Hsp70 Molecular Chaperones and Parkinson's Disease

被引：56
|
作者：
Witt, Stephan N. [1 ]
机构：
[1] Louisiana State Univ, Hlth Sci Ctr, Dept Biochem & Mol Biol, Shreveport, LA 71130 USA
来源：
BIOPOLYMERS | 2010年 / 93卷 / 03期
关键词：
alpha-synuclein; aggregate; amyloid; chaperone; heat shock protein; MUTANT ALPHA-SYNUCLEIN; HEAT-SHOCK-PROTEIN; DROSOPHILA MODEL; FIBRIL FORMATION; PLASMA-MEMBRANE; IN-VIVO; SACCHAROMYCES-CEREVISIAE; AGGREGATION; CHIP; TOXICITY;
D O I：
10.1002/bip.21302
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：
Because over expression of Hsp70 molecular chaperones suppresses the toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and various polyQ-diseases (Huntington's disease and ataxias), Hsp70 is garnering attention as a possible therapeutic agent for these various diseases. Here, I review progress in this fascinating field of molecular chaperones and neurodegeneration and describe our current understanding of the mechanisms by which Hsp70 protects cells from the PD-relared protein called alpha-synuclein (alpha-syn). (C) 2009 Wiley Periodicals, Inc. Biopolymers 93: 218-228, 2010.
引用
收藏
页码：218 / 228
页数：11
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