Störkel S, Schneider H M, Müntefering H, Kashiwagi S
Lab Invest. 1983 Jan;48(1):108-11.
Human and experimental amyloidosis can occur either as a generalized widespread deposit of various proteins or a localized deposit. We looked for local amyloidosis caused iatrogenically under clinical and experimental conditions. Subcutaneous tissue from one diabetic patient and six Wistar rats, which had received a continuous local infusion of 1.2 iu of insulin daily for 6 weeks, was examined histologically. In all cases the development of granulation tissue around the tip of the catheter was observed. In addition, inhomogenous extracellular deposits showing green birefringence under polarized light when stained Congo red were seen. Immunohistologically, they displayed binding of anti-insulin antibody. Electron microscopy demonstrated a typical spear-like fibrillar structure with a fibril diameter of 60 to 80 A. These findings confirmed that the deposited substance was amyloid. Iatrogenically administered protein produced in vivo amyloidosis at the site of its entry. Insulin can lead to the formation of amyloid fibrils not only in vitro but also in vivo.
人类和实验性淀粉样变性可表现为各种蛋白质的全身性广泛沉积或局部沉积。我们在临床和实验条件下寻找医源性引起的局部淀粉样变性。对一名糖尿病患者和六只Wistar大鼠的皮下组织进行了组织学检查,这些大鼠每天持续局部输注1.2国际单位胰岛素,持续6周。在所有病例中,均观察到导管尖端周围肉芽组织的形成。此外,当用刚果红染色时,在偏振光下可见不均匀的细胞外沉积物呈现绿色双折射。免疫组织化学显示,它们与抗胰岛素抗体结合。电子显微镜显示典型的矛状纤维结构,纤维直径为60至80埃。这些发现证实沉积物质为淀粉样蛋白。医源性给药的蛋白质在其进入部位产生体内淀粉样变性。胰岛素不仅能在体外而且能在体内导致淀粉样纤维的形成。