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

•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.•HSP70 has a variety of cancer-related functions. HSP70 is abundantly expressed in cancer and has a wide range of activities.•...

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Published in:International immunopharmacology 2023-09, Vol.122, p.110492-110492, Article 110492
Main Authors: Sha, Gengyu, Jiang, Zhengting, Zhang, Wenjie, Jiang, Chuwen, Wang, Daorong, Tang, Dong
Format: Article
Language:English
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Summary:•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.•HSP70 has a variety of cancer-related functions. HSP70 is abundantly expressed in cancer and has a wide range of activities.•HSP70 is versatile in various ways, including promoting angiogenesis, inhibiting cellular senescence, enhancing tumor cell metastasis and serving as a biomarker for liquid biopsy. 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.
ISSN:1567-5769
1878-1705
DOI:10.1016/j.intimp.2023.110492