Ishihara T, Takahashi M, Koga M, Yokota T, Yamashita Y, Uchino F
First Department of Pathology, Yamaguchi University School of Medicine, Ube, Japan.
Lab Invest. 1991 Feb;64(2):265-71.
Evidence for amyloid fibril formation in rough endoplasmic reticulum (RER) of plasma cells from the duodenum of a 62-year-old man with localized A lambda amyloidosis is described. The inclusions in RER of plasma cells were composed of tightly packed, regular arrays of fibrils cut in both longitudinal and cross-sections. The fibrils within the inclusions, measuring 10 nm in width, were oriented parallel to the long axis of the inclusions. By immunoelectron microscopy with an antihuman A lambda antiserum, gold particles labeled the fibrils located both in the RER of plasma cells and in the extracellular space. In addition, electron-dense material in the dilated RER was occasionally labeled. These findings suggest that at least some amyloid fibrils are unequivocally created in the RER of plasma cells.
描述了一名62岁患有局限性Aλ淀粉样变性的男性十二指肠浆细胞粗面内质网（RER）中淀粉样纤维形成的证据。浆细胞RER中的包涵体由紧密排列的规则纤维阵列组成，这些纤维在纵切面和横切面上均有显示。包涵体内的纤维宽度为10nm，与包涵体的长轴平行排列。通过使用抗人Aλ抗血清的免疫电子显微镜观察，金颗粒标记了位于浆细胞RER和细胞外空间中的纤维。此外，扩张的RER中的电子致密物质偶尔也会被标记。这些发现表明，至少一些淀粉样纤维明确是在浆细胞的RER中形成的。
