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Advances in Heat-Shock Response and Heat-Shock Proteins
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Advances in Heat-Shock Response and Heat-Shock Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 20 February 2025 | Viewed by 5795

Special Issue Editor

Dr. Nikolas Nikolaidis

E-Mail Website
Guest Editor
Department of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, CA 92834-6850, USA
Interests: heat-shock response; membrane-associated heat-shock proteins; protein–lipid interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to announce a forthcoming Special Issue entitled "Advances in Heat-Shock Response and Heat-Shock Proteins" in the Journal of International Journal of Molecular Sciences. This Special Issue will focus on recent discoveries related to the regulation and function of heat-shock proteins (HSPs) in maintaining protein homeostasis, managing stress, and influencing disease states. The key topics to be addressed include the post-translational modification of HSPs, the interplay between HSP pathways, the role of HSPs in neurodegenerative disorders and cancer, and more.

We welcome the submission of original research articles, authoritative reviews, perspectives, and commentaries. Through this Special Issue, we aim to compile high-quality contributions that enhance our understanding of the diverse functional roles and therapeutic potential of the heat-shock response. We look forward to your contributions to this exciting Special Issue exploring new frontiers in HSP research.

Dr. Nikolas Nikolaidis
Guest Editor

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 short 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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 (HSPs)
  • heat-shock response 
  • protein homeostasis
  • molecular chaperones
  • neurodegenerative disorders
  • cancer
  • cell signaling
  • post-translational modifications
  • proteostasis
  • stress response

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Published Papers (4 papers)

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Research

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17 pages, 1489 KiB  
Article
Prenatal Acoustic Signals Influence Nestling Heat Shock Protein Response to Heat and Heterophil-to-Lymphocyte Ratio in a Desert Bird
by Eve Udino, Anaïs Pessato, BriAnne Addison, Ondi L. Crino, Katherine L. Buchanan and Mylene M. Mariette
Int. J. Mol. Sci. 2024, 25(22), 12194; https://doi.org/10.3390/ijms252212194 - 13 Nov 2024
Viewed by 443
Abstract
Heat shock proteins (HSPs) are essential to cellular protection against heat stress. However, the causes of inter-individual variation in HSP regulation remain unclear. This study aimed to test the impact of early-life conditions on the HSP response to heat in zebra finches. In [...] Read more.
Heat shock proteins (HSPs) are essential to cellular protection against heat stress. However, the causes of inter-individual variation in HSP regulation remain unclear. This study aimed to test the impact of early-life conditions on the HSP response to heat in zebra finches. In this arid-adapted bird, incubating parents emit “heat-calls” at high temperatures, which adaptively alter offspring’s phenotypes. Embryos were exposed to heat-calls or control-calls, and at 13 days post-hatch nestlings were separated into two different experiments to test responses to either chronic nest temperature (“in-nest” experiment) or an acute “heat-challenge”. Blood samples were collected to measure levels of heat shock cognate 70, heat shock protein 90α, corticosterone and the heterophil-to-lymphocyte (H/L) ratio. In the in-nest experiment, both HSPs were upregulated in response to increasing nest temperatures only in control-calls nestlings (HSC70: p = 0.010, HSP90α: p = 0.050), which also had a marginally higher H/L ratio overall than heat-call birds (p = 0.066). These results point to a higher heat sensitivity in control-call nestlings. Furthermore, comparing across experiments, only the H/L ratio differed, being higher in heat-challenged than in in-nest nestlings (p = 0.009). Overall, this study shows for the first time that a prenatal acoustic signal of heat affects the nestling HSP response to postnatal temperature. Full article
(This article belongs to the Special Issue Advances in Heat-Shock Response and Heat-Shock Proteins)
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15 pages, 3065 KiB  
Article
Skeletal Muscle Heat Shock Protein Content and the Repeated Bout Effect
by Marius Locke and Giovanni Bruccoleri
Int. J. Mol. Sci. 2024, 25(7), 4017; https://doi.org/10.3390/ijms25074017 - 4 Apr 2024
Viewed by 1133
Abstract
The “Repeated Bout Effect” (RBE) occurs when a skeletal muscle is preconditioned with a few lengthening contractions (LC) prior to exposing the muscle to a greater number of LC. The preconditioning (PC) results in significantly less damage and preservation of force. Since it [...] Read more.
The “Repeated Bout Effect” (RBE) occurs when a skeletal muscle is preconditioned with a few lengthening contractions (LC) prior to exposing the muscle to a greater number of LC. The preconditioning (PC) results in significantly less damage and preservation of force. Since it takes only a few LC to increase muscle heat shock protein (HSP) content, it was of interest to examine the relationship between HSPs and the RBE. To do this, one tibialis anterior (TA) muscle from Sprague–Dawley rats (n = 5/group) was preconditioned with either 0, 5, or 15 lengthening contractions (LC) and exposed to a treatment of 60 LC 48 h later. Preconditioning TA muscles with 15 LC, but not 5 LC, significantly elevated muscle αB-crystallin (p < 0.05), HSP25 (p < 0.05), and HSP72 content (p < 0.001). These preconditioned TA muscles also showed a significantly (p < 0.05) reduced loss of active torque throughout the subsequent 60 LC. While there was a trend for all preconditioned muscles to maintain higher peak torque levels throughout the 60 LC, no significant differences were detected between the groups. Morphologically, preconditioned muscles appeared to show less discernible muscle fiber damage. In conclusion, an elevated skeletal muscle HSP content from preconditioning may contribute to the RBE. Full article
(This article belongs to the Special Issue Advances in Heat-Shock Response and Heat-Shock Proteins)
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18 pages, 5762 KiB  
Article
Perturbation of Copper Homeostasis Sensitizes Cancer Cells to Elevated Temperature
by Enzo M. Scutigliani, Jons van Hattum, Fernando Lobo-Cerna, Joanne Kruyswijk, Maja Myrcha, Frederique E. G. A. Dekkers, Ron A. Hoebe, Finn Edwards, Jetta J. Oppelaar, Liffert Vogt, Sanne Bootsma, Maarten F. Bijlsma, Daisy I. Picavet, Johannes Crezee, Jorg R. Oddens, Theo M. de Reijke and Przemek M. Krawczyk
Int. J. Mol. Sci. 2024, 25(1), 423; https://doi.org/10.3390/ijms25010423 - 28 Dec 2023
Viewed by 1293
Abstract
Temporary elevation of tumor temperature, also known as hyperthermia, is a safe and well-tolerated treatment modality. The efficacy of hyperthermia can be improved by efficient thermosensitizers, and various candidate drugs, including inhibitors of the heat stress response, have been explored in vitro and [...] Read more.
Temporary elevation of tumor temperature, also known as hyperthermia, is a safe and well-tolerated treatment modality. The efficacy of hyperthermia can be improved by efficient thermosensitizers, and various candidate drugs, including inhibitors of the heat stress response, have been explored in vitro and in animal models, but clinically relevant thermosensitizers are lacking. Here, we employ unbiased in silico approaches to uncover new mechanisms and compounds that could be leveraged to increase the thermosensitivity of cancer cells. We then focus on elesclomol, a well-performing compound, which amplifies cell killing by hyperthermia by 5- to 20-fold in cell lines and outperforms clinically applied chemotherapy when combined with hyperthermia in vitro. Surprisingly, our findings suggest that the thermosensitizing effects of elesclomol are independent of its previously reported modes of action but depend on copper shuttling. Importantly, we show that, like elesclomol, multiple other copper shuttlers can thermosensitize, suggesting that disturbing copper homeostasis could be a general strategy for improving the efficacy of hyperthermia. Full article
(This article belongs to the Special Issue Advances in Heat-Shock Response and Heat-Shock Proteins)
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Review

