Heat Shock Proteins in Cancer Immunotherapy.

Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy.

Das JK ，Xiong X ，Ren X ，Yang JM ，Song J ... -  《-》

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

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.

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

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy.

Yun CW ，Kim HJ ，Lim JH ，Lee SH ... -  《Cells》

The role of heat shock proteins in cancer.

Heat shock proteins (HSPs) are an evolutionary family of proteins that act as molecular chaperones. According to their size they have been classified into the following families; HSP90, HSP70, HSP60, HSP40 and HSP27. They prevent the formation of nonspecific protein aggregates and they assist proteins in the acquisition of their normal architecture. Moreover, HSPs are likely to have anti-apoptotic properties and are actively involved in various processes as tumor cell proliferation, invasion, metastases and death. Notably, these proteins have been reported to be significantly elevated in a plethora of human cancers. Their over-expression has been robustly associated with therapeutic resistance and poor survival. In this way, HSPs may have important therapeutic implications and they can be targeted by specific drugs. In this review, we discuss the influence of HSP27, HSP40, HSP60, HSP70 and HSP90 on human cancers. In addition, we report the existing scientific data on this issue with an effort to highlight the possible future implication of HSPs as tumor biomarkers or drug targets for improving prognosis and treatment of cancer patients around the world.

Lianos GD ，Alexiou GA ，Mangano A ，Mangano A ，Rausei S ，Boni L ，Dionigi G ，Roukos DH ... -  《-》

Recent advances in heat shock proteins in cancer diagnosis, prognosis, metabolism and treatment.

Heat shock proteins (HSPs) are a group of proteins, also known as molecular chaperones, which participate in protein folding and maturation in response to stresses or high temperature. According to their molecular weights, mammalian HSPs are classified into HSP27, HSP40, HSP60, HSP70, HSP90, and large HSPs. Previous studies have revealed that HSPs play important roles in oncogenesis and malignant progression because they can modulate all six hallmark traits of cancer. Because of this, HSPs have been propelled into the spotlight as biomarkers for cancer diagnosis and prognosis, as well as an exciting anticancer drug target. However, the relationship between the expression level of HSPs and their activity and cancer diagnosis, prognosis, metabolism and treatment is not clear and has not been completely established. Herein, this review summarizes and discusses recent advances and perspectives in major HSPs as biomarkers for cancer diagnosis, as regulators for cancer metabolism or as therapeutic targets for cancer therapy, which may provide new directions to improve the accuracy of cancer diagnosis and develop more effective and safer anticancer therapeutics.

Yang S ，Xiao H ，Cao L 《-》