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Heat shock proteins in cancer - Known but always being rediscovered: Their perspectives in cancer immunotherapy

A. Mazurakova, Z. Solarova, L. Koklesova, M. Caprnda, R. Prosecky, A. Khakymov, D. Baranenko, P. Kubatka, L. Mirossay, P. Kruzliak, P. Solar

. 2023 ; 68 (2) : 464-473. [pub] 20231104

Language English Country Netherlands

Document type Journal Article, Review

Persistent link   https://www.medvik.cz/link/bmc24001247

Heat shock proteins (HSPs) represent cellular chaperones that are classified into several families, including HSP27, HSP40, HSP60, HSP70, and HSP90. The role of HSPs in the cell includes the facilitation of protein folding and maintaining protein structure. Both processes play crucial roles during stress conditions in the cell such as heat shock, degradation, and hypoxia. Moreover, HSPs are important modulators of cellular proliferation and differentiation, and are strongly associated with the molecular orchestration of carcinogenesis. The expression and/or activity of HSPs in cancer cells is generally abnormally high and is associated with increased metastatic potential and activity of cancer stem cells, more pronounced angiogenesis, downregulated apoptosis, and the resistance to anticancer therapy in many patients. Based on the mentioned reasons, HSPs have strong potential as valid diagnostic, prognostic, and therapeutic biomarkers in clinical oncology. In addition, numerous papers describe the role of HSPs as chaperones in the regulation of immune responses inside and outside the cell. Importantly, highly expressed/activated HSPs may be inhibited via immunotherapeutic targets in various types of cancers. The aim of this work is to provide a comprehensive overview of the relationship between HSPs and the tumor cell with the intention of highlighting the potential use of HSPs in personalized cancer management.

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$a Mazurakova, Alena $u Department of Anatomy, Jessenius Faculty of Medicine, Comenius University in Bratislava, Martin, Slovakia
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$a Heat shock proteins (HSPs) represent cellular chaperones that are classified into several families, including HSP27, HSP40, HSP60, HSP70, and HSP90. The role of HSPs in the cell includes the facilitation of protein folding and maintaining protein structure. Both processes play crucial roles during stress conditions in the cell such as heat shock, degradation, and hypoxia. Moreover, HSPs are important modulators of cellular proliferation and differentiation, and are strongly associated with the molecular orchestration of carcinogenesis. The expression and/or activity of HSPs in cancer cells is generally abnormally high and is associated with increased metastatic potential and activity of cancer stem cells, more pronounced angiogenesis, downregulated apoptosis, and the resistance to anticancer therapy in many patients. Based on the mentioned reasons, HSPs have strong potential as valid diagnostic, prognostic, and therapeutic biomarkers in clinical oncology. In addition, numerous papers describe the role of HSPs as chaperones in the regulation of immune responses inside and outside the cell. Importantly, highly expressed/activated HSPs may be inhibited via immunotherapeutic targets in various types of cancers. The aim of this work is to provide a comprehensive overview of the relationship between HSPs and the tumor cell with the intention of highlighting the potential use of HSPs in personalized cancer management.
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$a Solarova, Zuzana $u Department of Pharmacology, Faculty of Medicine, Pavol Jozef Safarik University, Kosice, Slovakia
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$a Koklesova, Lenka $u Clinic of Obstetrics and Gynecology, Jessenius Faculty of Medicine, Comenius University in Bratislava, Martin, Slovakia
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$a Caprnda, Martin $u 1st Department of Internal Medicine, Faculty of Medicine, Comenius University and University Hospital, Bratislava, Slovakia
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$a Prosecky, Robert $u 2nd Department of Internal Medicine, Faculty of Medicine, Masaryk University and St. Anne's University Hospital, Brno, Czech Republic; International Clinical Research Centre, St. Anne's University Hospital and Masaryk University, Brno, Czech Republic
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$a Khakymov, Artur $u International Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint-Petersburg, Russian Federation
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$a Baranenko, Denis $u International Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint-Petersburg, Russian Federation
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$a Kubatka, Peter $u Department of Histology and Embryology, Jessenius Faculty of Medicine, Comenius University in Bratislava, Martin, Slovakia
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$a Mirossay, Ladislav $u Department of Pharmacology, Faculty of Medicine, Pavol Jozef Safarik University, Kosice, Slovakia
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$a Kruzliak, Peter $u 2nd Department of Surgery, Faculty of Medicine, Masaryk University and St. Anne's University Hospital, Brno, Czech Republic. Electronic address: kruzliakpeter@gmail.com
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$a Solar, Peter $u Department of Medical Biology, Faculty of Medicine, Pavol Jozef Safarik University, Kosice, Slovakia. Electronic address: peter.solar@upjs.sk
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