Piccardo P, Ghetti B, Dickson D W, Vinters H V, Giaccone G, Bugiani O, Tagliavini F, Young K, Dlouhy S R, Seiler C
Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, USA.
J Neuropathol Exp Neurol. 1995 Nov;54(6):790-801. doi: 10.1097/00005072-199511000-00006.
Gerstmann-Sträussler-Scheinker (GSS) disease is a familial neurological disorder pathologically characterized by accumulation of prion protein (PrP) in the form of fibrillary and non-fibrillary deposits within the cerebrum and cerebellum. We have studied two patients in whom the disease is caused by a leucine for proline amino acid substitution at residue 102 of PrP. In both patients, the neuropathologic findings are similar, consisting of spongiform changes, amyloid deposits, and gliosis. To investigate the antigenic profile of PrP deposits, we used antibodies raised against several peptides that correspond to segments of the N-terminus, repeat region, midregion, and C-terminus of PrP. By immunohistochemistry, PrP amyloid cores are best labeled by antibodies directed to epitopes spanning PrP residues 90-165. In GSS disease caused by a substitution of thymine to cytosine at PRNP codon 198 (Indiana kindred), the major amyloidogenic peptide spans residues 58-150; therefore, in these two genetic forms of GSS disease, amyloid may be composed of different peptides.
格斯特曼-施特劳斯勒-谢inker（GSS）病是一种家族性神经疾病，其病理特征是朊蛋白（PrP）以纤维状和非纤维状沉积物的形式在大脑和小脑中积聚。我们研究了两名患者，他们的疾病是由PrP第102位氨基酸的脯氨酸被亮氨酸替代引起的。在这两名患者中，神经病理学发现相似，包括海绵状改变、淀粉样沉积物和胶质细胞增生。为了研究PrP沉积物的抗原谱，我们使用了针对与PrP的N端、重复区域、中间区域和C端片段相对应的几种肽产生的抗体。通过免疫组织化学，PrP淀粉样核心最好用针对跨越PrP第90-165位残基的表位的抗体标记。在由PRNP密码子198处胸腺嘧啶替换为胞嘧啶引起的GSS病（印第安纳家族）中，主要的淀粉样生成肽跨越第58-150位残基；因此，在这两种遗传形式的GSS病中，淀粉样物质可能由不同的肽组成。
