLUORESCENT ANTIBODY TECHNIQUE; HUMANS; MEMBRANES; MICROSCOPY; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, CONFOCAL; PROTEIN STRUCTURE, QUATERNARY;

EID: 79952021123     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-756-3_15     Document Type: Chapter

References (22)

1. 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
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. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486–489
4. Cecchi C, Baglioni S, Fiorillo C, Pensalfini A, Liguri G, Nosi D, Rigacci S, Bucciantini M, Stefani M (2005) Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates. J Cell Sci 118:3459–3470
5. Kourie JI, Henry CL (2002) Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules. Clin Exp Pharmacol Physiol 29:741–753
6. 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
7. Cecchi C, Nichino D, Zampagni M, Bernacchioni C, Evangelisti E, Liguri G, Pensalfini A, Gliozzi A, Stefani M, Relini A (2009) A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells. Biochim Biophys Acta 1788:2204–2216
8. Gosal WS, Meyers SL, Radford SE, Thomson NH (2006) Amyloid under the atomic force microscope. Protein Pept Lett 13:261–270
9. Santos NC, Castanho MA (2004) An over-wiew of the biophysical applications of atomic force microscopy. Biophys Chem 2:133–149
10. Möller C, Allen M, Elings V, Engel A, Müller DJ (1999) Tapping-mode atomic microscopy produces faithful high-resolution images of protein surfaces. Biophys J 77:1150–1158
11. Müller DJ, Fotiadis D, Scheurig S, Müller SA, Engel A (1999) Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys J 76:1101–1111
12. Tashima Y, Oe R, Lee S, Sugihara G (2004) The effect of cholesterol and monosialogan-glioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids. J Biol Chem 279:17587–17595
13. Diociaiuti M, Polzi LZ, Valvo L, Malchiodi-Albedi F, Bombelli C, Gaudiano MC (2006) Calcitonin forms oligomeric pore-like structures in lipid membranes. Biophys J 91:2275–2281
14. Engel MFM, Khemtemourian L, Kleijer CC, Meeldijk HJD, Jacobs J, Verkleij AJ, de Kruijff B, Killian JA, Hoppener JWM (2008) Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. PNAS 105:6033–6038
15. Pieri L, Bucciantini M, Guasti P, Savistchenk J, Melki R, Stefani M (2009) Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicles permeabilization and charge selectivity. Biophis J 96:3319–3330
16. Selkoe DJ (2001) Alzheimer’s disease: genes, proteins, and therapy. PhysiolRev 81:741–766
17. Dahlgren KN, Manelli AM, Stine WB, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-β peptides dif-ferentially affect neuronal viability. J Biol Chem 277:32046–32053
18. Klein WL (2002) Aβ toxicity in Alzheimer’s disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Intl 41:345–352
19. Lacor PN, Buniel MC, Chang L, Fernandez SJ, Gong Y, Viola KL, Lambert MP, Velasco PT, Bigio EH, Finch CE, Krafft GA, Klein WI (2004) Synaptic targeting by Alzheimer’s-related amyloid β oligomers. J Neurosci 24:10191–10200
20. Wakabayashi M, Okada T, Kozutsumi Y, Matsuzaki K (2005) GM1 ganglioside-medi-ated accumulation of amyloid beta-protein on cell membranes. Biochim Biophys Res Com 328:1019–1023
21. Demuro A, Mina E, Kayed R, Milton S, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294–17300
22. Kayed R, Pensalfini A, Margol L, Sokolov Y, Sarsoza F, Head E, Hall J, Glabe CG (2009) Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284:4230–4237