Walsh Dominic M, Selkoe Dennis J
Laboratory for Neurodegenerative Research, The Conway Institute, University College Dublin, Belfield, Dublin, Republic of Ireland.
J Neurochem. 2007 Jun;101(5):1172-84. doi: 10.1111/j.1471-4159.2006.04426.x. Epub 2007 Feb 5.
Converging lines of evidence suggest that progressive accumulation of the amyloid beta-protein (A beta) plays a central role in the genesis of Alzheimer's disease, but it was long assumed that A beta had to be assembled into extracellular amyloid fibrils to exert its cytotoxic effects. Over the past decade, data have emerged from the use of synthetic A beta peptides, cell culture models, beta-amyloid precursor protein transgenic mice and human brain to suggest that pre-fibrillar, diffusible assemblies of A beta are also deleterious. Although the precise molecular identity of these soluble toxins remains unsettled, accumulating evidence suggests that soluble forms of A beta are indeed the proximate effectors of synapse loss and neuronal injury. Here we review recent progress in understanding the role of soluble oligomers in Alzheimer's disease.
越来越多的证据表明,β-淀粉样蛋白(Aβ)的渐进性积累在阿尔茨海默病的发生中起着核心作用,但长期以来人们一直认为,Aβ必须组装成细胞外淀粉样纤维才能发挥其细胞毒性作用。在过去十年中,通过使用合成Aβ肽、细胞培养模型、β-淀粉样前体蛋白转基因小鼠和人脑得出的数据表明,Aβ的纤维前、可扩散聚集体也具有有害作用。尽管这些可溶性毒素的确切分子身份尚未确定,但越来越多的证据表明,可溶性Aβ形式确实是突触丧失和神经元损伤的直接效应物。在这里,我们综述了在理解可溶性寡聚体在阿尔茨海默病中的作用方面的最新进展。