Rösner H, Rebhan M, Vacun G, Vanmechelen E
Institute of Zoology, University of Hohenheim, Stuttgart, Germany.
Neuroreport. 1994 May 9;5(9):1164-6. doi: 10.1097/00001756-199405000-00036.
Immunoblots from embryonic chicken optic lobes (midbrain) and spinal cord were found to contain different proteins with a molecular weight between 45 and 70 kDa that are recognized by monoclonal antibodies (mAbs) directed at human tau proteins. Each appears as a doublet on SDS-PAGE. The upper, slower migrating bands were recognized by AT8, a monoclonal antibody that requires a phosphorylated Ser-202, an epitope specific for abnormally phosphorylated tau of paired helical filaments (PHF-tau) in Alzheimer brains. The corresponding faster migrating bands were stained by the mAbs BT2 and tau-1, both requiring an epitope containing a non-phosphorylated Ser-202. Phosphatase treatment abolished binding of AT8 and induced an additional binding of tau-1 (and BT2) to the upper bands. Thus, the data suggest that in embryonic chicken central nervous system Ser-202 occurs in a phosphorylated and in a non-phosphorylated state in several distinct tau isoforms.
研究发现,来自胚胎鸡视叶(中脑)和脊髓的免疫印迹含有分子量在45至70 kDa之间的不同蛋白质,这些蛋白质可被针对人类tau蛋白的单克隆抗体(mAb)识别。在SDS-PAGE上,每种蛋白均呈现为双峰。迁移较慢的上带可被AT8识别,AT8是一种单克隆抗体,需要磷酸化的Ser-202,这是阿尔茨海默病大脑中配对螺旋丝(PHF-tau)异常磷酸化tau的特异性表位。相应迁移较快的条带可被单克隆抗体BT2和tau-1染色,这两种抗体都需要一个包含非磷酸化Ser-202的表位。磷酸酶处理消除了AT8的结合,并诱导tau-1(和BT2)与上带的额外结合。因此,数据表明,在胚胎鸡中枢神经系统中,Ser-202在几种不同的tau异构体中以磷酸化和非磷酸化状态存在。