PHOSPHORYLATION SITES ON TAU BY TAU PROTEIN KINASE-I, A BOVINE DERIVED KINASE GENERATING AN EPITOPE OF PAIRED HELICAL FILAMENTS

被引：146

作者：

ISHIGURO, K

OMORI, A

TAKAMATSU, M

SATO, K

ARIOKA, M

UCHIDA, T

IMAHORI, K

机构：

[1] Mitsubishi Kasei Institute of Life Sciences, Tokyo

来源：

NEUROSCIENCE LETTERS | 1992年 / 148卷 / 1-2期

关键词：

TAU PROTEIN; PROTEIN KINASE; PHOSPHORYLATION; PAIRED HELICAL FILAMENT; ALZHEIMER DISEASE; MICROTUBULE;

D O I：

10.1016/0304-3940(92)90839-Y

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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. Ser 1 99, 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) 519-5261). 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.

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页码：202 / 206

页数：5

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