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©2014 Baishideng Publishing Group Inc. All rights reserved.
Protein seeding in Alzheimer’s disease and Parkinson’s disease: Similarities and differences
Tarek Ibrahim, JoAnne McLaurin, Sunnybrook Research Institute and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M4N 3M5, Canada
Author contributions: Ibrahim T and McLaurin J contributed to this paper.
Supported by In part by CIHR MOP#102467 (McLaurin J); Cryptic Rite Charitable Foundation (McLaurin J)
Conflict-of-interest: The authors declare no conflict of interest with this publication.
Open-Access: This article is an open-access article which selected by an in-house editor and fully peer-reviewed by external reviewers. It distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Correspondence to: JoAnne McLaurin, PhD, Sunnybrook Research Institute and Department of Laboratory Medicine and Pathobiology, University of Toronto, 2075 Bayview Avenue, Rm S113, Toronto M4N 3M5, Canada. jmclaurin@sri.utoronto.ca
Telephone: +1-416-4806100-2270 Fax: +1-416-4805737
Received: September 30, 2014
Peer-review started: October 1, 2014
First decision: October 28, 2014
Revised: November 21, 2014
Accepted: December 3, 2014
Article in press: December 10, 2014
Published online: December 28, 2014
Processing time: 86 Days and 16 Hours
Peer-review started: October 1, 2014
First decision: October 28, 2014
Revised: November 21, 2014
Accepted: December 3, 2014
Article in press: December 10, 2014
Published online: December 28, 2014
Processing time: 86 Days and 16 Hours
Core Tip
Core tip: The disease-specific proteins of Alzheimer’s and Parkinson’s disease show many similarities as prion-like seeds in the brain. In addition to sharing structural features as misfolded proteins, the interactions and mechanisms that underlie the propagation of these proteins may also be shared, hijacking natural cellular responses in ways not unlike those of pore-forming toxins. Differences in temporal and spatial patterns of disease progression stems from the existence of conformational variants. Misfolded proteins that can be generated in vitro, can seed widespread pathology in non-transgenic animal models and question our understanding of disease progression in neurodegenerative diseases.