SHIFT FROM FETAL-TYPE TO ALZHEIMER-TYPE PHOSPHORYLATED TAU-PROTEINS IN SKNSH-SY 5Y CELLS TREATED WITH OKADAIC ACID

被引：36

作者：

DUPONT-WALLOIS, L

SAUTIERE, PE

COCQUERELLE, C

BAILLEUL, B

DELACOURTE, A

CAILLET-BOUDIN, ML

机构：

[1] INSERM, U156, NEUROSCI LAB, F-59045 LILLE, FRANCE

[2] INSERM, U124, F-59045 LILLE, FRANCE

来源：

FEBS LETTERS | 1995年 / 357卷 / 02期

关键词：

TAU PROTEIN; OKADAIC ACID; PHOSPHORYLATION; ALZHEIMERS DISEASE; SKNSH-SY CELL;

D O I：

10.1016/0014-5793(94)01361-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tau proteins are abnormally phosphorylated in Alzheimer's disease. Pathological Tau proteins named PHF-Tau 55, PHF-Tau 64, and PHF-Tau 69, are the main constituents of the paired helical filaments (PHF). When treating SKNSH-SY 5Y cells with okadaic acid (OA), Tau 55 protein was clearly induced whereas Tau 64 protein was only faintly induced. Here, me show that the absence of Tau 69 could be explained by the fact that adult isoforms containing N-terminal inserts are not detected. Phosphorylation is similar for untreated cellular Tau proteins and fetal Tau proteins, while OA cell treatment transformed fetal-type into Alzheimer-type phosphorylated proteins.

引用

页码：197 / 201

页数：5

共 27 条

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