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Prion protein and Abeta-related synaptic toxicity impairment.

ABSTRACT: Alzheimer's disease (AD), the most common neurodegenerative disorder, goes along with extracellular amyloid-beta (Abeta) deposits. The cognitive decline observed during AD progression correlates with damaged spines, dendrites and synapses in hippocampus and cortex. Numerous studies have shown that Abeta oligomers, both synthetic and derived from cultures and AD brains, potently impair synaptic structure and functions. The cellular prion protein (PrP(C)) was proposed to mediate this effect. We report that ablation or overexpression of PrP(C) had no effect on the impairment of hippocampal synaptic plasticity in a transgenic model of AD. These findings challenge the role of PrP(C) as a mediator of Abeta toxicity.

SUBMITTER: Calella AM

PROVIDER: S-EPMC2962809 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Prion protein and Abeta-related synaptic toxicity impairment.

Calella Anna Maria AM Farinelli Mélissa M Nuvolone Mario M Mirante Osvaldo O Moos Rita R Falsig Jeppe J Mansuy Isabelle M IM Aguzzi Adriano A

EMBO molecular medicine 20100801 8

Alzheimer's disease (AD), the most common neurodegenerative disorder, goes along with extracellular amyloid-beta (Abeta) deposits. The cognitive decline observed during AD progression correlates with damaged spines, dendrites and synapses in hippocampus and cortex. Numerous studies have shown that Abeta oligomers, both synthetic and derived from cultures and AD brains, potently impair synaptic structure and functions. The cellular prion protein (PrP(C)) was proposed to mediate this effect. We re ...[more]

PMID: 20665634

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