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Cellular Prion Protein as a Receptor of Toxic Amyloid-?42 Oligomers Is Important for Alzheimer's Disease.

ABSTRACT: The pathological features of Alzheimer's disease (AD) include senile plaques induced by amyloid-? (A?) 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 C ) levels. PrP C is a high affinity receptor for oligomeric A? and is important for A?-induced neurotoxicity and thus plays a critical role in AD pathogenesis. The determination of the relationship between PrP C and AD and the characterization of PrP C binding to A? will facilitate the development of novel therapies for AD.

SUBMITTER: Zhang Y

PROVIDER: S-EPMC6682659 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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

Zhang Yuan Y Zhao Yanfang Y Zhang Lei L Yu Wanpeng W Wang Yu Y Chang Wenguang W

Frontiers in cellular neuroscience 20190730

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 C ) levels. PrP C is a high affinity receptor for oligomeric Aβ and is important for Aβ- ...[more]

PMID: 31417361

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Cellular prion protein as a receptor for amyloid-β oligomers in Alzheimer's disease.

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