Analyzing the aggregation of polyglutamine-expansion proteins and its modulation by molecular chaperones

被引：10

作者：

Kubota, Hiroshi ^{[1
]}

Kitamura, Akira ^{[2
]}

Nagata, Kazuhiro ^{[3
]}

机构：

[1] Akita Univ, Fac Engn & Resource Sci, Dept Life Sci, Akita 0108502, Japan

[2] Hokkaido Univ, Fac Adv Life Sci, Lab Mol Cell Dynam, Kita Ku, Sapporo, Hokkaido 0010021, Japan

[3] Kyoto Sangyo Univ, Fac Life Sci, Mol & Cellular Biol Lab, Kita Ku, Kyoto 6038555, Japan

来源：

METHODS | 2011年 / 53卷 / 03期

基金：

日本学术振兴会;

关键词：

Aggregation; Molecular chaperone; Neurodegenerative disease; Polyglutamine; Protein folding; HEAT-SHOCK PROTEINS; FLUORESCENCE CORRELATION SPECTROSCOPY; RESONANCE ENERGY-TRANSFER; INCLUSION-BODY FORMATION; NEURODEGENERATIVE DISEASES; IN-VIVO; HUNTINGTONS-DISEASE; PARKINSONS-DISEASE; HSP70; CHAPERONES; QUALITY-CONTROL;

D O I：

10.1016/j.ymeth.2010.12.035

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Polyglutamine (polyQ)-expansion proteins cause protein aggregation in the cytosol and nucleus of neuronal cells, leading to neurodegenerative diseases. For example, expansion of the polyQ tract (>40 repeats) in huntingtin (htt) proteins leads to Huntington disease, while polyQ-expanded ataxins cause several types of ataxias. PolyQ-rich inclusions are found in neuronal cells of patients, suggesting that polyQ disease is caused by protein misfolding. However, the mechanisms by which polyQ-expansion proteins exert neuronal toxicity are largely unknown. Here, we review experimental procedures to analyze the roles of molecular chaperones in preventing polyQ aggregation and toxicity as well as to measure the characteristics and dynamics of polyQ aggregation, particularly focusing on cellular models and dynamic imaging of fluorescently-labeled polyQ-expansion proteins and their modulation by chaperones. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：267 / 274

页数：8