Dorj Gantsetseg, Okada Hiroyuki, Miyazawa Kohtaro, Masujin Kentaro, Kimura Kumiko, Mohri Shirou, Yokoyama Takashi
Prion Disease Research Center, National Institute of Animal Health, Tsukuba 305-0856, Japan.
J Vet Med Sci. 2012 Sep;74(9):1207-10. doi: 10.1292/jvms.12-0037. Epub 2012 May 15.
An abnormal isoform of prion protein (PrP(Sc)) was extracted from formalin-fixed paraffin-embedded (FFPE) tissues from sheep and analyzed by western blotting. PrP(Sc) immunoreactivity against anti-PrP monoclonal antibody T2, which recognizes discontinuous PrP sequences, differed amongst individual scrapie sheep cases. This may reflect structural differences in PrP(Sc) that have been formalin-fixed prior to their extraction. This study indicates that western blotting by using FFPE tissues is useful for the retrospective analysis of transmissible spongiform encephalopathies in which only formalin-fixed samples are available and in conducting transmissible spongiform encephalopathies surveillance where freezing system is insufficient.
从绵羊的福尔马林固定石蜡包埋(FFPE)组织中提取了异常形式的朊病毒蛋白(PrP(Sc)),并通过蛋白质印迹法进行分析。抗PrP单克隆抗体T2可识别不连续的PrP序列,不同羊瘙痒病病例的PrP(Sc)对该抗体的免疫反应性有所不同。这可能反映了在提取前已用福尔马林固定的PrP(Sc)的结构差异。本研究表明,对于仅能获得福尔马林固定样本的可传播性海绵状脑病的回顾性分析,以及在冷冻系统不足的情况下进行可传播性海绵状脑病监测,使用FFPE组织进行蛋白质印迹法是有用的。