Pockley Alan Graham, Muthana Munitta, Calderwood Stuart K
School of Medicine and Biomedical Sciences, University of Sheffield, Beech Hill Road, Sheffield S10 2RX, UK.
Trends Biochem Sci. 2008 Feb;33(2):71-9. doi: 10.1016/j.tibs.2007.10.005. Epub 2008 Jan 7.
Stress proteins (SPs) from the heat shock and glucose-regulated protein families are abundant intracellular molecules that have powerful extracellular roles as immune modulators. Mammalian immune cells encounter both identical (self) SPs and non-identical SPs derived from invading pathogens. Although such extracellular SPs can function as powerful immunological adjuvants, SPs, including Hsp60 and Hsp70, can also attenuate inflammatory disease via apparent effects on immunoregulatory T cell populations. It therefore seems that the immunostimulatory and immunosuppressive potential of extracellular SPs depends on the context in which they are encountered by the cellular immune-response network. Conclusions regarding the immunobiology of these powerful immunomodulatory molecules must therefore take into account their dichotomous properties and their physiological role and importance must be interpreted in the context of the complex in vivo microenvironments in which these proteins exist.
热休克蛋白家族和葡萄糖调节蛋白家族中的应激蛋白（SPs）是细胞内丰富的分子，作为免疫调节剂在细胞外发挥着重要作用。哺乳动物免疫细胞会接触到来自入侵病原体的相同（自身）SPs和不同的SPs。尽管这种细胞外SPs可作为强大的免疫佐剂发挥作用，但包括Hsp60和Hsp70在内的SPs也可通过对免疫调节性T细胞群体的明显作用来减轻炎症性疾病。因此，细胞外SPs的免疫刺激和免疫抑制潜力似乎取决于细胞免疫反应网络遇到它们的背景。因此，关于这些强大免疫调节分子免疫生物学的结论必须考虑到它们的双重特性，并且它们的生理作用和重要性必须在这些蛋白质存在的复杂体内微环境中进行解释。
