Abstract
Heat shock proteins (HSPs), most of which are molecular chaperones, are highly conserved proteins produced by cells under physiological stress or pathological conditions. HSP60 (57–69 kDa) can promote or inhibit cell apoptosis through different mechanisms, and its abnormal expression is also related to tumour cell metastasis and drug resistance. In recent years, HSP60 has received increasing attention in the field of cancer research due to its potential as a diagnostic and prognostic biomarker or therapeutic target. However, in different types of cancer, the specific mechanisms of abnormally expressed HSP60 in tumour carcinogenesis and drug resistance are complicated and still require further study. In this article, we comprehensively review the regulative mechanisms of HSP60 on apoptosis, its applications as a cancer diagnostic biomarker and a therapeutic target, evidence of involvement in tumour resistance and the applications of exosomal HSP60 in liquid biopsy. By evaluating the current findings of HSP60 in cancer research, we highlight some core issues that need to be addressed for the use of HSP60 as a diagnostic or prognostic biomarker and therapeutic target in certain types of cancer.
Acknowledgements
The authors thank Professor Takashi Ikejima of Shenyang Pharmaceutical University for his valuable suggestions on the manuscript.
Author contributions
Bo Sun: A student responsible for stating the idea of the article, conducting literature search and analysis, writing and revising the manuscript. Ganghui Li: A student who helping to revise figures. Qing Yu: A lecture responsible for writing and revising the manuscript. Dongchun Liu: A professor responsible for giving critical suggestions and revising the manuscript. Xing Tang: A professor responsible for giving critical suggestions.
Disclosure statement
No potential conflict of interest was reported by the author(s).