Abstract
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.
Highlights
Cells respond to stressful conditions by activating stress response proteins that promote cellular sustenance
We summarize the immunomodulatory activities of Heat shock proteins (HSPs) and recent advances in utilization of HSPs in anticancer immunotherapy
Cancer immunotherapy has gained great success as an effective therapeutic option in our fight against some malignant tumors such as melanoma. e potential of HSPs as therapeutic targets for immunotherapy has been increasingly appreciated in the past decade
Summary
Cells respond to stressful conditions by activating stress response proteins that promote cellular sustenance. Heat shock proteins (HSPs) are highly conserved stress response chaperone proteins, which are synthesized in response to various stresses. E ability of the HSPs to protect cells from damaging stress has been attributed to their chaperoning activity through which they prevent misfolding and expedite the refolding and renaturation of proteins [1, 2]. HSPs play critical roles in inhibiting proapoptogenic molecules through modulation of several signaling cascades such as JNK, AKT, and NF-κB [3]. E overwhelming evidence on the emerging role of HSPs in modulating carcinogenesis has precisely extended their relevance from simple diagnostic biomarkers to central targets in cancer therapeutics HSPs play critical roles in inhibiting proapoptogenic molecules through modulation of several signaling cascades such as JNK, AKT, and NF-κB [3]. e HSPs are at the core of maintaining a fine balance between cell death and survival, significantly impacting the biological consequences. e overwhelming evidence on the emerging role of HSPs in modulating carcinogenesis has precisely extended their relevance from simple diagnostic biomarkers to central targets in cancer therapeutics
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