Ohtsuka K, Suzuki T
Cell Stress Biology Research Group, Aichi Cancer Center Research Institute, Chikusa-ku, Nagoya, Japan.
Brain Res Bull. 2000 Sep 15;53(2):141-6. doi: 10.1016/s0361-9230(00)00325-7.
Heat shock proteins (HSPs) are induced not only by heat shock but also by various other environmental stresses. HSPs such as Hsp90, Hsp70, Hsp60, Hsp40 and Hsp28 are also expressed constitutively at normal growth temperatures and have basic and indispensable functions in the life cycle of proteins as molecular chaperones, as well as playing a role in protecting cells from deleterious stresses. Recently, Hsc70 and Hsp40 were found to be localized to the synapse in the mammalian central nervous system, indicating a synaptic role for these HSPs. Molecular chaperones are able to inhibit the aggregation of partially denatured proteins and refold them. In addition, molecular chaperones, especially Hsp70, protect the brain and heart from severe ischemia. In these respects, there are expectations for the use of molecular chaperones for protection against and therapeutic treatment of inherited diseases caused by protein misfolding. In this study, we review Hsp70 and Hsp40, and refer to the roles of these molecules in the synapse and cytoprotective functions of HSPs in stress tolerance and neurodegenerative diseases.
热休克蛋白（HSPs）不仅可由热休克诱导产生，也可由各种其他环境应激诱导产生。诸如Hsp90、Hsp70、Hsp60、Hsp40和Hsp28等热休克蛋白在正常生长温度下也会组成性表达，并作为分子伴侣在蛋白质的生命周期中发挥基本且不可或缺的功能，同时在保护细胞免受有害应激方面也发挥作用。最近，人们发现Hsc70和Hsp40定位于哺乳动物中枢神经系统的突触，这表明这些热休克蛋白在突触中发挥作用。分子伴侣能够抑制部分变性蛋白质的聚集并使其重新折叠。此外，分子伴侣，尤其是Hsp70，可保护大脑和心脏免受严重缺血的影响。在这些方面，人们期望利用分子伴侣来预防和治疗由蛋白质错误折叠引起的遗传性疾病。在本研究中，我们综述了Hsp70和Hsp40，并提及了这些分子在突触中的作用以及热休克蛋白在应激耐受性和神经退行性疾病中的细胞保护功能。
