Du Sihan, Liu Ying, Yuan Yuan, Wang Yuran, Chen Yanfang, Wang Shuai, Chi Yuhua
School of Medical Imaging, Weifang Medical University, Weifang, Shandong, China.
Department of Radiotherapy, Affiliated Hospital of Weifang Medical University, Weifang, Shandong, China.
Front Cell Dev Biol. 2022 Aug 10;10:942828. doi: 10.3389/fcell.2022.942828. eCollection 2022.
The 70 kDa heat shock protein (HSP70) is one of the most conserved proteins and a ubiquitous molecular chaperone that plays a role in the folding, remodeling, and degradation of various proteins to maintain proteostasis. It has been shown that HSP70 is abundantly expressed in cancer and enhances tumor resistance to radiotherapy by inhibiting multiple apoptotic pathways, such as interfering with the cellular senescence program, promoting angiogenesis, and supporting metastasis. Thus, HSP70 provides an effective target for enhancing the effects of radiation therapy in the clinical management of cancer patients. Inhibition of HSP70 enhances the radiation-induced tumor-killing effect and thus improves the efficacy of radiotherapy. This article reviews the sensitivity of Hsp70 and its related inhibitors to radiotherapy of tumor cells.
70 kDa热休克蛋白(HSP70)是最保守的蛋白质之一,也是一种普遍存在的分子伴侣,在各种蛋白质的折叠、重塑和降解过程中发挥作用,以维持蛋白质稳态。研究表明,HSP70在癌症中大量表达,并通过抑制多种凋亡途径增强肿瘤对放疗的抗性,如干扰细胞衰老程序、促进血管生成和支持转移。因此,HSP70为提高癌症患者临床治疗中放射治疗的效果提供了一个有效的靶点。抑制HSP70可增强辐射诱导的肿瘤杀伤作用,从而提高放疗疗效。本文综述了Hsp70及其相关抑制剂对肿瘤细胞放疗的敏感性。