Molecular Chaperone: Cancer and Cell Death 2021

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Pathology".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 3722

Special Issue Editor


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Guest Editor
Laboratory of Cell Protection Mechanisms, Institute of Cytology of Russian Academy of Sciences, 194064 St. Petersburg, Russia
Interests: molecular chaperones; protein–protein interactions; molecular targets in anticancer therapy; propagation of neurodegenerative pathologies
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Special Issue Information

Dear Colleagues, 

The analysis of systems maintaining cell proteostasis and based on molecular chaperones shows that these mechanisms are closely associated with the molecular systems controlling cell survival, growth, and proliferation. Moreover, chaperones are essential to the immunological response to a variety of pathogenic as well as therapeutic factors. It is also important to note that elevating the chaperone content in cells increases their protection against harmful agents. Cancer cells of many types overexpress chaperones to fight against well-known stressors, such as oxidative stress and hypoxia, as well as against antitumor medicines, particularly drugs inducing apoptosis. Generally, chaperones are activated by transcriptional signals controlling the behavior of a cell in changing surroundings, while, functionally, the chaperones are involved in the most important processes, defining a compromise between cell death, life, and growth and being implicated in apoptosis, autophagy, and protein quality control. Therefore, targeting molecular chaperones may cause fluctuations in different signaling systems, and such inhibition has been shown to result in tumor delay or death. Strikingly, some chaperones occurring exogenously play a pivotal role in the induction of the immunological response to tumors, and this effect is employed in the protocols of the immunotherapy of hard tumors.

The role of molecular chaperones in human pathologies is contradictory, and in cancer therapy, we should employ instruments suppressing chaperones; while fighting against pathogenic factors affecting normal cells, the activity of the heat shock proteins must be increased. 

The goal of this Special Issue is to broadly present the current knowledge on the role of chaperones in the process of cancer progression and normal cell death/survival.

We look forward to your contributions.

Prof. Boris Margulis
Guest Editor

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Keywords

  • chaperones
  • cancer
  • heat shock
  • proteins immunotherapy

Published Papers (2 papers)

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17 pages, 3436 KiB  
Article
The Role of p53 Protein in the Realization of the Exogenous Heat Shock Protein 70 Anti-Apoptotic Effect during Axotomy
by Svetlana V. Demyanenko, Maria A. Pitinova, Valentina A. Dzreyan, Yuliya N. Kalyuzhnaya, Moez A. Eid, Andrey Y. Abramov, Michael B. Evgen’ev and David G. Garbuz
Cells 2022, 11(1), 93; https://doi.org/10.3390/cells11010093 - 29 Dec 2021
Cited by 2 | Viewed by 1896
Abstract
The search for effective neuroprotective agents for the treatment of neurotrauma has always been of great interest to researchers around the world. Extracellular heat shock protein 70 (eHsp70) is considered a promising agent to study, as it has been demonstrated to exert a [...] Read more.
The search for effective neuroprotective agents for the treatment of neurotrauma has always been of great interest to researchers around the world. Extracellular heat shock protein 70 (eHsp70) is considered a promising agent to study, as it has been demonstrated to exert a significant neuroprotective activity against various neurodegenerative diseases. We showed that eHsp70 can penetrate neurons and glial cells when added to the incubation medium, and can accumulate in the nuclei of neurons and satellite glial cells after axotomy. eHsp70 reduces apoptosis and necrosis of the glial cells, but not the neurons. At the same time, co-localization of eHsp70 with p53 protein, one of the key regulators of apoptosis, was noted. eHsp70 reduces the level of the p53 protein apoptosis promoter both in glial cells and in the nuclei and cytoplasm of neurons, which indicates its neuroprotective effect. The ability of eHsp70 to reverse the proapoptotic effect of the p53 activator WR1065 may indicate its ability to regulate p53 activity or its proteosome-dependent degradation. Full article
(This article belongs to the Special Issue Molecular Chaperone: Cancer and Cell Death 2021)
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2 pages, 170 KiB  
Correction
Correction: Kim et al. Cell Surface GRP94 as a Novel Emerging Therapeutic Target for Monoclonal Antibody Cancer Therapy. Cells 2021, 10, 670
by Ji Woong Kim, Yea Bin Cho and Sukmook Lee
Cells 2021, 10(5), 1198; https://doi.org/10.3390/cells10051198 - 14 May 2021
Cited by 2 | Viewed by 1369
Abstract
In Section 4.1.3 of the published paper, the authors made an incorrect and unsupported statement regarding PU-H71 and a Samus-sponsored Phase 1 clinical trial [...] Full article
(This article belongs to the Special Issue Molecular Chaperone: Cancer and Cell Death 2021)
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