Abstract
Intracellular heat shock proteins (HSP) are overexpressed in majority of malignantly transformed cells providing stress-tolerance of tumor cells and playing important role in pathophysiology of tumor growth. The discovery of this fact has led to the development of anticancer drugs targeting molecular chaperone neutralization to sensitize tumor cells to such stressors as chemo- and radiotherapy. However, the results of applying these preparations proved to be insufficiently efficient in inhibiting tumor growth and preventing tumor progression. The finding about membrane and extracellular HSP localization has initiated a new trend in the development of methods of active immunotherapy of cancer. This has become possible due to the molecular chaperone’s ability to transform even the most tolerogenic tumor-associated antigens into immunogenic in the reaction of cross-presentation, as well as the HSP ability to function as endogenous alarmins – the agonists of pattern recognition receptor structures of the immune system – which stimulate functional maturation of antigen presenting cells. Thus, this chapter summarizes the reported as well as our own data concerning the application of HSP in cancer immune therapy.
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Abbreviations
- APC:
-
Antigen presenting cells
- CTL:
-
Cytotoxic T-lymphocytes
- FDA:
-
Food and Drug Administration, USA
- HSP:
-
Heat shock proteins
- LOX-1:
-
Lectin-like oxidized low-density lipoprotein receptor-1
- MHC:
-
The major histocompatibility complex
- siRNA:
-
Small interfering RNA
- SREC-1:
-
Scavenger receptor expressed by endothelial cells-1
- TLR:
-
Toll-like receptors
- Treg:
-
Regulatory T-cells
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Acknowledgements
This work was supported by R.E. Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, NAS of Ukraine and Taras Shevchenko National University of Kyiv.
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Didenko, G., Kruts, O., Skivka, L., Prylutskyy, Y. (2018). The Effectiveness of Antitumor Vaccine Enriched with a Heat Shock Protein 70. In: Asea, A., Kaur, P. (eds) HSP70 in Human Diseases and Disorders. Heat Shock Proteins, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-89551-2_17
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