Amyloid peptide attenuates the proteasome activity in neuronal cells

被引：129

作者：

Oh, S

Hong, HS

Hwang, E

Sim, HJ

Lee, W

Shin, SJ

Mook-Jung, I ^{[1
]}

机构：

[1] Seoul Natl Univ, Coll Med, Dept Biochem, Seoul 110799, South Korea

[2] Seoul Natl Univ, Coll Med, Inst Canc Res, Seoul 110799, South Korea

[3] Ajou Univ, Program Neurosci, Suwon 441749, South Korea

[4] Korea Inst Sci & Technol, Seoul 130650, South Korea

来源：

MECHANISMS OF AGEING AND DEVELOPMENT | 2005年 / 126卷 / 12期

关键词：

Tg2576; proteasome; chymotrypsin-like activity; amyloid beta-peptide;

D O I：

10.1016/j.mad.2005.07.006

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Previous studies have suggested a possible relationship between the ubiquitin-proteasome pathway and some pathological manifestations of Alzheimer's disease (AD). This study investigated the possibility that the A beta peptides interact with the ubiquitin-proteasome pathway inside neuronal cells. The ubiquitin-proteasome activity decreased with age in the brains of Tg2576 mice while the A beta(1-42) levels increased. In cultured neuronal cells, an extracellular treatment of A beta markedly decreased the proteasome activity and extracellular treated A beta peptides were found in the cytoplasmic compartment. These results suggest that the extracellular A beta peptides enter the cell and inhibit the proteasome activity, which might play a role in the pathogenesis of AD. (c) 2005 Elsevier Ireland Ltd. All rights reserved.

引用

页码：1292 / 1299

页数：8

共 45 条

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