Uchino F, Takahashi M, Yokota T, Ishihara T
Appl Pathol. 1985;3(1-2):78-87.
Using an electron-microscopic, enzyme-labeled antibody method and cytochemical method in addition to conventional electron microscopy, we investigated the mechanism by which serum amyloid A protein (SAA) and amyloid fibrils were formed in the liver of mice with experimental amyloidosis. After induction, SAA was found initially on the rough endoplasmic reticulum of hepatocytes followed sequentially by the Golgi apparatus and secretory granules of hepatocytes. Shortly afterwards, SAA was observed in Disse's spaces, hepatic sinusoids and Kupffer cells. Amyloid fibrils appeared to accumulate predominantly extracellularly in the cytoplasmic invaginations of Kupffer cells or hepatocytes. However, they seemed to be partially formed by lysosomal enzymes in the cytoplasm of Kupffer cells.
除了传统电子显微镜检查外,我们还使用电子显微镜、酶标记抗体法和细胞化学方法,研究了实验性淀粉样变性小鼠肝脏中血清淀粉样蛋白A(SAA)和淀粉样纤维形成的机制。诱导后,最初在肝细胞的粗面内质网上发现SAA,随后依次出现在肝细胞的高尔基体和分泌颗粒上。不久之后,在狄氏间隙、肝血窦和库普弗细胞中观察到SAA。淀粉样纤维似乎主要在细胞外积聚在库普弗细胞或肝细胞的细胞质内陷中。然而,它们似乎部分是由库普弗细胞细胞质中的溶酶体酶形成的。