Linder E, Lehto V P, Virtanen I
Acta Pathol Microbiol Scand A. 1979 Sep;87A(5):299-306. doi: 10.1111/j.1699-0463.1979.tb00056.x.
The commonly accepted markers for amyliod are a fibrillar ultrastructure and congophilia combined with green birefringence when viewed under polarized light. Although a number of cells have been implicated in amyloid formation the detailed events leading to accumulation of amyloid are still unknown. Previous studies have suggested that amyloid shares antigenic properties with cytoskeletal intermediate (10 nm) filaments and connective tissue microfibrils. In the present study we show that such filaments present in fibroblasts and lymphoid cells have an affinity for Congo red, exhibit the typical green birefringence and are ultrastructurally indistinguishable from amyloid fibrils. Intermediate filaments of cultured fibroblasts depleted of nutrient medium retained the Congo red birefringent property and typical ultrastructure despite cell damage. Our observations suggest that amyloid deposits may form locally through abnormal accumulation of bundles of cytoskeletal intermediate filaments under conditions characterized by increased cell proliferation and death.
淀粉样蛋白公认的标志物是纤维状超微结构以及嗜刚果红性,即在偏振光下观察时呈现绿色双折射。尽管许多细胞与淀粉样蛋白的形成有关,但导致淀粉样蛋白积累的详细过程仍不清楚。先前的研究表明,淀粉样蛋白与细胞骨架中间丝(10纳米)和结缔组织微原纤维具有共同的抗原特性。在本研究中,我们发现成纤维细胞和淋巴细胞中存在的此类细丝对刚果红具有亲和力,呈现典型的绿色双折射,并且在超微结构上与淀粉样纤维无法区分。耗尽营养培养基的培养成纤维细胞的中间丝尽管细胞受损,但仍保留刚果红双折射特性和典型的超微结构。我们的观察结果表明,在以细胞增殖和死亡增加为特征的条件下,淀粉样蛋白沉积物可能通过细胞骨架中间丝束的异常积累而局部形成。