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Cancers
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Heat Shock Proteins in Cancers
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Heat Shock Proteins in Cancers

A special issue of Cancers (ISSN 2072-6694). This special issue belongs to the section "Tumor Microenvironment".

Deadline for manuscript submissions: closed (15 December 2024) | Viewed by 6179

Special Issue Editors

Prof. Dr. Anna Lubkowska

E-Mail Website
Guest Editor
Chair and Department of Functional Diagnostic and Physical Medicine, Pomeranian Medical University in Szczecin, ul. Żołnierska 54, 71-210 Szczecin, Poland
Interests: thermoregulation; adaptive physiology; physical activity; rehabilitation; sports medicine; aging
Special Issues, Collections and Topics in MDPI journals
Dr. Weronika Ratajczak

E-Mail Website
Guest Editor
Chair and Department of Functional Diagnostics and Physical Medicine, Pomeranian Medical University, Żołnierska 54, 71-210 Szczecin, Poland
Interests: aging; microbiota; prostatic diseases; immunology; cancer biology

Special Issue Information

Dear Colleagues,

Heat shock proteins (HSPs), molecular chaperone proteins, are known to be one of the main proteins that play a role in maintaining cell homeostasis. They are involved in the process of protein folding and its maturation; they also play a role in cell proliferation and differentiation, as well as in the process of carcinogenesis. The increased expression of HSPs that occurs during the neoplastic process favors the creation of an environment suitable for the development of a neoplastic tumor, during which cellular homeostasis is dysregulated. HSPs are of multidirectional importance in the development of cancer, including by increasing their proliferation, promoting the avoidance of antigrowth signals and escaping from cell death, inhibiting cell aging, increasing angiogenesis and metastasis, or avoiding responses from the immune system.

Due to their properties, HSPs are an alternative to anticancer therapy, e.g., when tumor cells become resistant to currently available treatment. The inhibition of HSPs in cancer therapy may provide promising results, among others, by eliminating proteins responsible for tumor growth. Tumor-specific HSPs may be good prognostic markers of an organism's response to treatment.

Understanding the exact mechanisms of HSP (intracellular and extracellular) action is important due to the development of alternative, but also more precise methods of treatment of various types of cancers of clinical significance.

Prof. Dr. Anna Lubkowska
Dr. Weronika Ratajczak
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cancers is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • heat shock proteins
  • extracellular HSPs
  • intracellular HSPs
  • cancer
  • cancer therapy
  • biomarkers
  • molecular targets
  • cancer biology
  • cancer pharmacology

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Published Papers (2 papers)

