Chloroquine myopathy suggests that tau is degraded in lysosomes: implication for the formation of paired helical filaments in Alzheimer's disease

被引：37

作者：

Oyama, F

Murakami, N

Ihara, Y

机构：

[1] Univ Tokyo, Fac Med, Dept Neuropathol, Bunkyo Ku, Tokyo 1130033, Japan

[2] Univ Otago, Dept Anat & Struct Biol, Dunedin, New Zealand

[3] Natl Ctr Neurol & Psychiat, Dept Ultrastruct Res, Kodaira 1870031, Tokyo, Japan

[4] Japan Sci & Technol Corp, Core Res Evolut Sci & Technol, Tokyo, Japan

来源：

NEUROSCIENCE RESEARCH | 1998年 / 31卷 / 01期

基金：

日本学术振兴会;

关键词：

Alzheimer's disease; chloroquine myopathy; lysosome; rimmed vacuole; tau; paired helical filaments;

D O I：

10.1016/S0168-0102(98)00020-0

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

We have found that amorphous tau deposits in chloroquine myopathy (CM), a vacuolar myopathy induced by the administration of chloroquine, a well-known lysosomotropic agent. The dynamics of tau in CM and immunocytochemistry strongly suggest that the accumulation of tau is due to defective tau degradation in the lysosomal compartment in the muscle. This observation may offer a new view on the formation of paired helical filaments in Alzheimer's disease: this selective protein degradation pathway may be defective and result in intracellular accumulation of tau, thereby forming the unusual filaments. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：1 / 8

页数：8

共 67 条

[1] An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation [J].