中文摘要：

Prion 疾病是人和动物的一组能递送的致命的 neurodegenerative 混乱，包括牛的海绵状的 encephalopathy， scrapie，和 CreutzfeldtJakob 疾病。Microglia，中央神经系统的居民巨噬细胞，对病理学的织物改变精致地敏感，改变他们的形态学和显型采用一个所谓的激活的状态并且执行免疫学的响应 pathophysiological 大脑侮辱工作。尽管最近的调查结果提供了珍贵卓见进角色 microglia，在在 prion 观察的 proinflammatory 事件玩，为这些回答的开始负责的细胞内部的发信号分子尚待被阐明。看起来 microglial 激活包含 PrP106126 绑定和象 CD36 和 integrins 那样的房间表面免疫者和粘附分子的激活与象 Fyn 那样的 Src 家庭酷氨酸 kinases 的随后的招募， Lyn，和 Syk kinases。在现在的学习，我们证明 CD36 涉及导致 PrP106126 的 microglial 激活并且 PP2 和 piceatannol (照片) 能废除毒害神经的 prion 在 microglia 的导致肽的可诱导的氮的氧化物 synthase 激活。这些调查结果作为 Src 家庭 kinase Fyn 和涉及毒害神经的 prion peptidesmicroglia 相互作用的酷氨酸 kinase Syk 禁止者揭开 PP2 和照片的一个以前未被认出的角色，因此提供新卓见进由毒害神经的 prion 肽位于 microglia 的激活下面的机制。

英文摘要：

Prion diseases are a group of transmissible fatal neurodegen- erative disorders of humans and animals, including bovine spongiform encephalopathy, scrapie, and Creutzfeldt- Jakob disease. Microglia, the resident macrophages of the central nervous system, are exquisitely sensitive to patho- logical tissue alterations, altering their morphology and phenotype to adopt a so-called activated state and perform immunological functions in response to pathophysiological brain insults. Although recent findings have provided valu- able insights into the role microglia play in the proinflamma- tory events observed in prion, the intracellular signaling molecules responsible for the initiation of these responses remain to be elucidated. It seems that microglial activation involve PrP106-126 binding and the activation of cell surface immune and adhesion molecules such as CD36 and integ- rins, with the subsequent recruitment of Src family tyrosine kinases such as Fyn, Lyn, and Syk kinases. In the present study, we show that CD36 is involved in PrP106-126-induced microglial activation and that PP2 and piceatannol （Pic） can abrogate neurotoxic prion peptides-induced inducible nitric oxide synthase activation in microglia. These findings unveil a previously unrecognized role of PP2 and Pic as Src family kinase Fyn and the tyrosine kinase Syk inhibitor involved in neurotoxic prion peptides-microglia interactions, thus pro- viding new insights into mechanisms underlying the activa- tion of microgiia by neurotoxic prion peptides.