Journal
NEUROSCIENCE
Volume 170, Issue 4, Pages 1028-1034Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuroscience.2010.08.014
Keywords
astrocyte; central nervous system
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Funding
- Ministry of Education, Science, Sports, and Culture, Japan [19209050, 20591798]
- Grants-in-Aid for Scientific Research [19209050, 20591798] Funding Source: KAKEN
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Heat shock protein 27 (HSP27), a low-molecular-weight HSP, is recognized as a molecular chaperone. In response to various stimuli, HSP27 expression is induced in the CNS. However, the exact roles of HSP27 in the CNS have not yet been clarified. It has been reported that interleukin (IL)-1 beta stimulates IL-6 synthesis in C6 glioma cells. In the present study, we investigated the role of HSP27 in the IL-1 beta-induced IL-6 synthesis in C6 cells. IL-1 beta alone did not affect the levels of HSP27. The IL-1 beta-induced IL-6 release in HSP27-downregulated C6 cells were enhanced compared with those in control siRNA-transfected cells. On the other hand, the IL-1 beta-induced IL-6 release was significantly enhanced in C6 cells transfected with HSP27 than those in control cells in time- and dose-dependent manner. The IL-1 beta-induced IL-6 release and the mRNA expression were markedly suppressed in C6 cells transfected with phosphorylated HSP27, while those in the cells transfected with unphosphorylated HSP27 were enhanced. In conclusion, these results strongly suggest that phosphorylated status of HSP27 has a switching role in the IL-1 beta-induced IL-6 synthesis in C6 glioma cells. (C) 2010 IBRO. Published by Elsevier Ltd. All rights reserved.
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