探讨小鼠肌肉组织中老化淀粉样变纤维的传播性

Transmission of mouse senile amyloid fibrils in skeletal muscle

目的探讨淀粉样变纤维AApoAII在小鼠肌肉组织中的传播性。方法本研究采用R1.P1-Apoa2c小鼠进行系统性淀粉样变诱导实验,诱导实验进行2个月后,判断从骨骼肌组织中提取淀粉样变纤维的沉积程度,并进行2次传播实验。结果从骨骼肌组织中提取淀粉样变纤维可诱发小鼠系统性淀粉样变。结论与prion蛋白质具有相似的特点,小鼠老化淀粉样变纤维可通过骨骼肌传播淀粉样变,而此结果为淀粉样变疾病的预防及发生机制的解析提供了新的理论依据。

Recently, prion-like transmission has been found in various amyloidosis. AApoAII amyloid fibrils in mouse senile amyloidosis have exhibited transmissibility. AApoAII amyloid fibrils, which were excreted from mice and contained in fe- ces or milk, cause mouse senile amyloidosis. However, transmissibility of AApoAII amyloid fibrils through other pathways has not yet been established. In this study, we injected AApoAII amyloid fibrils into R1. P1-Apoa2^c mice to induce AApoAII sys- temic amyloidosis. Two months later, AApoAII amyloid fibrils, which deposited in the skeletal muscles of amyloid-affected mice, were used to induce AApoAII systemic amyloidosis. Mouse senile amyloidosis which deposited in skeletal muscles could induce secondary transmission of AApoAII amyloidosis. The evidence of transmission through skeletal muscles in non-prion systemic amyloidosis is found in our study. This pathway of transmission provides new insight into the potential for food-borne pathogenesis and etiology of systemic amyloidosis.