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Antioxidants
Special Issues
Superoxide Dismutase in Health and Disease
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Superoxide Dismutase in Health and Disease

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Antioxidant Enzyme Systems".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 26873

Special Issue Editor

Dr. Ehab H Sarsour

E-Mail Website
Guest Editor
College of Osteopathic Medicine, Kansas City University, Kansas City, MI, USA
Interests: aging; cancer; cell cycle; tumor microenvironment; radiation biology; redox biology; antioxidants

Special Issue Information

Dear Colleagues,

Superoxide is one of the main reactive oxygen species produced by living cells, most eukaryotic organisms require oxygen to survive. Eukaryotic cells evolved defense mechanisms against superoxide, which is known as the superoxide dismutase (SOD) system. Three enzymes make up the superoxide dismutase system in mammalian cells, they all the same function in which to convert superoxide to hydrogen peroxide and oxygen, but they differ in location and molecular structure. There are two Copper zinc containing superoxide dismutases and one Manganese containing superoxide dismutase. The first Copper zinc superoxide dismutase (CuZnSOD or SOD1) located in the cytoplasm, nucleus and intermembrane space of mitochondria, the other Copper zinc containing superoxide dismutase is the Extracellular superoxide dismutase (EcSOD or SOD3). Manganese superoxide dismutase (MnSOD or SOD2) is in the mitochondrial matrix. The importance and uniqueness of each of the SOD enzymes comes from their diverse locations outside and within the cell, which give the cells the ability of cells to response to the changes of the extra and intracellular environments, that ensure cells health, homeostasis, and survival which ultimately reflect on the health of tissue and the organism. Impairment of any of these SODs mostly lead to cellular damage, malfunction, and death, which lead to development of disease. Changes in SODs expression and activity have been linked to many diseases including aging, cancer, cardiovascular, and neurodegenerative diseases. For example, Drs Larry Oberley and Gary Buettner suggested SOD2 as tumor suppressor gene due to diminished levels of antioxidant enzymes including SOD2 in cancer cells. Mutations found in the SOD1 gene such as D90A, A4V and G93A have been linked to the development of the neurodegenerative disorder Amyotrophic lateral sclerosis. Changes in SOD3 expression and activity has been linked to many cardiovascular disease conditions such as atherosclerosis, hypertension, and ischemia reperfusion injury. While many effects of SODs on health and disease have been establish there are always new discoveries, concepts and innovation that are introduced everyday highlighting the importance of these primary antioxidant enzymes.

This Special Issue of “Superoxide dismutase in health and disease” is seeking quality original research papers and reviews that introduces new discoveries and broaden our understanding to the role of SODs in health and disease on the cellular and molecular level, and the application of this knowledge in preserving health and treating disease. The subjects of the research can include any of the SOD enzymes and the emerging field of SOD mimics.  We welcome research papers that introduce new discoveries and concepts or expand on the current knowledge and research with new insights and approaches.

Dr. Ehab H Sarsour
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. 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

  • Aging
  • Neurodegeneration
  • Cardiovascular
  • Superoxide dismutase
  • Cancer
  • Metabolism
  • Oxidative stress
  • Superoxide dismutase mimics
  • reactive oxygen species
  • Antioxidants

Published Papers (7 papers)

