Chaperone-like activities of alpha-synuclein:alpha-synuclein assists enzyme activities of esterasesChaperone-like activities of α-synuclein: α-Synuclein assists enzyme activities of esterases
- Other Titles
- Chaperone-like activities of α-synuclein: α-Synuclein assists enzyme activities of esterases
- Authors
- 안미선; 김승범; 강미라; 유연우; 김두헌
- Issue Date
- Aug-2006
- Publisher
- Elsevier
- Citation
- Biochemical and Biophysical Research Communications, v.346, no.4, pp 1142 - 1149
- Pages
- 8
- Journal Title
- Biochemical and Biophysical Research Communications
- Volume
- 346
- Number
- 4
- Start Page
- 1142
- End Page
- 1149
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159248
- DOI
- 10.1016/j.bbrc.2006.05.213
- ISSN
- 0006-291X
1090-2104
- Abstract
- α-Synuclein, a major constituent of Lewy bodies (LBs), has been implicated to play a critical role in the pathogenesis of Parkinson’s disease (PD), although the physiological function of α-synuclein has not yet been known. Here we have shown that α-synuclein, which has no well-defined secondary or tertiary structure, can protect the enzyme activity of microbial esterases against stress conditions such as heat, pH, and organic solvents. In particular, the flexibility of α-synuclein and its C-terminal region seems to be important for complex formation, but the structural integrity of the C-terminal region may not be required for stabilization of enzyme activity. In addition, atomic force microscopy (AFM) and in vivo enzyme assays showed highly specific interactions of esterases with α-synuclein. Our results indicate that α-synuclein not only protects the enzyme activity of microbial esterases in vitro, but also can stabilize the active conformation of microbial esterases in vivo.
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