摘要
热休克蛋白(HSPs)已经被发现在抗原经典呈递与交叉呈递途径、巨噬细胞与淋巴细胞的活化以及树突状细胞的活化成熟中发挥了重要的作用。但也有一些实验发现热休克蛋白的重组产物可能会被含有暴露疏水残基的病原体相关分子所污染,这种污染可能才是造成已发现的大部分体外热休克蛋白细胞因子效应的真正原因。而在体外产生的热休克蛋白抗原呈递和交叉呈递作用则有可能是由其结合或伴随的分子,而非热休克蛋白本身。
Heat shock proteins（HSPs） have been reported to play important roles in antigen presentation and cross-presentation, activation of macrophages and lymphocytes, and activation and maturation of dendritic cells. However some reports discovered that the recombinant HSP products may be contaminated with pathogen-associated molecules which contain exposed hydrophobic residues. These contaminants appear to he responsible for most reported in vitro cytokine effects of HSPs. The in vitro HSP antigen presentation and crosspresentation are a result of molecules bound to or chaperoned by HSPs but not a result of HSPs themselves.
出处
《医学综述》
2013年第7期1179-1181,共3页
Medical Recapitulate
关键词
热休克蛋白
分子伴侣
抗原呈递
细胞因子效应
Heat shock proteins
Molecular chaperones
Antigen presentation
Cytokine effects
