Prion protein and Aβ-related synaptic toxicity impairment

被引：214

作者：

Calella, Anna Maria ^{[2
]}

Farinelli, Melissa ^{[1
]}

Nuvolone, Mario ^{[2
,3
]}

Mirante, Osvaldo ^{[1
]}

Moos, Rita ^{[2
]}

Falsig, Jeppe ^{[2
]}

Mansuy, Isabelle M. ^{[1
]}

Aguzzi, Adriano ^{[2
]}

机构：

[1] Univ Zurich, Dept Biol, Fac Med, Brain Res Inst,Swiss Fed Inst Technol, Zurich, Switzerland

[2] Univ Zurich Hosp, Inst Neuropathol, CH-8091 Zurich, Switzerland

[3] Univ Pavia, Fdn IRCCS Policlin San Matteo, Amyloid Ctr, Dept Internal Med, I-27100 Pavia, Italy

来源：

EMBO MOLECULAR MEDICINE | 2010年 / 2卷 / 08期

基金：

欧洲研究理事会; 新加坡国家研究基金会;

关键词：

Alzheimer's disease; amyloid; prion protein; synaptic plasticity; MICE; OLIGOMERS; PRP; MOUSE; PLASTICITY; MUTATION; DISEASE; MEMORY;

D O I：

10.1002/emmm.201000082

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

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

引用

页码：306 / 314

页数：9

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