牛源激酶——微管相关蛋白激酶I使微管相关蛋白磷酸化的位点，该激酶可产生成对螺旋丝的一个表位。
Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments.
作者信息
Ishiguro K, Omori A, Takamatsu M, Sato K, Arioka M, Uchida T, Imahori K
机构信息
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
出版信息
Neurosci Lett. 1992 Dec 14;148(1-2):202-6. doi: 10.1016/0304-3940(92)90839-y.
Tau protein kinase I (TPKI) isolated from bovine brain has been determined to phosphorylate tau at four distinct sites by detecting modified Ser and Thr residues with protein sequencer. Ser199, Thr231, Ser396 and Ser413 were all found to have been phosphorylated by TPKI (numbering of amino acids was done in relation to the longest human tau [Neuron, 3 (1989) 519-526]). These phosphorylations generate an epitope of PHF (paired helical filaments) and eliminate the recognition of tau by the monoclonal antibody, tau-1. These results suggested that TPKI might be responsible for at least some of the phosphorylation of tau to induce PHF formation.
从牛脑中分离出的tau蛋白激酶I（TPKI），通过用蛋白质测序仪检测修饰的丝氨酸（Ser）和苏氨酸（Thr）残基，已确定其能在四个不同位点使tau蛋白磷酸化。已发现Ser199、Thr231、Ser396和Ser413均被TPKI磷酸化（氨基酸编号是相对于最长的人类tau蛋白进行的[《神经元》，3（1989年）519 - 526]）。这些磷酸化作用产生了PHF（双螺旋丝）的一个表位，并消除了单克隆抗体tau - 1对tau蛋白的识别。这些结果表明，TPKI可能至少对部分tau蛋白的磷酸化负责，从而诱导PHF的形成。
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