Prion protein and Aβ-related synaptic toxicity impairment
Prion protein and Aβ-related synaptic toxicity impairment
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DOI：
10.1002/emmm.201000082
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发表时间：
2010-08-01
影响因子：
11.1
通讯作者：
Aguzzi, Adriano
中科院分区：
文献类型：
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作者：
Calella, Anna Maria;Farinelli, Melissa;Aguzzi, Adriano
阿尔茨海默病（AD）是最常见的神经退行性疾病，其沿着细胞外淀粉样蛋白β（A β）沉积。在AD进展期间观察到的认知下降与海马和皮质中的受损的棘、树突和突触相关。许多研究表明，A β寡聚体，无论是合成的还是来自培养物和AD大脑的，都有力地损害了突触结构和功能。细胞朊蛋白（PrPc）被认为是介导这种效应的。我们报告说，消融或过表达的PrPc没有影响海马突触可塑性的损伤在AD的转基因模型。这些发现挑战了PrPc作为A β毒性介质的作用。
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.