Cellular Prion Protein as a Receptor of Toxic Amyloid-β42 Oligomers Is Important for Alzheimer’s Disease

• Published in: Frontiers in cellular neuroscience Vol. 13; p. 339
• Main Authors: Zhang, Yuan, Zhao, Yanfang, Zhang, Lei, Yu, Wanpeng, Wang, Yu, Chang, Wenguang
• Format: Journal Article
• Language: English
• Published: Switzerland Frontiers Research Foundation 30.07.2019; Frontiers Media S.A
• Subjects: Alzheimer's disease; amyloid-β; Binding sites; Brain; cellular prion protein; Cognitive ability; Disease; Hypotheses; Neurofibrillary tangles; Neuroscience; Neurotoxicity; oligomers; Pathogenesis; Pathology; Prion protein; Proteins; receptor; Senile plaques; Tau protein; China; amyloid-β; receptor; Alzheimer’s disease; cellular prion protein; oligomers
• ISSN: 1662-5102; 1662-5102
• DOI: 10.3389/fncel.2019.00339

The pathological features of Alzheimer's disease (AD) include senile plaques induced by amyloid-β (Aβ) protein deposits, neurofibrillary tangles formed by aggregates of hyperphosphorylated tau proteins and neuronal cell loss in specific position within the brain. Recent observations have suggested the possibility of an association between AD and cellular prion protein (PrP ) levels. PrP is a high affinity receptor for oligomeric Aβ and is important for Aβ-induced neurotoxicity and thus plays a critical role in AD pathogenesis. The determination of the relationship between PrP and AD and the characterization of PrP binding to Aβ will facilitate the development of novel therapies for AD.