Heat Shock Proteins in Cancer Treatment

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Medical Research".

Deadline for manuscript submissions: closed (22 October 2022) | Viewed by 2294

Special Issue Editor


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Guest Editor
INSERM U1231 ‘Lipides Nutrition Cancer’, University of Burgundy, 21078 Dijon, France
Interests: heat shock proteins; cancer; DNA damage repair; chaperones

Special Issue Information

Dear Colleagues,

Cancer is one of the leading causes of deaths worldwide with around 10 million deaths each year. Due to the growth of populations and their aging, the burden of cancer is expected to grow, in both westernized societies where it is already dominant, but also worldwide. Despite decades of research on the subject, successfully treating cancer patients is still uncertain. Many factors have been shown to increase or decrease cancer patients’ odds of survival. Heat shock proteins (HSPs) are such factors and have been linked to negative outcomes in many cancers. HSPs are protein chaperones that protect cells from various stresses and insults and ensure the stability of the proteome. Tumors are submitted to the stress of their own modified biology and the tumor microenvironment. Furthermore, anticancer treatments represent an additional level of stress for cancer cells. It is therefore unsurprising that many studies conclude that HSPs increase the aggressivity of cancers and their resistance to treatments. This Special Edition focuses on the importance of HSPs in the context of treating cancer. The scope of this Special Edition covers in vitro, in vivo as well as clinical studies, and aims at reporting the latest findings in the following areas:

  • Exploring the pathways through which HSPs confer resistance to anticancer therapies.
  • Identifying anticancer therapies whose effectiveness is unaffected by HSPs.
  • Refining the prognosis value of HSP expression in specific cancer types and anticancer treatment.
  • The targeting of HSPs in order to ameliorate the effectiveness of anticancer therapies.

Dr. Sebastien Causse
Guest Editor

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Keywords

  • cancer
  • anticancer treatment
  • heat shock protein
  • heat shock response

Published Papers (1 paper)

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Review

15 pages, 901 KiB  
Review
Heat Shock Protein 70 and 90 Family in Prostate Cancer
by Xun Fu, Jiang Liu, Xin Yan, Michael E. DiSanto and Xinhua Zhang
Life 2022, 12(10), 1489; https://doi.org/10.3390/life12101489 - 26 Sep 2022
Cited by 8 | Viewed by 1887
Abstract
Prostate cancer (PCa) is the second most frequent cancer that affects aging men worldwide. However, its exact pathogenesis has not been fully elucidated. The heat shock protein (HSP) family has cell-protective properties that may promote tumor growth and protect cancer cells from death. [...] Read more.
Prostate cancer (PCa) is the second most frequent cancer that affects aging men worldwide. However, its exact pathogenesis has not been fully elucidated. The heat shock protein (HSP) family has cell-protective properties that may promote tumor growth and protect cancer cells from death. On a cellular level, HSP molecules have a strong relationship with multiple important biological processes, such as cell differentiation, epithelial–mesenchymal transition (EMT), and fibrosis. Because of the facilitation of HSP family molecules on tumorigenesis, a number of agents and inhibitors are being developed with potent antitumor effects whose target site is the critical structure of HSP molecules. Among all target molecules, HSP70 family and HSP90 are two groups that have been well studied, and therefore, the development of their inhibitors makes great progress. Only a small number of agents, however, have been clinically tested in recruited patients. As a result, more clinical studies are warranted for the establishment of the relationship between the HSP70 family, alongside the HSP90 molecule, and prostate cancer treatment. Full article
(This article belongs to the Special Issue Heat Shock Proteins in Cancer Treatment)
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