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Research

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17 pages, 3414 KiB  
Article
TLR2-Bound Cancer-Secreted Hsp70 Induces MerTK-Mediated Immunosuppression and Tumorigenesis in Solid Tumors
by Ahmet Kaynak, Subrahmanya D. Vallabhapurapu, Harold W. Davis, Eric P. Smith, Petr Muller, Borek Vojtesek, Robert S. Franco, Wen-Hai Shao and Xiaoyang Qi
Cancers 2025, 17(3), 450; https://doi.org/10.3390/cancers17030450 - 28 Jan 2025
Cited by 2 | Viewed by 1114
Abstract
Background: A hallmark of cancer is the presence of an immunosuppressive tumor microenvironment (TME). Immunosuppressive M2 macrophages (MΦs) in the TME facilitate escape from immune surveillance and promote tumor growth; therefore, TME-induced immunosuppression is a potent immunotherapeutic approach to treating cancer. Methods [...] Read more.
Background: A hallmark of cancer is the presence of an immunosuppressive tumor microenvironment (TME). Immunosuppressive M2 macrophages (MΦs) in the TME facilitate escape from immune surveillance and promote tumor growth; therefore, TME-induced immunosuppression is a potent immunotherapeutic approach to treating cancer. Methods: Cancer cell-secreted proteins were detected by using liquid chromatography–mass spectrometry (LC-MS). Neutralizing antibodies (nAbs) were used to assess which proteins were involved in MΦs polarization and differentiation. The protein–protein interaction was characterized using co-immunoprecipitation and immunofluorescence assays. Cancer-secreted heat shock protein 70 (Hsp70) protein was quantified using an enzyme-linked immunosorbent assay (ELISA). MΦ polarization and tumor growth were assessed in vivo with subcutaneous LLC-GFP tumor models and toll-like receptor 2 (TLR2) knockout mice; in vitro assessments were conducted using TLR2 knockout and both LLC-GFP and LN227 lentiviral-mediated knockdown (KD) cells. Results: Cancer cells released a secreted form of Hsp70 that acted on MΦ TLR2 to upregulate Mer receptor tyrosine kinase (MerTK) and induce MΦ M2 polarization. Hsp70 nAbs led to a reduction in CD14 expression by 75% in THP-1 cells in response to Gli36 EMD-CM. In addition, neutralizing TLR2 nAbs resulted in a 30% and 50% reduction in CD14 expression on THP-1 cells in response to MiaPaCa-2 and Gli36 exosome/microparticle-depleted conditioned media (EMD-CMs), respectively. Hsp70, TLR2, and MerTK formed a protein complex. Tumor growth and intra-tumor M2 MΦs were significantly reduced upon cancer cell Hsp70 knockdown and in TLR2 knockout mice. Conclusions: Cancer-secreted Hsp70 interacts with TLR2, upregulates MerTK on MΦs, and induces immunosuppressive MΦ M2 polarization. This previously unreported action of secreted Hsp70 suggests that disrupting the Hsp70-TLR2-MerTK interaction could serve as a promising immunotherapeutic approach to mitigate TME immunosuppression in solid cancers. Full article
(This article belongs to the Special Issue Heat Shock Proteins in Cancers)
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Review

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38 pages, 1732 KiB  
Review
Heat Shock Proteins, a Double-Edged Sword: Significance in Cancer Progression, Chemotherapy Resistance and Novel Therapeutic Perspectives
by Dominika Kunachowicz, Magdalena Król-Kulikowska, Wiktoria Raczycka, Jakub Sleziak, Marta Błażejewska and Julita Kulbacka
Cancers 2024, 16(8), 1500; https://doi.org/10.3390/cancers16081500 - 14 Apr 2024
Cited by 8 | Viewed by 4462
Abstract
Heat shock proteins (Hsps) are involved in one of the adaptive mechanisms protecting cells against environmental and metabolic stress. Moreover, the large role of these proteins in the carcinogenesis process, as well as in chemoresistance, was noticed. This review aims to draw attention [...] Read more.
Heat shock proteins (Hsps) are involved in one of the adaptive mechanisms protecting cells against environmental and metabolic stress. Moreover, the large role of these proteins in the carcinogenesis process, as well as in chemoresistance, was noticed. This review aims to draw attention to the possibilities of using Hsps in developing new cancer therapy methods, as well as to indicate directions for future research on this topic. In order to discuss this matter, a thorough review of the latest scientific literature was carried out, taking into account the importance of selected proteins from the Hsp family, including Hsp27, Hsp40, Hsp60, Hsp70, Hsp90 and Hsp110. One of the more characteristic features of all Hsps is that they play a multifaceted role in cancer progression, which makes them an obvious target for modern anticancer therapy. Some researchers emphasize the importance of directly inhibiting the action of these proteins. In turn, others point to their possible use in the design of cancer vaccines, which would work by inducing an immune response in various types of cancer. Due to these possibilities, it is believed that the use of Hsps may contribute to the progress of oncoimmunology, and thus help in the development of modern anticancer therapies, which would be characterized by higher effectiveness and lower toxicity to the patients. Full article
(This article belongs to the Special Issue Heat Shock Proteins in Cancers)
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