Askanas V, McFerrin J, Alvarez R B, Baqué S, Engel W K
Department of Neurology, University of Southern California, School of Medicine, Good Samaritan Hospital, Los Angeles 90017-1912, USA.
Neuroreport. 1997 Jul 7;8(9-10):2155-8. doi: 10.1097/00001756-199707070-00012.
Direct transfer of the beta-amyloid precursor protein (beta APP) gene into cultured normal human muscle, using recombinant adenovirus vector, was sufficient to induce several of the typical light microscopic, electron microscopic (EM), and EM-immunochemical aspects of the inclusion-body myositis (IBM) phenotype, including congophilia, clusters of amyloid-beta-positive 6-10 nm filaments, and 15-21 nm tubulofilamentous inclusions in the nuclei. Our results suggest that excessive production of intracellular beta APP may play an important role in the pathogenic cascade leading to the IBM phenotype.
使用重组腺病毒载体将β-淀粉样前体蛋白（β-APP）基因直接导入培养的正常人类肌肉中，足以诱导包涵体肌炎（IBM）表型的一些典型光学显微镜、电子显微镜（EM）和EM免疫化学特征，包括刚果红染色阳性、淀粉样β蛋白阳性的6-10纳米细丝簇，以及细胞核中15-21纳米的微管丝状包涵体。我们的结果表明，细胞内β-APP的过量产生可能在导致IBM表型的致病级联反应中起重要作用。
