Kiang J G, Tsokos G C
Department of Clinical Physiology, Walter Reed Army Institute of Research, Washington, DC 20307-5100, USA.
Pharmacol Ther. 1998 Nov;80(2):183-201. doi: 10.1016/s0163-7258(98)00028-x.
Heat shock proteins (HSPs) are detected in all cells, prokaryotic and eukaryotic. In vivo and in vitro studies have shown that various stressors transiently increase production of HSPs as protection against harmful insults. Increased levels of HSPs occur after environmental stresses, infection, normal physiological processes, and gene transfer. Although the mechanisms by which HSPs protect cells are not clearly understood, their expression can be modulated by cell signal transducers, such as changes in intracellular pH, cyclic AMP, Ca2+, Na+, inositol trisphosphate, protein kinase C, and protein phosphatases. Most of the HSPs interact with other proteins in cells and alter their function. These and other protein-protein interactions may mediate the little understood effects of HSPs on various cell functions. In this review, we focus on the structure of the HSP-70 family (HSP-70s), regulation of HSP-70 gene expression, their cytoprotective effects, and the possibility of regulating HSP-70 expression through modulation of signal transduction pathways. The clinical importance and therapeutic potential of HSPs are discussed.
热休克蛋白（HSPs）在所有细胞中均有发现，包括原核细胞和真核细胞。体内和体外研究表明，各种应激源会短暂增加HSPs的产生，以抵御有害刺激。在环境应激、感染、正常生理过程以及基因转移后，HSPs水平会升高。尽管HSPs保护细胞的机制尚不清楚，但其表达可由细胞信号转导器调节，如细胞内pH值、环磷酸腺苷、Ca2+、Na+、肌醇三磷酸、蛋白激酶C和蛋白磷酸酶的变化。大多数HSPs在细胞内与其他蛋白质相互作用并改变其功能。这些以及其他蛋白质-蛋白质相互作用可能介导了HSPs对各种细胞功能的鲜为人知的影响。在本综述中，我们重点关注HSP-70家族（HSP-70s）的结构、HSP-70基因表达的调控、它们的细胞保护作用以及通过调节信号转导途径来调控HSP-70表达的可能性。文中还讨论了HSPs的临床重要性和治疗潜力。
