DnaK/DnaJ/GrpE of Hsp70 system have differing effects on α-synuclein fibrillation involved in Parkinson's disease

被引：12

作者：

Ahmad, Atta ^{[1
]}

机构：

[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2010年 / 46卷 / 02期

关键词：

alpha-Synuclein; Chaperones; DnaK; DnaJ; GrpE; Parkinson's; Amyloid; MOLECULAR CHAPERONE; BACTERIOPHAGE-LAMBDA; ESCHERICHIA-COLI; DROSOPHILA MODEL; DNA-REPLICATION; AGGREGATION; COMPLEX; DOMAIN; NMR; TOXICITY;

D O I：

10.1016/j.ijbiomac.2009.12.017

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：

Chaperones assist in maintenance of functional proteome in vivo. However. they seem to be either ineffective or overwhelmed in the case of protein misfolding diseases like Parkinson's, Huntington's or Alzheimer's. Studies involving one or two chaperones from Hsp70 system cannot provide comprehensive information about the involvement of whole system We present for the first time, in vitro characterization of the effect of each component of Hsp70 system on alpha-synuclein (involved in Parkinson's) using SEC and ThT assay. Our results show while some components enhance the aggregation others seem to stabilize alpha-synuclein against aggregation Keeping whole Hsp70 system intact, the factor responsible for triggering aggregation seemed to be initial alpha-synuclein conformation (C) 2010 Elsevier B V All rights reserved

引用

页码：275 / 279

页数：5

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