Prion protein oligomer and its neurotoxicity

Huang P, Lian F, Wen Y, Guo C, Lin D.

Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):442-51. doi: 10.1093/abbs/gmt037

School of Life Science and Technology, China Pharmaceutical University, Nanjing 21009, China

The prion diseases, also known as transmissible spongiform encephalopathies, are fatal neurodegenerative disorders. According to the protein only hypothesis, the key molecular event in the pathogenesis of prion disease is the conformational conversion of the host-derived cellular prionprotein (PrPC) into a misfolded form (scrapie PrP, PrPSc). Increasing evidence has shown that the most infectious factor is the smaller subfibrillar oligomers formed by prion proteins. Both the prionoligomer and PrPSc are rich in -sheet structure and resistant to the proteolysis of proteinase K. The prionoligomer is soluble in physiologic environments whereas PrPSc is insoluble. Various prion oligomers are formed in different conditions. Prion oligomers exhibited more neurotoxicity both in vitro and in vivo than the fibrillar forms of PrPSc, implying that prion oligomers could be potential drug targets for attacking prion diseases. In this article, we describe recent experimental evidence regarding prion oligomers, with a special focus on prionoligomer formation and itsneurotoxicity.

图例: PrPSc结构模型

全文: http://abbs.oxfordjournals.org/content/45/6/442.full

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