Hintner H, Stössl H, Höpfl R, Grubauer G, Fritsch P
Universitätsklinik für Dermatologie und Venerologie Innsbruck.
Hautarzt. 1988 Jul;39(7):419-25.
Electron-microscopic, histochemical and immunological studies have shown that the deposits of primary and secondary localized cutaneous amyloid (amyloid K) consist mainly of keratin filament material. The amyloid P component is the second most significant constituent. Pathogenetically, defective keratinocyte apoptosis is the most likely mechanism of generation for amyloid K. Apoptosis is a distinct mode of cell death according to which individual basal keratinocytes disintegrate in physiological and pathological conditions to form membrane-bound "apoptotic" bodies consisting mainly of keratin filament aggregates. These lose their protective membrane and drop into the upper dermis, where they present as keratin (Civatte, cytoid) bodies, which are regularly coated with immunoglobulins. Overproduction of keratin bodies and/or a defect in their degradation by enzymatic digestion or phagocytosis by macrophages and fibroblasts, followed by conversion into amyloid fibrils, may be responsible for the generation of deposits of amyloid K.
电子显微镜、组织化学和免疫学研究表明，原发性和继发性局限性皮肤淀粉样变（淀粉样蛋白K）的沉积物主要由角蛋白丝物质组成。淀粉样蛋白P成分是第二重要的组成部分。从发病机制来看，角质形成细胞凋亡缺陷是淀粉样蛋白K最可能的产生机制。凋亡是一种独特的细胞死亡方式，根据这种方式，单个基底角质形成细胞在生理和病理条件下解体，形成主要由角蛋白丝聚集体组成的膜结合“凋亡”小体。这些小体失去其保护膜并掉入真皮上层，在那里它们呈现为角蛋白（西瓦特，细胞样）小体，这些小体通常被免疫球蛋白覆盖。角质形成小体过度产生和/或其被酶消化或被巨噬细胞和成纤维细胞吞噬降解存在缺陷，随后转化为淀粉样纤维，可能是淀粉样蛋白K沉积物产生的原因。
