Propagation of Protein Aggregation in Neurodegenerative Diseases
Authors: Marc I Diamond
Jaime Vaquer-Alicea
Journal: Annual Review of Biochemistry (2019)
Discipline: BIOLOGY & BIOCHEMISTRY
Keywords: aggregation; amyloid; prion; propagation; strain
Affiliations: Center for Alzheimer's and Neurodegenerative Diseases, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA; email: .

Abstract:  Most common neurodegenerative diseases feature deposition of protein amyloids and degeneration of brain networks. Amyloids are ordered protein assemblies that can act as templates for their own replication through monomer addition. Evidence suggests that this characteristic may underlie the progression of pathology in neurodegenerative diseases. Many different amyloid proteins, including Aβ, tau, and α-synuclein, exhibit properties similar to those of infectious prion protein in experimental systems: discrete and self-replicating amyloid structures, transcellular propagation of aggregation, and transmissible neuropathology. This review discusses the contribution of prion phenomena and transcellular propagation to the progression of pathology in common neurodegenerative diseases such as Alzheimer's and Parkinson's. It reviews fundamental events such as cell entry, amplification, and transcellular movement. It also discusses amyloid strains, which produce distinct patterns of neuropathology and spread through the nervous system. These concepts may impact the development of new diagnostic and therapeutic strategies. 

Retracted: No

PubPeer comments:
 Figure 5B: much more similar than expected (red boxes) after brightness enhancement and vertical stretching. Could the authors please comment? ![file] , 
 Figure 6B: much more similar than expected (red boxes) after vertical stretching. Could the authors please comment? ![file] , 
 Figure 5A: **Procaspase-8 NA** and **actin HSC-4** panels appear to be much more similar than expected (pink boxes) after resizing and rotation. ![file] , 
 #1 Dear Aneurus Inconstans Thank you for your series of valuable suggestions. We will sincerely verify the matters pointed out. I m sorry, many collaborators have already resigned from academia. Therefore, we will report again after a while for verification. , 
 Expression of Concern published on 29 September 2021: https: onlinelibrary.wiley.com doi 10.1002 ijc.33825 It reads: This Expression of Concern is for the above article, published online on May 30, 2003, in Wiley Online Library (wileyonlinelibrary.com), and has been published by agreement between the journal Editor-in-Chief, the first and corresponding author, Dr. Masayasu Iwase, and John Wiley Sons, Ltd. The Expression of Concern has been agreed due to concerns regarding data presented in Figure 1, 5 and 6. In Figure 1B, in the right panel (HSC-4), bands #2-4 for FAS appear highly similar to bands #1-3 for GAPDH. In Figure 5A, bands for Procaspase-8 in u201cNAu201d appear similar to those for u03b2-actin in u201cHSC-4u2033. In Figure 5B, bands for c-FLIP in u201cNAu201d and for c-FLIP in u201cHSC-4u2033 appear similar after brightness enhancement and vertical stretching. In Figure 6B, bands for u03b2-actin in u201cNAu201d andu201d HSC-4u2033 appear similar after vertical stretching. The authors have been unable to provide original data underlying these images due to the time that has elapsed. The corresponding author does not agree to the above-mentioned issues in Figure 5Au2009+u2009B, but states that the mistakes in Figure 1B and Figure 6B occurred accidentally. He provided alternative images for correction of the issues in Figure 1B and Figure 6B, but due to the lack of original raw data, the origin of these images also remains uncertain. The authoru2019s institution, Showa University, has been contacted but no investigation was initiated. As a result, the journal is issuing this Expression of Concern to alert readers. , 
 #5 I realize only now that the Editorial Board spotted one additional problem in Figure 1B, kudos to them: ![file] ,