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Special Issue "Endoplasmic Reticulum Stress and Unfolded Protein Response 2021"

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

Deadline for manuscript submissions: 30 June 2021.

Special Issue Editor

Prof. Ireneusz Majsterek
E-Mail Website
Guest Editor
Department of Clinical Chemistry and Biochemistry, Medical University of Lodz, Lodz, Poland
Interests: DNA damage and repair; kinases inhibitors; Unfolded Protein Response; eye disease
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

The endoplasmic reticulum (ER) plays a role in the maintenance of numerous aspects of cellular and organismal homeostasis by folding, modifying, and exporting nascent secretory and transmembrane proteins. Failure of the ER's adaptive capacity results in accumulation of unfolded or malfolded proteins in the ER lumen (ER stress). To avoid cellular damage, mammalian cells activate the specific signals from the ER to the cytosol or nucleus to enhance the capacity for protein folding, attenuate the synthesis of proteins, and degrade unfolded proteins. These signaling pathways are collectively known as the unfolded protein response (UPR). UPR was originally described as a system by which cells evade damage in response to acute ER perturbation. However, recent advances have revealed that UPR also regulates cell differentiation and maturation or basal cellular homeostasis. Further, ER stress has been reported to have relationships with neurodegenerative diseases, diabetes, metabolic syndromes, and cancer. Therefore, it has been attracting attention in terms of elucidating pathogenic mechanisms and developing therapeutics.

This Special Issue provides diverse aspects of ER stress and UPR in various physiological and pathological events. We invite authors to submit original research and review articles related to any research into ER stress and UPR signaling.

Prof. Ireneusz Majsterek
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 papers will be 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

  • ER stress
  • UPR signaling
  • Physiological ER stress
  • Protein folding
  • Unfolded proteins
  • ER stress sensors
  • ER-associated degradation
  • Protein quality control
  • ER stress-induced cell death
  • Protein misfolding disease

Published Papers (1 paper)

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Research

Open AccessArticle
Endoplasmic Reticulum Stress Contributes to Gefitinib-Induced Apoptosis in Glioma
Int. J. Mol. Sci. 2021, 22(8), 3934; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22083934 - 11 Apr 2021
Viewed by 277
Abstract
Adequate stress on the Endoplasmic Reticulum (ER) with the Unfolded Protein Response (UPR) could maintain glioma malignancy. Uncontrolled ER stress, on the other hand, predisposes an apoptosis-dominant UPR program. We studied here the proapoptotic actions of the Epidermal Growth Factor Receptor (EGFR) inhibitor [...] Read more.
Adequate stress on the Endoplasmic Reticulum (ER) with the Unfolded Protein Response (UPR) could maintain glioma malignancy. Uncontrolled ER stress, on the other hand, predisposes an apoptosis-dominant UPR program. We studied here the proapoptotic actions of the Epidermal Growth Factor Receptor (EGFR) inhibitor gefitinib, with the focus on ER stress. The study models were human H4 and U87 glioma cell lines. We found that the glioma cell-killing effects of gefitinib involved caspase 3 apoptotic cascades. Three branches of ER stress, namely Activating Transcription Factor-6 (ATF6), Protein Kinase R (PKR)-Like ER Kinase (PERK), and Inositol-Requiring Enzyme 1 (IRE1), were activated by gefitinib, along with the elevation of intracellular free Ca2+, Reactive Oxygen Species (ROS), and NADPH Oxidase2/4 (NOX2/4). Specifically, elevated IRE1 phosphorylation, Tumor Necrosis Factor (TNF) Receptor-Associated Factor-2 (TRAF2) expression, Apoptosis Signal-Regulating Kinase-1 (Ask1) phosphorylation, c-Jun N-Terminal Kinase (JNK) phosphorylation, and Noxa expression appeared in gefitinib-treated glioma cells. Genetic, pharmacological, and biochemical studies further indicated an active ROS/ER stress/Ask1/JNK/Noxa axis causing the glioma apoptosis induced by gefitinib. The findings suggest that ER-stress-based therapeutic targeting could be a promising option in EGFR inhibitor glioma therapy, and may ultimately achieve a better patient response. Full article
(This article belongs to the Special Issue Endoplasmic Reticulum Stress and Unfolded Protein Response 2021)
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