| Literature DB >> 27325705 |
Jinghui Luo1, Sebastian K T S Wärmländer2, Astrid Gräslund2, Jan Pieter Abrahams3.
Abstract
Many protein folding diseases are intimately associated with accumulation of amyloid aggregates. The amyloid materials formed by different proteins/peptides share many structural similarities, despite sometimes large amino acid sequence differences. Some amyloid diseases constitute risk factors for others, and the progression of one amyloid disease may affect the progression of another. These connections are arguably related to amyloid aggregates of one protein being able to directly nucleate amyloid formation of another, different protein: the amyloid cross-interaction. Here, we discuss such cross-interactions between the Alzheimer disease amyloid-β (Aβ) peptide and other amyloid proteins in the context of what is known from in vitro and in vivo experiments, and of what might be learned from clinical studies. The aim is to clarify potential molecular associations between different amyloid diseases. We argue that the amyloid cascade hypothesis in Alzheimer disease should be expanded to include cross-interactions between Aβ and other amyloid proteins.Entities:
Keywords: Alzheimer disease; amyloid; amyloid-beta (Aβ); cross-amyloid interaction; fibrillation; oligomer; oligomerization
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Year: 2016 PMID: 27325705 PMCID: PMC4974365 DOI: 10.1074/jbc.R116.714576
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157