Migheli A, Attanasio A, Vigliani M C, Schiffer D
Second Neurologic Clinic, University of Turin, Italy.
Neurosci Lett. 1991 Jan 2;121(1-2):55-8. doi: 10.1016/0304-3940(91)90648-d.
Dystrophic neurites have been previously observed around prionic protein-derived amyloid plaques of Gerstmann-Sträussler-Scheinker (GSS) disease. Ubiquitin (Ubq) immunohistochemistry reveals the presence of dot-like stainings around many of these plaques. In order to determine the nature of ubiquitinated deposits, we performed an immunogold electron microscope study on autoptic samples from the cerebellum of a GSS patient. Both pre- and post-embedding staining methods showed Ubq-positive dense bodies and filamentous structures, belonging to dystrophic neurites. They are analogous to ubiquitinated neuritic processes described around cerebellar amyloid plaques of Alzheimer's disease (AD). These results suggest that amyloid deposition is responsible for the degeneration of adjacent axon terminals in both AD and GSS.
以往在格斯特曼-施特劳斯勒-谢克尔综合征（GSS）患者的朊蛋白衍生淀粉样斑块周围观察到营养不良性神经突。泛素（Ubq）免疫组织化学显示，许多此类斑块周围存在点状染色。为了确定泛素化沉积物的性质，我们对一名GSS患者小脑的尸检样本进行了免疫金电子显微镜研究。包埋前和包埋后的染色方法均显示Ubq阳性致密体和丝状结构，属于营养不良性神经突。它们类似于在阿尔茨海默病（AD）小脑淀粉样斑块周围描述的泛素化神经突过程。这些结果表明，淀粉样沉积是导致AD和GSS中相邻轴突终末变性的原因。
