Gabai Vladimir L, Sherman Michael Y
Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
J Appl Physiol (1985). 2002 Apr;92(4):1743-8. doi: 10.1152/japplphysiol.01101.2001.
Heat shock of mammalian cells causes protein damage and activates a number of signaling pathways. Some of these pathways enhance the ability of cells to survive heat shock, e.g., induction of molecular chaperones [heat shock protein (HSP) HSP72 and HSP27], activation of the protein kinases extracellular signal-regulated kinase and Akt, and phosphorylation of HSP27. On the other hand, heat shock can activate a stress kinase, c-Jun NH2-terminal kinase, thus triggering both apoptotic and nonapoptotic cell death programs. Recent data indicate that kinases activated by heat shock can regulate synthesis and functioning of the molecular chaperones, and these chaperones modulate activity of the cell death and survival pathways. Therefore, the overall balance of the pathways and their interplay determine whether a cell exposed to heat shock will die or survive and become stress tolerant.
哺乳动物细胞的热休克会导致蛋白质损伤并激活多种信号通路。其中一些通路可增强细胞在热休克中的存活能力，例如诱导分子伴侣[热休克蛋白（HSP）HSP72和HSP27]、激活蛋白激酶细胞外信号调节激酶和Akt以及HSP27的磷酸化。另一方面，热休克可激活应激激酶c-Jun氨基末端激酶，从而触发凋亡和非凋亡细胞死亡程序。最近的数据表明，热休克激活的激酶可调节分子伴侣的合成和功能，而这些分子伴侣可调节细胞死亡和存活通路的活性。因此，这些通路的总体平衡及其相互作用决定了暴露于热休克的细胞是会死亡还是存活并变得耐受应激。
