Prion protein functions and dysfunction in prion diseases.
Prion protein functions and dysfunction in prion diseases.
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DOI：
10.2174/092986709787002673
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发表时间：
2009
影响因子：
4.1
通讯作者：
A. Sakudo;K. Ikuta
中科院分区：
文献类型：
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作者：
A. Sakudo;K. Ikuta
朊病毒病是由感染性颗粒引起的人畜共患传染病。朊病毒的主要成分可能是一种正常细胞表面蛋白的错误折叠的部分蛋白酶抗性构象异构体（PrP（Sc）），细胞朊病毒蛋白（PrP（C）），其抗氧化作用通过使用朊病毒蛋白（PrP）敲除小鼠和细胞系的研究推测。朊病毒病的主要共同特征是PrP（Sc）沉积、星形细胞增多和空泡化，但这些特征的存在和传播途径取决于朊病毒菌株和宿主物种的组合。一般来说，朊病毒首先在淋巴网状系统中复制，尽管PrP（Sc）在淋巴组织中的存在似乎取决于朊病毒暴露途径或朊病毒株类型等因素。之后，朊病毒通过神经元通路沿沿着外周神经进入大脑，在那里它们的转化导致PrP（Sc）的积累和PrP（C）的缺乏，在病因学上导致神经元的死亡，包括细胞凋亡和自噬。本文就PrP（C）和PrP（Sc）及其在朊病毒疾病发病机制中的作用作一综述。
Prion diseases are zoonotic infectious diseases caused by infectious particles, termed prions. Main component of prions is presumably a misfolded, partially protease-resistant conformer (PrP(Sc)) of a normal cell surface protein, the cellular prion protein (PrP(C)), whose anti-oxidative role is presumed by studies using prion protein (PrP)-knockout mice and cell lines. Major common features of prion diseases are PrP(Sc) deposition, astrocytosis, and vacuolation, but the presence of these features and transmission route are dependent on the combination of prion strain and host species. Generally, prions replicate first in the lymphoreticular system, although the presence of PrP(Sc) within lymphoid tissues seems to be dependent on factors such as route of prion exposure or type of prion strain. After that, prions travel to the brain via neuronal pathways along peripheral nerves, where their conversion leads to the accumulation of PrP(Sc) and a deficiency of PrP(C), contributing etiologically to the death of neurons including apoptosis and autophagy. In this review, we provide an overview of current information on PrP(C) and PrP(Sc) as well as their involvement in the pathogenesis of prion diseases.