Horiguchi Y, Fine J D, Leigh I M, Yoshiki T, Ueda M, Imamura S
Department of Dermatology, Kyoto University.
J Invest Dermatol. 1992 Jul;99(1):12-8. doi: 10.1111/1523-1747.ep12611384.
Skin lesions of lichenoid amyloidosis and macular amyloidosis were immunohistochemically investigated using five monoclonal antibodies against basement membrane zone (BMZ) components. A hemidesmosomal component did not contribute to amyloid deposits, but components of the lamina densa and anchoring fibrils were associated with amyloid deposits in the uppermost dermis. Immunoelectron microscopy revealed that these BMZ components were not only aggregated in the BMZ and dermis, but were also involved in the individual amyloid islets. The lamina densa was disrupted in the interface areas just above the amyloid deposits, where cytoplasm of the basal cells directly faced the aggregate of amyloid filaments. Aggregates of some BMZ components were continuous to the amyloid islets from the lamina densa area. These findings suggest that a lamina densa malformation is involved in amyloid production in the interface of the BMZ, and support the secretion theory rather than the fibrillar body theory of amyloidogenesis in these types of primary localized cutaneous amyloidosis.
使用五种针对基底膜带（BMZ）成分的单克隆抗体，对苔藓样淀粉样变和斑状淀粉样变的皮肤病变进行了免疫组织化学研究。一种半桥粒成分与淀粉样沉积物无关，但致密板和锚定纤维的成分与最上层真皮中的淀粉样沉积物有关。免疫电子显微镜显示，这些BMZ成分不仅聚集在BMZ和真皮中，还参与了单个淀粉样蛋白岛的形成。在淀粉样沉积物上方的界面区域，致密板被破坏，此处基底细胞的细胞质直接面对淀粉样细丝的聚集体。一些BMZ成分的聚集体从致密板区域延续到淀粉样蛋白岛。这些发现表明，致密板畸形参与了BMZ界面处的淀粉样蛋白生成，并支持了这些类型的原发性局限性皮肤淀粉样变的分泌理论而非淀粉样蛋白生成的纤维体理论。
