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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 found to play an important role in the classical antigen presentation and cross-presentation pathways, the activation of macrophages and lymphocytes, and the activation and maturation of dendritic cells. However, some experiments have found that recombinant heat shock proteins may be contaminated by pathogen-associated molecules that contain hydrophobic residues and that this contamination may be the real cause of most of the cytokine effects of the heat shock proteins found in vitro. In vitro production of heat shock protein antigen presentation and cross-presentation may be its binding or accompanying molecules, rather than the heat shock protein itself.