期刊
CURRENT MEDICINAL CHEMISTRY
卷 16, 期 3, 页码 380-389出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986709787002673
关键词
Anti-oxidation; apoptosis; autophagy; oxidative stress; prion disease; prion protein; reactive oxygen species; transmissible spongiform encephalopathy
资金
- Ministry of Education, Science, Culture and Technology of Japan
- Ministry of Agriculture, Forestry and Fisheries of Japan
- Ministry of Health, Labour and Welfare of Japan
Prion diseases are zoonotic infectious diseases caused by infectious particles, termed prions. Main component of prions is presumably a misfolded, partially protease-resistant conformer (PrPSc) of a normal cell surface protein, the cellular prion protein (PrPC), whose anti- oxidative role is presumed by studies using prion protein (PrP)-knockout mice and cell lines. Major common features of prion diseases are PrPSc 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据