朊病毒蛋白生物合成及其在神经退行性变中的新作用。
Prion protein biosynthesis and its emerging role in neurodegeneration.
作者信息
Chakrabarti Oishee, Ashok Aarthi, Hegde Ramanujan S
机构信息
Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
出版信息
Trends Biochem Sci. 2009 Jun;34(6):287-95. doi: 10.1016/j.tibs.2009.03.001. Epub 2009 May 15.
Various fatal neurodegenerative disorders are caused by altered metabolism of the prion protein (PrP). These diseases are typically transmissible by an unusual 'protein-only' mechanism in which a misfolded isomer, PrP(Sc), confers its aberrant conformation onto normal cellular PrP. An impressive range of studies has investigated nearly every aspect of this fascinating event; yet, our understanding of how PrP(Sc) accumulation might lead to cellular dysfunction and neurodegeneration is trifling. Recent advances in our understanding of normal PrP biosynthesis and degradation might have unexpectedly shed new light on this complex problem. Indeed, our current understanding of normal PrP cell biology, coupled with a growing appreciation of its complex metabolism, is providing new hypotheses for PrP-mediated neurodegeneration.
多种致命的神经退行性疾病是由朊病毒蛋白（PrP）代谢改变引起的。这些疾病通常通过一种不同寻常的“仅蛋白质”机制传播，即错误折叠的异构体PrP(Sc)将其异常构象赋予正常细胞PrP。一系列令人印象深刻的研究几乎对这一引人入胜的事件的方方面面都进行了调查；然而，我们对PrP(Sc)积累如何导致细胞功能障碍和神经退行性变的了解却微乎其微。我们对正常PrP生物合成和降解的理解方面的最新进展可能意外地为这个复杂问题带来了新的启示。事实上，我们目前对正常PrP细胞生物学的理解，再加上对其复杂代谢的日益认识，正在为PrP介导的神经退行性变提供新的假说。
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