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alpha-synuclein has structural and functional similarities to small heat shock proteins

Authors
Kim, Thomas DoohunChoi, ERhim, HPaik, SRYang, CH
Issue Date
Nov-2004
Publisher
ACADEMIC PRESS
Keywords
Parkinson's disease; Small heat shock protein; α-Synuclein
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.324, no.4, pp 1352 - 1359
Pages
8
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
324
Number
4
Start Page
1352
End Page
1359
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159227
DOI
10.1016/j.bbrc.2004.09.208
ISSN
0006-291X
1090-2104
Abstract
The aggregation and fibrillization of α-synuclein, a major component of Lewy bodies, is a key event in Parkinson's disease. Although the mechanisms of fibrils formation are largely investigated, physiological function of α-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of α-synuclein is similar to α-crystalline domain of small heat shock proteins. In our experiments, α-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses. © 2004 Elsevier Inc. All rights reserved.
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