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- Title
Prion protein participates in the regulation of classical and alternative activation of BV2 microglia.
- Authors
Shi, Fushan; Yang, Lifeng; Kouadir, Mohammed; Yang, Yang; Ding, Tianjian; Wang, Jihong; Zhou, Xiangmei; Yin, Xiaomin; Zhao, Deming
- Abstract
The cellular prion protein (PrPc) is a glycoprotein anchored by glycosylphosphatidylinositol (GPI) to the cell surface and is abundantly expressed in the central nervous system. Numerous studies have suggested a protective function for PrPc, including protection from ischemic and excitotoxic lesions and several apoptotic insults, and recent reports have shown that PrPc has a context-dependent neuroprotective function. In this study, we investigated the effect of PPNP down-regulation on various forms of microglial activation. We first examined the mRNA expression of PRNP upon exposure to IFN-y, IL-4, or IL-10 in BV2 microglia. We then analyzed the effect of si-RNA-mediated disruption of PRNP on different parameters of microglial activation in IFN-y-, IL-4-, or IL-10 stimulated microglia. The results showed that PRNP mRNA expression was invariably down-regulated in microglia upon exposure to IFN-y, IL-4, or IL-10. PRNP silencing prior to cytokines treatment reduced the responsiveness of microglia to INF-y treatment, significantly altered IL-4-induced microglial activation phenotype, and had no effect on IL-10-induced microglial activation. Together, these results support a role of PrPc in the modulation of the shift of microglia from a quiescent state to an activated phenotype and in the regulation of the microglial response during classical and alternative activation.
- Subjects
MICROGLIA; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOPROTEINS; NEUROPROTECTIVE agents; CYTOKINES; MESSENGER RNA
- Publication
Journal of Neurochemistry, 2013, Vol 124, Issue 2, p168
- ISSN
0022-3042
- Publication type
Article
- DOI
10.1111/jnc.12053