β-淀粉样寡聚体和阿尔茨海默病中的细胞朊病毒蛋白。
Beta-amyloid oligomers and cellular prion protein in Alzheimer's disease.
机构信息
Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University School of Medicine, 295 Congress Ave., BCMM 436, New Haven, CT 06536-0812, USA.
出版信息
J Mol Med (Berl). 2010 Apr;88(4):331-8. doi: 10.1007/s00109-009-0568-7. Epub 2009 Dec 4.
Abstract
Prefibrillar oligomers of the beta-amyloid peptide (A beta) are recognized as potential mediators of Alzheimer's disease (AD) pathophysiology. Deficits in synaptic function, neurotoxicity, and the progression of AD have all been linked to the oligomeric A beta assemblies rather than to A beta monomers or to amyloid plaques. However, the molecular sites of A beta oligomer action have remained largely unknown. Recently, the cellular prion protein (PrP(C)) has been shown to act as a functional receptor for A beta oligomers in brain slices. Because PrP(C) serves as the substrate for Creutzfeldt-Jakob Disease (CJD), these data suggest mechanistic similarities between the two neurodegenerative diseases. Here, we review the importance of A beta oligomers in AD, commonalities between AD and CJD, and the newly emergent role of PrP(C) as a receptor for A beta oligomers.
摘要
β淀粉样肽（Aβ）的原纤维前低聚物被认为是阿尔茨海默病（AD）病理生理学的潜在介质。突触功能障碍、神经毒性以及 AD 的进展都与低聚物 Aβ 组装有关，而不是与 Aβ单体或淀粉样斑块有关。然而，Aβ低聚物作用的分子部位在很大程度上仍然未知。最近，细胞朊病毒蛋白（PrP（C））已被证明在脑切片中作为 Aβ低聚物的功能受体发挥作用。由于 PrP（C）是克雅氏病（CJD）的底物，这些数据表明这两种神经退行性疾病之间存在机制相似性。在这里，我们回顾了 Aβ低聚物在 AD 中的重要性、AD 和 CJD 之间的共同性，以及 PrP（C）作为 Aβ低聚物受体的新出现作用。
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