Kitamoto T, Doh-ura K, Muramoto T, Miyazono M, Tateishi J
Department of Neuropathology, Kyushu University, Fukuoka, Japan.
Am J Pathol. 1992 Aug;141(2):271-7.
We immunohistochemically examined tissue sections from patients with prion protein (PrP) polymorphism using hydrolytic autoclaving enhancement. Abnormal PrP accumulations could be classified into plaque formations (plaque-type) and the diffuse gray matter stainings including synaptic structures (synaptic-type). Insertional polymorphism, a point mutation in codon 102 or 117/129, and a polymorphism in codon 129 (Val129) result in plaque-type PrP accumulations. The patients with codon 102 mutation also have synaptic-type PrP accumulations. However, a point mutation in codon 200 did not show plaque-type accumulations, and only showed synaptic-type PrP accumulations. Likewise, sporadic Creutzfeldt-Jakob disease patients without any known mutations only have synaptic type accumulations. These results imply that the primary structures of PrP influence the phenotype of prion diseases, especially in abnormal PrP distributions of the central nervous system.
我们使用水解高压灭菌增强法对患有朊病毒蛋白（PrP）多态性的患者组织切片进行了免疫组织化学检查。异常PrP聚集可分为斑块形成（斑块型）和包括突触结构在内的弥漫性灰质染色（突触型）。插入多态性、密码子102或117/129的点突变以及密码子129（Val129）的多态性导致斑块型PrP聚集。密码子102突变的患者也有突触型PrP聚集。然而，密码子200的点突变未显示斑块型聚集，仅显示突触型PrP聚集。同样，没有任何已知突变的散发性克雅氏病患者仅有突触型聚集。这些结果表明，PrP的一级结构影响朊病毒疾病的表型，尤其是在中枢神经系统异常PrP分布方面。
