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Antioxidants
Special Issues
Oxidative-Stress in Human Diseases—3rd Edition
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Oxidative-Stress in Human Diseases—3rd Edition

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Health Outcomes of Antioxidants and Oxidative Stress".

Deadline for manuscript submissions: 31 October 2024 | Viewed by 1260

Special Issue Editor

Dr. Soliman Khatib

E-Mail Website
Guest Editor
1. Department of Natural Products and Nutrition, MIGAL—Galilee Research Institute, Kiryat Shmona 11016, Israel
2. Faculty of Sciences, Tel Hai Academic College, Qiryat Shemona 12208, Israel
Interests: natural compounds; analytical chemistry; metabolomics; oxidative stress; atherosclerosis
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Oxidative stress (OS) is essential in the pathogenesis of human chronic diseases such as cardiovascular and kidney diseases, diabetes, neurodegenerative disorders, cancer, inflammation-related diseases, and aging. OS is a condition characterized by an imbalance between the production and accumulation of oxygen and nitrogen reactive species (ROS/RNS) in cells and tissues, and it occurs when the generation of these compounds exceeds the ability of the biological system to neutralize them.

ROS/RNS, such as superoxide (O2•−), hydrogen peroxide (H2O2), hydroxyl radical (HO•), nitrogen oxide (NO•), peroxynitrite (ONOO−), and hypochlorous acid (HOCl), are all products of normal metabolic pathways in humans; their production may increase as a result of influential external factors, such as pollution, cigarette smoke, or internally, as a result of impaired intracellular metabolism. Long-term exposure to increased levels of ROS/RNS can cause structural defects of lipids, proteins, DNA, and RNA, as well as the functional alteration of several enzymes and cellular structures, leading to an increase in OS and pathogenesis.

We invite you to share your latest original and innovative research findings or review articles in this upcoming Special Issue, “Oxidative-Stress in Human Diseases—3rd Edition”. We welcome clinical and pre-clinical studies on the relationship between OS and human diseases, novel diagnosis methods and mechanisms, as well as approaches for preventing and treating diseases related to OS.

Dr. Soliman Khatib
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at mdpi.longhoe.net 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. Antioxidants is an international peer-reviewed open access monthly 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

  • oxidative stress
  • ROS/RNS
  • human diseases
  • antioxidants
  • OS biomarkers

Published Papers (2 papers)

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Research

13 pages, 1681 KiB  
Article
Trehalose Protects against Superoxide Dismutase 1 Proteinopathy in an Amyotrophic Lateral Sclerosis Model
by Rayne S. S. Magalhães, José R. Monteiro Neto, Gabriela D. Ribeiro, Luan H. Paranhos and Elis C. A. Eleutherio
Antioxidants 2024, 13(7), 807; https://doi.org/10.3390/antiox13070807 - 3 Jul 2024
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Abstract
This work aimed to study the effect of trehalose in protecting cells against Sod1 proteinopathy associated with amyotrophic lateral sclerosis (ALS). Humanized yeast cells in which native Sod1 was replaced by wild-type human Sod1 or an ALS mutant (WT-A4V Sod1 heterodimer) were used [...] Read more.
This work aimed to study the effect of trehalose in protecting cells against Sod1 proteinopathy associated with amyotrophic lateral sclerosis (ALS). Humanized yeast cells in which native Sod1 was replaced by wild-type human Sod1 or an ALS mutant (WT-A4V Sod1 heterodimer) were used as the experimental model. Cells were treated with 10% trehalose (p/v) before or after the appearance of hSod1 proteinopathy induced by oxidative stress. In both conditions, trehalose reduced the number of cells with Sod1 inclusions, increased Sod1 activity, and decreased the levels of intracellular oxidation, demonstrating that trehalose avoids Sod1 misfolding and loss of function in response to oxidative stress. The survival rates of ALS Sod1 cells stressed in the presence of trehalose were 60% higher than in their absence. Treatment with trehalose after the appearance of Sod1 inclusions in cells expressing WT Sod1 doubled longevity; after 5 days, non-treated cells did not survive, but 15% of cells treated with sugar were still alive. Altogether, our results emphasize the potential of trehalose as a novel therapy, which might be applied preventively in ALS patients with a family history of the disease or after diagnosis in ALS patients who discover the disease following the first symptoms. Full article
(This article belongs to the Special Issue Oxidative-Stress in Human Diseases—3rd Edition)
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19 pages, 1487 KiB  
Article
Catalase, Glutathione Peroxidase, and Peroxiredoxin 2 in Erythrocyte Cytosol and Membrane in Hereditary Spherocytosis, Sickle Cell Disease, and β-Thalassemia
by Daniela Melo, Fátima Ferreira, Maria José Teles, Graça Porto, Susana Coimbra, Susana Rocha and Alice Santos-Silva
Antioxidants 2024, 13(6), 629; https://doi.org/10.3390/antiox13060629 - 22 May 2024
Viewed by 639
Abstract
Catalase (CAT), glutathione peroxidase (GPx), and peroxiredoxin 2 (Prx2) can counteract the deleterious effects of oxidative stress (OS). Their binding to the red blood cell (RBC) membrane has been reported in non-immune hemolytic anemias (NIHAs). Our aim was to evaluate the relationships between [...] Read more.
Catalase (CAT), glutathione peroxidase (GPx), and peroxiredoxin 2 (Prx2) can counteract the deleterious effects of oxidative stress (OS). Their binding to the red blood cell (RBC) membrane has been reported in non-immune hemolytic anemias (NIHAs). Our aim was to evaluate the relationships between CAT, GPx, and Prx2, focusing on their role at the RBC membrane, in hereditary spherocytosis (HS), sickle cell disease (SCD), β-thalassemia (β-thal), and healthy individuals. The studies were performed in plasma and in the RBC cytosol and membrane, evaluating OS biomarkers and the enzymatic activities and/or the amounts of CAT, GPx, and Prx2. The binding of the enzymes to the membrane appears to be the primary protective mechanism against oxidative membrane injuries in healthy RBCs. In HS (unsplenectomized) and β-thal, translocation from the cytosol to the membrane of CAT and Prx2, respectively, was observed, probably to counteract lipid peroxidation. RBCs from splenectomized HS patients showed the highest membrane-bound hemoglobin, CAT, and GPx amounts in the membrane. SCD patients presented the lowest amount of enzyme linkage, possibly due to structural changes induced by sickle hemoglobin. The OS-induced changes and antioxidant response were different between the studied NIHAs and may contribute to the different clinical patterns in these patients. Full article
(This article belongs to the Special Issue Oxidative-Stress in Human Diseases—3rd Edition)
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