scholarly journals Alzheimer’s Amyloid-β Oligomers Rescue Cellular Prion Protein Induced Tau Reduction via the Fyn Pathway

2013 ◽  
Vol 4 (9) ◽  
pp. 1287-1296 ◽  
Author(s):  
Rong-Jie Chen ◽  
Wei-Wei Chang ◽  
Yu-Chun Lin ◽  
Pei-Lin Cheng ◽  
Yun-Ru Chen
Keyword(s):  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein

scholarly journals Prion protein and prion disease at a glance

2021 ◽  
Vol 134 (17) ◽  
Author(s):  
Caihong Zhu ◽  
Adriano Aguzzi
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Neurodegenerative Disorders ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Future Studies ◽  
Associated Proteins ◽  
Main Component ◽  
Conformational Conversion

ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the phenomenon of prionoid, or prion-like, spread has also been observed in many other disease-associated proteins, such as amyloid β (Aβ), tau and α-synuclein. This Cell Science at a Glance and the accompanying poster highlight recently described physiological roles of prion protein and the advanced understanding of pathogenesis of prion disease they have afforded. Importantly, prion protein may also be involved in the pathogenesis of other neurodegenerative disorders such as Alzheimer's and Parkinson's disease. Therapeutic studies of prion disease have also exploited novel strategies to combat these devastating diseases. Future studies on prion protein and prion disease will deepen our understanding of the pathogenesis of a broad spectrum of neurodegenerative conditions.

scholarly journals Impact of the Cellular Prion Protein on Amyloid-β and 3PO-Tau Processing

2013 ◽  
Vol 38 (3) ◽  
pp. 551-565 ◽  
Author(s):  
Matthias Schmitz ◽  
Katharina Wulf ◽  
Sandra C. Signore ◽  
Walter J. Schulz-Schaeffer ◽  
Pawel Kermer ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein

scholarly journals Targeting glutamatergic and cellular prion protein mechanisms of amyloid β-mediated persistent synaptic plasticity disruption: Longitudinal studies

2017 ◽  
Vol 121 ◽  
pp. 231-246 ◽  
Author(s):  
Dainan Zhang ◽  
Yingjie Qi ◽  
Igor Klyubin ◽  
Tomas Ondrejcak ◽  
Claire J. Sarell ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Longitudinal Studies ◽  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein

scholarly journals Dextran sulfate sodium inhibits amyloid-β oligomer binding to cellular prion protein

2015 ◽  
Vol 134 (4) ◽  
pp. 611-617 ◽  
Author(s):  
Takahiro Aimi ◽  
Koichiro Suzuki ◽  
Tatsuya Hoshino ◽  
Tohru Mizushima
Keyword(s):  
Prion Protein ◽  
Dextran Sulfate ◽  
Dextran Sulfate Sodium ◽  
Amyloid Β ◽  
Cellular Prion Protein

scholarly journals Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Nature ◽  
2009 ◽  
Vol 457 (7233) ◽  
pp. 1128-1132 ◽  
Author(s):  
Juha Laurén ◽  
David A. Gimbel ◽  
Haakon B. Nygaard ◽  
John W. Gilbert ◽  
Stephen M. Strittmatter
Keyword(s):  
Synaptic Plasticity ◽  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein

scholarly journals Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier

2012 ◽  
Vol 32 (4) ◽  
pp. 628-632 ◽  
Author(s):  
Thorsten Pflanzner ◽  
Benjamin Petsch ◽  
Bettina André-Dohmen ◽  
Andreas Müller-Schiffmann ◽  
Sabrina Tschickardt ◽  
...  
Keyword(s):  
Prion Protein ◽  
Blood Brain Barrier ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Brain Barrier ◽  
Putative Receptor ◽  
Blood Brain ◽  
In Vitro Bbb Model

The blood—brain barrier (BBB) facilitates amyloid-β (Aβ) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating Aβ neurotoxicity in Alzheimer's disease (AD), participates in Aβ transcytosis across the BBB. Using an in vitro BBB model, [125I]-Aβ1–40 transcytosis was reduced by genetic knockout of PrPc or after addition of a competing PrPc-specific antibody. Furthermore, we provide evidence that PrPc is expressed in endothelial cells and, that monomeric Aβ1–40 binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD.

scholarly journals mGlu5 receptors and cellular prion protein mediate amyloid-β-facilitated synaptic long-term depression in vivo

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Neng-Wei Hu ◽  
Andrew J. Nicoll ◽  
Dainan Zhang ◽  
Alexandra J. Mably ◽  
Tiernan O’Malley ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Long Term Depression ◽  
Mglu5 Receptors
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