Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Cellular Prion Protein and Amyloid – β Oligomers in Alzheimer's Disease – There Are Connections?

Naomi Hachiya
,
Michał Fułek
ORCID logo ,
Katarzyna Zajączkowska
ORCID logo ,
Donata Kurpas
,
Elżbieta Trypka
,
Jerzy Leszek
*
Version 1 : Received: 2 May 2021 / Approved: 5 May 2021 / Online: 5 May 2021 (10:45:04 CEST)

How to cite: Hachiya, N.; Fułek, M.; Zajączkowska, K.; Kurpas, D.; Trypka, E.; Leszek, J. Cellular Prion Protein and Amyloid – β Oligomers in Alzheimer's Disease – There Are Connections?. Preprints 2021, 2021050032. https://doi.org/10.20944/preprints202105.0032.v1 Hachiya, N.; Fułek, M.; Zajączkowska, K.; Kurpas, D.; Trypka, E.; Leszek, J. Cellular Prion Protein and Amyloid – β Oligomers in Alzheimer's Disease – There Are Connections?. Preprints 2021, 2021050032. https://doi.org/10.20944/preprints202105.0032.v1

Abstract

Alzheimer’s disease (AD) is the most common cause of dementia worldwide. Pathological deposits of neurotoxin proteins within the brain, such as amyloid-Beta and hyperphosphorylated tau tangles, are prominent features in AD. The prion protein (PrP) is involved in neurodegeneration via its conversion from the normal cellular form PrPc, to the infection form PrP Sc. Some studies indicated that posttranslationally modified PrPc isoforms plays a fundamental role in AD pathological progression. Several studies have shown that interaction of Aβ oligomers with N-terminal residues of the PrPc protein region appears critical for neuronal toxicity. The PrPc-Aβ binding always occur in AD brains and is never detected in nondemented controls and the binding of Aβ aggregates to PrPc is restricted to the N-terminus of PrPc.

Keywords

Alzheimer’s disease; cellular prion protein; amyloid β and PrP interaction in Alzheimer’s; BACE1; Aβ

Subject

Medicine and Pharmacology, Immunology and Allergy

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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