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首页> 外文期刊>The Journal of Neuroscience: The Official Journal of the Society for Neuroscience >Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain.
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Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain.

机译：在培养的神经元和大脑的突触和突触中阿尔茨海默氏症β-淀粉样蛋白的低聚。

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摘要

Multiple lines of evidence implicate beta-amyloid (Abeta) in the pathogenesis of Alzheimer's disease (AD), but the mechanisms whereby Abeta is involved remain unclear. Addition of Abeta to the extracellular space can be neurotoxic. Intraneuronal Abeta42 accumulation is also associated with neurodegeneration. We reported previously that in Tg2576 amyloid precursor protein mutant transgenic mice, brain Abeta42 localized by immunoelectron microscopy to, and accumulated with aging in, the outer membranes of multivesicular bodies, especially in neuronal processes and synaptic compartments. We now demonstrate that primary neurons from Tg2576 mice recapitulate the in vivo localization and accumulation of Abeta42 with time in culture. Furthermore, we demonstrate that Abeta42 aggregates into oligomers within endosomal vesicles and along microtubules of neuronal processes, both in Tg2576 neurons with time in culture and in Tg2576 and human AD brain. These Abeta42 oligomer accumulations are associated with pathological alterations within processes and synaptic compartments in Tg2576 mouse and human AD brains.
机译：有多种证据表明β-淀粉样蛋白（Abeta）参与了阿尔茨海默氏病（AD）的发病机理，但尚不清楚Abeta参与的机制。在细胞外空间添加Abeta可能具有神经毒性。神经内Abeta42积累也与神经变性有关。我们以前曾报道过，在Tg2576淀粉样蛋白前体蛋白突变的转基因小鼠中，脑Abeta42通过免疫电子显微镜定位到多囊体的外膜，并随着年龄的增长而积累，尤其是在神经元突触和突触区室中。我们现在证明，来自Tg2576小鼠的原代神经元随着时间的流逝而概括了Abeta42的体内定位和积累。此外，我们证明，随着时间的推移，在Tg2576神经元中以及在Tg2576和人AD脑中，Abeta42均会聚集到内体小泡内以及沿着神经元过程的微管的寡聚体中。这些Abeta42低聚物积累与Tg2576小鼠和人类AD脑的过程和突触区室中的病理变化有关。

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