Immunocytochemical localization of amyloid precursor protein in rat brain.
Immunocytochemical localization of amyloid precursor protein in rat brain.
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大鼠脑中淀粉样蛋白前体蛋白的免疫细胞化学定位。
DOI：
10.1002/cne.903480207
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Greengard,P
中科院分区：
文献类型：
--
作者：
Ouimet,CC;Baerwald,KD;Gandy,SE;Greengard,P
应用细胞质结构域特异性抗体研究了淀粉样蛋白前体蛋白（APP）在大鼠脑中的定位。光镜免疫细胞化学表明，APP存在于大多数神经元、一些少突胶质细胞和直径小于10 μm的胶质细胞群中。各神经元的免疫反应性有明显差异，其中较大的神经元免疫反应性最强。缺乏细胞质的神经元，如嗅球、齿状回和小脑中的颗粒细胞，免疫反应较弱。神经pil免疫反应性也有差异；这种染色在尾核、外侧隔、内侧束、丘脑背侧网状核和腹后核外侧部分最强。神经pil免疫染色在皮层第四层和颗粒细胞区最弱。APP似乎存在于绝大多数神经元的事实表明，这种蛋白质在所有神经元中起着共同的作用。在不同类型的神经元中，APP的稳态量存在很大差异，这表明APP可能在某些类型的神经元的功能中起特定的作用。©1994 Wiley‐Liss, Inc。
The localization ofamyloid precursor protein (APP) in rat brain was studied with a cytoplasmic domain‐specific antibody. Light microscopic immunocytochemistry demonstrated that APP is present in most neurons, in some oligodendrocytes, and in a population of cells with diameters less than 10 μm that may be glial. Marked differences in immunoreactivity among neurons were observed, and the strongest immunoreactivity was contained in larger neurons. Neurons with scant cytoplasm, such as granule cells in the olfactory bulb, dentate gyrus, and cerebellum, were weakly immunoreactive. Differences in neuropil immunoreactivity were also observed; this type of staining was strongest in the caudatoputamen, lateral septum, medial habenula, nucleus reticularis of the dorsal thalamus, and the lateral portion of the ventroposterior nucleus. Neuropil immunostaining was weakest in layer IV of cortex and in areas containing granule cells. The fact that APP seems to be present in the vast majority of neurons suggests that this protein plays a role common to all neurons. The fact that there is a great difference in the steady‐state amount of APP among different types of neurons suggests that APP may play a specific role in the function of certain classes of neurons. © 1994 Wiley‐Liss, Inc.