Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
8.1
4.9
Journals
IJMS
Special Issues
The Function of Stress Proteins in Cell Death and Diseases
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

The Function of Stress Proteins in Cell Death and Diseases

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

Deadline for manuscript submissions: closed (20 August 2024) | Viewed by 14845

Special Issue Editor

Prof. Dr. Xiangwei Gao

E-Mail Website
Guest Editor
Department of Public Health, Zhejiang University School of Medicine, Hangzhou 310058, China
Interests: mRNA metabolism; non-coding RNA; stress response; cancer; cell death

Special Issue Information

Dear Colleagues,

Human cells are regularly subjected to a variety of stimuli, such as heat shock, nutrient deprivation, oxidative stress, and genotoxic stress. While global gene expression is shut down, stress proteins are particularly produced in response to stimuli. These stress proteins are key players in the maintenance of cellular homeostasis and control several cellular processes, such as autophagy, cell death, and proliferation. The dysfunction of stress proteins is constantly linked to human diseases such as cancer, metabolic disorders, and neurodegenerative diseases.

The purpose of this topic is to thoroughly examine the regulation of stress protein functions, how stress proteins affect cellular homeostasis, and how they relate to cancer, metabolic disorders, and other diseases. We welcome the submission of high-quality original research articles, short communications, reviews, mini-reviews, and perspective papers associated with any relevant field of study.

Prof. Dr. Xiangwei Gao
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

  • stress response
  • gene expression
  • cellular homeostasis
  • cell death
  • autophagy
  • cancer
  • metabolic disease
  • neurodegenerative disease

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (3 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

13 pages, 4530 KiB  
Article
SIRT6 Inhibits Anoikis of Colorectal Cancer Cells by Down-Regulating NDRG1
by Fengying Li, Wentao Yu, Xiaoling Zhou, Jingyu Hou, Yunyi Gao, Jun Zhang and Xiangwei Gao
Int. J. Mol. Sci. 2024, 25(11), 5585; https://doi.org/10.3390/ijms25115585 - 21 May 2024
Cited by 2 | Viewed by 1704
Abstract
Anoikis, a form of apoptosis resulting from the loss of cell–extracellular matrix interaction, is a significant barrier to cancer cell metastasis. However, the epigenetic regulation of this process remains to be explored. Here, we demonstrate that the histone deacetylase sirtuin 6 (SIRT6) plays [...] Read more.
Anoikis, a form of apoptosis resulting from the loss of cell–extracellular matrix interaction, is a significant barrier to cancer cell metastasis. However, the epigenetic regulation of this process remains to be explored. Here, we demonstrate that the histone deacetylase sirtuin 6 (SIRT6) plays a pivotal role in conferring anoikis resistance to colorectal cancer (CRC) cells. The protein level of SIRT6 is negatively correlated with anoikis in CRC cells. The overexpression of SIRT6 decreases while the knockdown of SIRT6 increases detachment-induced anoikis. Mechanistically, SIRT6 inhibits the transcription of N-myc downstream-regulated gene 1 (NDRG1), a negative regulator of the AKT signaling pathway. We observed the up-regulation of SIRT6 in advanced-stage CRC samples. Together, our findings unveil a novel epigenetic program regulating the anoikis of CRC cells. Full article
(This article belongs to the Special Issue The Function of Stress Proteins in Cell Death and Diseases)
►▼ Show Figures

Figure 1

Review

Jump to: Research

32 pages, 3501 KiB  
Review
Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases
by Manish Kumar Singh, Yoonhwa Shin, Songhyun Ju, Sunhee Han, Wonchae Choe, Kyung-Sik Yoon, Sung Soo Kim and Insug Kang
Int. J. Mol. Sci. 2024, 25(8), 4209; https://doi.org/10.3390/ijms25084209 - 10 Apr 2024
Cited by 36 | Viewed by 9605
Abstract
The heat shock response is an evolutionarily conserved mechanism that protects cells or organisms from the harmful effects of various stressors such as heat, chemicals toxins, UV radiation, and oxidizing agents. The heat shock response triggers the expression of a specific set of [...] Read more.
The heat shock response is an evolutionarily conserved mechanism that protects cells or organisms from the harmful effects of various stressors such as heat, chemicals toxins, UV radiation, and oxidizing agents. The heat shock response triggers the expression of a specific set of genes and proteins known as heat shock genes/proteins or molecular chaperones, including HSP100, HSP90, HSP70, HSP60, and small HSPs. Heat shock proteins (HSPs) play a crucial role in thermotolerance and aiding in protecting cells from harmful insults of stressors. HSPs are involved in essential cellular functions such as protein folding, eliminating misfolded proteins, apoptosis, and modulating cell signaling. The stress response to various environmental insults has been extensively studied in organisms from prokaryotes to higher organisms. The responses of organisms to various environmental stressors rely on the intensity and threshold of the stress stimuli, which vary among organisms and cellular contexts. Studies on heat shock proteins have primarily focused on HSP70, HSP90, HSP60, small HSPs, and ubiquitin, along with their applications in human biology. The current review highlighted a comprehensive mechanism of heat shock response and explores the function of heat shock proteins in stress management, as well as their potential as therapeutic agents and diagnostic markers for various diseases. Full article
(This article belongs to the Special Issue The Function of Stress Proteins in Cell Death and Diseases)
►▼ Show Figures

Figure 1

45 pages, 2569 KiB  
Review
Modulating Stress Proteins in Response to Therapeutic Interventions for Parkinson’s Disease
by Serena Silvestro, Ivana Raffaele and Emanuela Mazzon
Int. J. Mol. Sci. 2023, 24(22), 16233; https://doi.org/10.3390/ijms242216233 - 12 Nov 2023
Cited by 5 | Viewed by 2657
Abstract
Parkinson’s disease (PD) is a neurodegenerative illness characterized by the degeneration of dopaminergic neurons in the substantia nigra, resulting in motor symptoms and without debilitating motors. A hallmark of this condition is the accumulation of misfolded proteins, a phenomenon that drives disease progression. [...] Read more.
Parkinson’s disease (PD) is a neurodegenerative illness characterized by the degeneration of dopaminergic neurons in the substantia nigra, resulting in motor symptoms and without debilitating motors. A hallmark of this condition is the accumulation of misfolded proteins, a phenomenon that drives disease progression. In this regard, heat shock proteins (HSPs) play a central role in the cellular response to stress, shielding cells from damage induced by protein aggregates and oxidative stress. As a result, researchers have become increasingly interested in modulating these proteins through pharmacological and non-pharmacological therapeutic interventions. This review aims to provide an overview of the preclinical experiments performed over the last decade in this research field. Specifically, it focuses on preclinical studies that center on the modulation of stress proteins for the treatment potential of PD. The findings display promise in targeting HSPs to ameliorate PD outcomes. Despite the complexity of HSPs and their co-chaperones, proteins such as HSP70, HSP27, HSP90, and glucose-regulated protein-78 (GRP78) may be efficacious in slowing or preventing disease progression. Nevertheless, clinical validation is essential to confirm the safety and effectiveness of these preclinical approaches. Full article
(This article belongs to the Special Issue The Function of Stress Proteins in Cell Death and Diseases)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-3
Back to TopTop