Askanas V, Bilak M, Engel W K, Alvarez R B, Tomé F, Leclerc A
Department of Neurology, University of Southern California School of Medicine, Los Angeles 90017.
Neuroreport. 1993 Oct 25;5(1):25-8. doi: 10.1097/00001756-199310000-00006.
In muscle biopsies of 8 sporadic inclusion-body myositis (S-IBM) and 4 hereditary inclusion-body myopathy (H-IBM) patients, vacuolated muscle fibers contained within their vacuoles strongly immunoreactive inclusions with 2 polyclonal and 1 monoclonal antibodies against prion protein (PrP). By light-microscopy, PrP deposits co-localized with beta-amyloid protein (A beta) and ubiquitin (Ub). By immuno-electronmicroscopy, both PrP and A beta were present on amorphous material and on 6-10 nm amyloid-like fibrils; and PrP and Ub co-localized on cytoplasmic twisted tubulofilaments (TTFs) and on amorphous material. Our study provides the first demonstration of abnormally accumulated PrP in pathological tissue other than brain, and it suggests that PrP may play a role in the pathogenesis of IBM.
在8例散发性包涵体肌炎（S-IBM）患者和4例遗传性包涵体肌病（H-IBM）患者的肌肉活检中，空泡化肌纤维的空泡内含有对2种多克隆抗体和1种抗朊病毒蛋白（PrP）单克隆抗体呈强免疫反应性的包涵体。通过光学显微镜观察，PrP沉积物与β-淀粉样蛋白（Aβ）和泛素（Ub）共定位。通过免疫电子显微镜观察，PrP和Aβ均存在于无定形物质和6-10纳米淀粉样纤维上；并且PrP和Ub在细胞质扭曲微管丝（TTF）和无定形物质上共定位。我们的研究首次证明了PrP在脑以外的病理组织中异常积聚，并且提示PrP可能在IBM的发病机制中起作用。
