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Cross-interactions between the Alzheimer Disease Amyloid-beta Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 4
2016 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 291, no 32, 16485-16493 p.Article, review/survey (Refereed) Published
Abstract [en]

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-beta (A beta) 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 A beta and other amyloid proteins.

Place, publisher, year, edition, pages
2016. Vol. 291, no 32, 16485-16493 p.
National Category
Biological Sciences
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URN: urn:nbn:se:su:diva-133372DOI: 10.1074/jbc.R116.714576ISI: 000380826700009PubMedID: 27325705OAI: oai:DiVA.org:su-133372DiVA: diva2:968074
Available from: 2016-09-12 Created: 2016-09-06 Last updated: 2016-09-12Bibliographically approved

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Wärmländer, Sebastian K. T. S.Gräslund, Astrid
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