title: Amyloid in neurodegenerative diseases: friend or foe?
abstract: Accumulation of amyloid-like aggregates is a hallmark of numerous neurodegenerative disorders such as Alzheimer's and polyglutamine disease. Yet, whether the amyloid inclusions found in these diseases are toxic or cytoprotective remains unclear. Various studies suggest that the toxic culprit in the amyloid folding pathway is actually a soluble oligomeric species which might interfere with normal cellular function by a multifactorial mechanism including aberrant protein-protein interactions. Molecular chaperones suppress toxicity of amyloidogenic proteins by inhibiting aggregation of non-native disease substrates and targeting them for refolding or degradation. Paradoxically, recent studies also suggest a protective action of chaperones in their promotion of the assembly of large, tightly packed, benign aggregates that sequester toxic protein species.
authors: Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, 107 Mason Farm Road, Chapel Hill, NC 27514, United States.
authors: Katie J
authors: KJ
authors: Wolfe
authors: Douglas M
authors: DM
authors: Cyr
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000378:metabolism*; D019610:Cytoprotection / Q000502:physiology; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D000682:Amyloid; D018832:Molecular Chaperones