期刊
JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY
卷 -, 期 -, 页码 -出版社
HINDAWI PUBLISHING CORPORATION
DOI: 10.1155/2012/252049
关键词
-
资金
- KIT
- JST
- JSPS
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [21580067, 22241052, 23013015] Funding Source: KAKEN
Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of alpha-synuclein, underlie neurodegenerative diseases including Alzheimer's, Parkinson, Huntington, Creutzfeldt diseases. Small heatshock proteins, such as alpha B-crystallin, act as chaperones to prevent protein aggregation and play a key role in the prevention of such protein disorganisation diseases. In this study, we have explored the potential for chaperone activity of alpha B-crystallin to suppress the formation of protein aggregates. We tested the ability of aB-crystallin to suppress the aggregation of a polyQ protein and alpha-synuclein in Drosophila. We found that alpha B-crystallin suppresses both the compound eye degeneration induced by polyQ and the alpha-synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined that alpha B-crystallin inhibits the aggregation of polyQ in vivo. These data provide a clue for the development of therapeutics for neurodegenerative diseases.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据