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首页> 外文期刊>The Journal of Clinical Investigation: The Official Journal of the American Society for Clinical Investigation >Underglycosylated prion protein modulates plaque formation in the brain COMMENT
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Underglycosylated prion protein modulates plaque formation in the brain COMMENT

机译：糖基化不足的朊病毒蛋白调节大脑中斑块的形成 评论

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摘要

The prion agent is unique in biology and is comprised of prion protein scrapie (PrPSc), a self-templating conformational variant of the host encoded prion protein cellular (PrPC). The deposition patterns of PrPSc in the CNS can vary considerably from a diffuse synaptic pattern to large plaque-like aggregates. Alterations of PrPC posttranslational processing can change PrPSc deposition patterns; however, the mechanism underlying these observations is unclear. In this issue of the JCI, Sevillano and authors determined that parenchymal PrPSc plaques of the mouse brain preferentially incorporated underglycosylated PrPC that had been liberated from the cell surface by the metalloproteinase, ADAM-10, in combination with heparan sulfate. These results provide mechanistic insight into the formation of PrPSc plaques and suggest that PrP posttranslational modifications direct pathogenicity as well as the rate of disease progression.
机译：朊病毒代理在生物学上是独一无二的，由朊病毒蛋白痒病 （PrPSc） 组成，PrPSc 是宿主编码的朊病毒蛋白细胞 （PrPC） 的自模板构象变体。PrPSc 在中枢神经系统中的沉积模式可以从弥漫性突触模式到大斑块状聚集体有很大差异。PrPC翻译后处理的改变可以改变PrPSc沉积模式;然而，这些观察结果背后的机制尚不清楚。在本期JCI中，Sevillano和作者确定小鼠大脑的实质PrPSc斑块优先掺入了由金属蛋白酶ADAM-10与硫酸乙酰肝素结合从细胞表面释放的糖基化不足的PrPC。这些结果为PrPSc斑块的形成提供了机制上的见解，并表明PrP翻译后修饰直接致病性和疾病进展速度。

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