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25 pages, 1575 KiB  
Review
Molecular Chaperonin HSP60: Current Understanding and Future Prospects
by Manish Kumar Singh, Yoonhwa Shin, Sunhee Han, Joohun Ha, Pramod K. Tiwari, Sung Soo Kim and Insug Kang
Int. J. Mol. Sci. 2024, 25(10), 5483; https://doi.org/10.3390/ijms25105483 - 17 May 2024
Cited by 3 | Viewed by 2175
Abstract
Molecular chaperones are highly conserved across evolution and play a crucial role in preserving protein homeostasis. The 60 kDa heat shock protein (HSP60), also referred to as chaperonin 60 (Cpn60), resides within mitochondria and is involved in maintaining the organelle’s proteome integrity and [...] Read more.
Molecular chaperones are highly conserved across evolution and play a crucial role in preserving protein homeostasis. The 60 kDa heat shock protein (HSP60), also referred to as chaperonin 60 (Cpn60), resides within mitochondria and is involved in maintaining the organelle’s proteome integrity and homeostasis. The HSP60 family, encompassing Cpn60, plays diverse roles in cellular processes, including protein folding, cell signaling, and managing high-temperature stress. In prokaryotes, HSP60 is well understood as a GroEL/GroES complex, which forms a double-ring cavity and aids in protein folding. In eukaryotes, HSP60 is implicated in numerous biological functions, like facilitating the folding of native proteins and influencing disease and development processes. Notably, research highlights its critical involvement in sustaining oxidative stress and preserving mitochondrial integrity. HSP60 perturbation results in the loss of the mitochondria integrity and activates apoptosis. Currently, numerous clinical investigations are in progress to explore targeting HSP60 both in vivo and in vitro across various disease models. These studies aim to enhance our comprehension of disease mechanisms and potentially harness HSP60 as a therapeutic target for various conditions, including cancer, inflammatory disorders, and neurodegenerative diseases. This review delves into the diverse functions of HSP60 in regulating proteo-homeostasis, oxidative stress, ROS, apoptosis, and its implications in diseases like cancer and neurodegeneration. Full article
(This article belongs to the Special Issue Advances in Heat-Shock Response and Heat-Shock Proteins)
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