Robert Jacques
Department of Microbiology and Immunology, University of Rochester Medical Center, Box 672 601, Elmwood Avenue, Rochester, NY 14642, USA.
Dev Comp Immunol. 2003 Jun-Jul;27(6-7):449-64. doi: 10.1016/s0145-305x(02)00160-x.
Heat shock proteins (hsps) are among the most abundant intracellular proteins. Their synthesis is rapidly up-regulated by various 'stressors' including temperature, glucose deprivation, infection and cancer. Certain hsps are able to: (i). associate and chaperone a large variety of cellular peptides; (ii). be efficiently internalized by antigen presenting cells (APC) through receptor-mediated endocytosis; (iii). channel antigenic peptides they chaperone in the APC's MHC class I presentation pathway; (iv). and stimulate inflammatory cytokines, chemokines and co-stimulatory molecules through the NFkappab signaling pathway. Extracellular release of hsps upon necrotic cell death and their modulated access at the surface of some cells, can be considered as a putative 'danger' signal. Based on the ancient origins and structural conservation of hsps, it has been proposed that, the role of hsps in immunity emerged early in evolution and to be widespread in extant organisms. Data from studies with the frog Xenopus support this proposition.
热休克蛋白（hsps）是细胞内最为丰富的蛋白质之一。包括温度、葡萄糖剥夺、感染和癌症在内的各种“应激源”可迅速上调其合成。某些热休克蛋白能够：（i）. 与多种细胞肽结合并充当伴侣蛋白；（ii）. 通过受体介导的内吞作用被抗原呈递细胞（APC）有效内化；（iii）. 在APC的MHC I类呈递途径中引导其所陪伴的抗原肽；（iv）. 并通过NFkappab信号通路刺激炎性细胞因子、趋化因子和共刺激分子。坏死性细胞死亡时热休克蛋白的细胞外释放以及它们在某些细胞表面的调节性接触，可被视为一种假定的“危险”信号。基于热休克蛋白的古老起源和结构保守性，有人提出，热休克蛋白在免疫中的作用在进化早期就已出现，并在现存生物体中广泛存在。来自对非洲爪蟾研究的数据支持这一观点。
