几种热激蛋白在细胞凋亡信号通路中的调控作用

Regulation of Apoptosis Signaling Pathway by Common Heat Shock Proteins

热激蛋白(heat shock proteins,HSPs)作为进化保守的蛋白家族之一,普遍存在于各种生物体中,并在生物体内发挥着重要的生理功能.大量的实验证据表明,热激蛋白与细胞凋亡密切相关,参与细胞凋亡信号通路的多个环节.近年来有关该领域的研究已获得了重要的突破与进展.一方面,热激蛋白主要起着抑制细胞凋亡、促进细胞存活的作用;另一方面,某些热激蛋白又能够作为凋亡蛋白的分子伴侣,促进细胞凋亡,比如HSP70能够激活DNase来促使细胞凋亡,线粒体内HSP60能够促进caspase依赖的细胞凋亡途径.本文在阐明细胞凋亡信号通路的基础上,综述了近年来几种不同热激蛋白家族(HSP90、HSP70、HSP60和小分子HSPs)在细胞凋亡调控中作用的研究进展,重点阐述了几种主要热激蛋白与细胞凋亡信号通路上相关因子的相互作用,并绘制了热激蛋白在细胞凋亡信号通路中的调控图,为进一步完善细胞凋亡调控网络研究提供一定的参考.

Heat shock proteins（HSPs）existed in various organisms as a conserved protein family.HSPs play important physiological functions in cell apoptosis and influence multiple components of the apoptotic pathways,such as to maintain cell survival by inhibiting the apoptotic cascades or to accelerate cell apoptosis as the chaperons of certain apoptotic factors.HSP70 and mitochondrial Hsp60 activate DNase and promote caspase-dependent apoptosis.In this review,we focus on the role of HSP90,HSP70,HSP60 and other small HSPs to summarize the interactions of HSPs with the components of the apoptotic pathways,and discuss their potentials for the regulation of the apoptotic signal networks.