Schubert W, Prior R, Weidemann A, Dircksen H, Multhaup G, Masters C L, Beyreuther K
Center for Molecular Biology, University of Heidelberg, F.R.G.
Brain Res. 1991 Nov 1;563(1-2):184-94. doi: 10.1016/0006-8993(91)91532-6.
We have recently shown that the amyloid beta A4 precursor protein (APP) is synthesized in neurons and undergoes fast axonal transport to synaptic sites [Koo et al., Proc. Natl. Acad. Sci. U.S.A., 87 (1990) 1561-1565]. Using immunofluorescence, laser confocal microscopy and immunoelectron microscopy with simultaneous detection of APP and synaptophysin, we now report a preferential localization of APP at synaptic sites of human and rat brain and at neuromuscular junctions. APP is further found on vesicular elements of neuronal perikarya, dendrites and axons. The synaptic localization of APP implies (1) a role of APP in physiological synaptic activity and (2) a potential and early impairment of central synapses when synaptic APP is converted to beta A4 amyloid during the pathological evolution of Alzheimer's disease and Down's syndrome.
我们最近发现，β淀粉样蛋白A4前体蛋白（APP）在神经元中合成，并通过快速轴突运输至突触部位[Koo等人，《美国国家科学院院刊》，87（1990）1561 - 1565]。通过免疫荧光、激光共聚焦显微镜以及同时检测APP和突触素的免疫电子显微镜技术，我们现在报告APP在人和大鼠脑的突触部位以及神经肌肉接头处存在优先定位。进一步发现APP存在于神经元胞体、树突和轴突的囊泡成分上。APP的突触定位意味着（1）APP在生理性突触活动中发挥作用，以及（2）在阿尔茨海默病和唐氏综合征的病理演变过程中，当突触APP转化为βA4淀粉样蛋白时，中枢突触可能会早期受损。
