The multifunction of HSP70 in cancer: Guardian or traitor to the survival of tumor cells and the next potential therapeutic target.

Abstract

Heat shock protein 70 (HSP70) is a highly conserved protein composed of nucleotide-binding domains (NBD) and C-terminal substrate binding domain (SBD) that can function as a "molecular chaperone". HSP70 was discovered to directly or indirectly play a regulatory role in both internal and external apoptosis pathways. Studies have shown that HSP70 can not only promote tumor progression, enhance tumor cell resistance and inhibit anticancer effects but also induce an anticancer response by activating immune cells. In addition, chemotherapy, radiotherapy and immunotherapy for cancer may be affected by HSP70, which has shown promising potential as an anticancer drug. In this review, we summarized the molecular structure and mechanism of HSP70 and discussed the dual effects of HSP70 on tumor cells and the possibility and potential methods of using HSP70 as a target to treat cancer.