Ishii T, Haga S
Acta Neuropathol. 1984;63(4):296-300. doi: 10.1007/BF00687336.
The presence of components of immunoglobulins (Ishii et al. 1975) and complements (Eikelenboom and Stam 1982) in senile plaques suggests that the immunologic mechanisms are involved in the causation of pathologic processes in the brain of patients with Alzheimer's disease. Senile plaques consists of amyloid degenerated neuritis and glia, and exact localization of complements among these tissue elements will provide an important clue to the pathogenesis of the Alzheimer brain. This report deals with light- and electron-microscopic localization of complements in amyloid fibrils of senile plaques by immunoperoxidase histochemistry. The presence of C1q, C4, and C3 is confirmed light-microscopically. At the ultrastructural level, anti-complement C1q, C4, and C3 peroxidase reaction products are exclusively localized on the amyloid fibrils, but no other tissue elements, such as normal or degenerated neurites, neurofibrillary tangles, or glia. The results indicate the presence of immune complex in amyloid fibrils of senile plaques, and little association of complements in senile plaques with neurofilament protein.
老年斑中存在免疫球蛋白成分(石井等人,1975年)和补体(艾克伦博姆和斯塔姆,1982年),这表明免疫机制参与了阿尔茨海默病患者大脑病理过程的发生。老年斑由淀粉样变性神经炎和神经胶质组成,补体在这些组织成分中的精确定位将为阿尔茨海默病大脑的发病机制提供重要线索。本报告通过免疫过氧化物酶组织化学研究了补体在老年斑淀粉样纤维中的光镜和电镜定位。光镜下证实了C1q、C4和C3的存在。在超微结构水平上,抗补体C1q、C4和C3过氧化物酶反应产物仅定位于淀粉样纤维上,而不存在于其他组织成分上,如正常或变性的神经突、神经原纤维缠结或神经胶质。结果表明老年斑淀粉样纤维中存在免疫复合物,且老年斑中的补体与神经丝蛋白几乎没有关联。