Galloway P G, Perry G, Gambetti P
J Neuropathol Exp Neurol. 1987 Mar;46(2):185-99. doi: 10.1097/00005072-198703000-00006.
Hirano bodies are eosinophilic, rod-shaped intraneuronal inclusions whose frequency increases with age and with Alzheimer's disease. To investigate their composition and possible relationship to the neuronal cytoskeleton, we employed immunocytochemistry and immunoelectronmicroscopy by using antisera to cytoskeletal proteins. The presence of actin, alpha-actinin, vinculin and tropomyosin was demonstrated diffusely throughout the Hirano body. The presence of these proteins supports the contention that Hirano bodies are derived from an abnormal organization of the neuronal cytoskeleton. The staining of Hirano bodies with fluorescent labelled phalloidin, a probe with a unique affinity for F-actin, indicates that the actin in Hirano bodies is in the F-state. Results of high voltage electron microscopy on 1.0 and 0.5 micron sections confirm the purely filamentous nature of Hirano bodies. These findings suggest that the mechanism of formation of Hirano bodies is different from that of the neurofibrillary tangle, another characteristic intraneuronal inclusion seen in Alzheimer patients.
Hirano小体是嗜酸性、杆状的神经元内包涵体，其出现频率随年龄增长以及阿尔茨海默病而增加。为了研究其组成以及与神经元细胞骨架的可能关系，我们通过使用针对细胞骨架蛋白的抗血清进行免疫细胞化学和免疫电子显微镜检查。肌动蛋白、α-辅肌动蛋白、纽蛋白和原肌球蛋白在整个Hirano小体内均呈弥漫性显示。这些蛋白质的存在支持了Hirano小体源自神经元细胞骨架异常组织的观点。用对F-肌动蛋白具有独特亲和力的荧光标记鬼笔环肽对Hirano小体进行染色，表明Hirano小体内的肌动蛋白处于F状态。对1.0微米和0.5微米切片进行的高电压电子显微镜检查结果证实了Hirano小体的纯丝状性质。这些发现表明，Hirano小体的形成机制与神经原纤维缠结不同，神经原纤维缠结是在阿尔茨海默病患者中看到的另一种典型的神经元内包涵体。