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Research

Jump to: Review, Other

17 pages, 6127 KiB  
Article
Transplantation of Human Glial Progenitors to Immunodeficient Neonatal Mice with Amyotrophic Lateral Sclerosis (SOD1/rag2)
by Luiza Stanaszek, Piotr Rogujski, Katarzyna Drela, Michal Fiedorowicz, Piotr Walczak, Barbara Lukomska and Miroslaw Janowski
Antioxidants 2022, 11(6), 1050; https://doi.org/10.3390/antiox11061050 - 26 May 2022
Cited by 2 | Viewed by 1801
Abstract
Amyotrophic lateral sclerosis (ALS) is a progressive, fatal disease with no effective therapy. The neurodegenerative character of ALS was an appealing target for stem cell-based regenerative approaches. Different types of stem cells have been transplanted in both preclinical and clinical settings, but no [...] Read more.
Amyotrophic lateral sclerosis (ALS) is a progressive, fatal disease with no effective therapy. The neurodegenerative character of ALS was an appealing target for stem cell-based regenerative approaches. Different types of stem cells have been transplanted in both preclinical and clinical settings, but no convincing outcomes have been noted. Human glial restricted precursors (hGRPs) transplanted intraventricularly to neonatal, immunodeficient mice rescued lifespan of dysmyelinated mice. Intraspinal injection of hGRPs also provided benefits in the mouse model of ALS. Therefore, we have recently developed an immunodeficient model of ALS (double mutant SOD1/rag2), and, in this study, we tested the strategy previously used in dysmyelinated mice of intraventricular transplantation of hGRPs to immunodeficient mice. To maximize potential therapeutic benefits, the cells were implanted into neonates. We used magnetic resonance imaging to investigate the progression of neurodegeneration and therapeutic responses. A cohort of animals was devoted to survival assessment. Postmortem analysis included immunohistochemistry, Nissl staining, and Western blots. Cell transplantation was not associated with improved animal survival, slowing neurodegeneration, or accumulation of misfolded superoxide dismutase 1. Postmortem analysis did not reveal any surviving hGRPs. Grafting into neonatal immunodeficient recipients did not prevent ALS-induced cell loss, which might explain the lack of positive therapeutic effects. The results of this study are in line with the modest effects of clinical neurotransplantations. Therefore, we urge stem cell and ALS communities to develop and implement cell tracking methods to better understand cell fates in the clinic. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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19 pages, 3703 KiB  
Article
Characterization of the p.L145F and p.S135N Mutations in SOD1: Impact on the Metabolism of Fibroblasts Derived from Amyotrophic Lateral Sclerosis Patients
by Elisa Perciballi, Federica Bovio, Jessica Rosati, Federica Arrigoni, Angela D’Anzi, Serena Lattante, Maurizio Gelati, Fabiola De Marchi, Ivan Lombardi, Giorgia Ruotolo, Matilde Forcella, Letizia Mazzini, Sandra D’Alfonso, Lucia Corrado, Mario Sabatelli, Amelia Conte, Luca De Gioia, Sabata Martino, Angelo Luigi Vescovi, Paola Fusi and Daniela Ferrariadd Show full author list remove Hide full author list
Antioxidants 2022, 11(5), 815; https://doi.org/10.3390/antiox11050815 - 22 Apr 2022
Cited by 3 | Viewed by 2632
Abstract
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the loss of the upper and lower motor neurons (MNs). About 10% of patients have a family history (familial, fALS); however, most patients seem to develop the sporadic form of the disease [...] Read more.
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the loss of the upper and lower motor neurons (MNs). About 10% of patients have a family history (familial, fALS); however, most patients seem to develop the sporadic form of the disease (sALS). SOD1 (Cu/Zn superoxide dismutase-1) is the first studied gene among the ones related to ALS. Mutant SOD1 can adopt multiple misfolded conformation, lose the correct coordination of metal binding, decrease structural stability, and form aggregates. For all these reasons, it is complicated to characterize the conformational alterations of the ALS-associated mutant SOD1, and how they relate to toxicity. In this work, we performed a multilayered study on fibroblasts derived from two ALS patients, namely SOD1L145F and SOD1S135N, carrying the p.L145F and the p.S135N missense variants, respectively. The patients showed diverse symptoms and disease progression in accordance with our bioinformatic analysis, which predicted the different effects of the two mutations in terms of protein structure. Interestingly, both mutations had an effect on the fibroblast energy metabolisms. However, while the SOD1L145F fibroblasts still relied more on oxidative phosphorylation, the SOD1S135N fibroblasts showed a metabolic shift toward glycolysis. Our study suggests that SOD1 mutations might lead to alterations in the energy metabolism. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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Review

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24 pages, 1759 KiB  
Review
SOD1 in ALS: Taking Stock in Pathogenic Mechanisms and the Role of Glial and Muscle Cells
by Caterina Peggion, Valeria Scalcon, Maria Lina Massimino, Kelly Nies, Raffaele Lopreiato, Maria Pia Rigobello and Alessandro Bertoli
Antioxidants 2022, 11(4), 614; https://doi.org/10.3390/antiox11040614 - 23 Mar 2022
Cited by 25 | Viewed by 5234
Abstract
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by the loss of motor neurons in the brain and spinal cord. While the exact causes of ALS are still unclear, the discovery that familial cases of ALS are related to mutations in [...] Read more.
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by the loss of motor neurons in the brain and spinal cord. While the exact causes of ALS are still unclear, the discovery that familial cases of ALS are related to mutations in the Cu/Zn superoxide dismutase (SOD1), a key antioxidant enzyme protecting cells from the deleterious effects of superoxide radicals, suggested that alterations in SOD1 functionality and/or aberrant SOD1 aggregation strongly contribute to ALS pathogenesis. A new scenario was opened in which, thanks to the generation of SOD1 related models, different mechanisms crucial for ALS progression were identified. These include excitotoxicity, oxidative stress, mitochondrial dysfunctions, and non-cell autonomous toxicity, also implicating altered Ca2+ metabolism. While most of the literature considers motor neurons as primary target of SOD1-mediated effects, here we mainly discuss the effects of SOD1 mutations in non-neuronal cells, such as glial and skeletal muscle cells, in ALS. Attention is given to the altered redox balance and Ca2+ homeostasis, two processes that are strictly related with each other. We also provide original data obtained in primary myocytes derived from hSOD1(G93A) transgenic mice, showing perturbed expression of Ca2+ transporters that may be responsible for altered mitochondrial Ca2+ fluxes. ALS-related SOD1 mutants are also responsible for early alterations of fundamental biological processes in skeletal myocytes that may impinge on skeletal muscle functions and the cross-talk between muscle cells and motor neurons during disease progression. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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10 pages, 1406 KiB  
Review
Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
by Joyce Xu, Xiaoyang Su, Stephen K. Burley and X. F. Steven Zheng
Antioxidants 2022, 11(2), 427; https://doi.org/10.3390/antiox11020427 - 21 Feb 2022
Cited by 14 | Viewed by 7352
Abstract
SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. It is well known as an essential antioxidant enzyme for maintaining cellular redox homeostasis. SOD1 dysregulation has been associated with many diseases, including amyotrophic lateral [...] Read more.
SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. It is well known as an essential antioxidant enzyme for maintaining cellular redox homeostasis. SOD1 dysregulation has been associated with many diseases, including amyotrophic lateral sclerosis (ALS), cancer, accelerated aging, and age-related diseases. Recent studies also revealed that SOD1 can serve as a regulatory protein in cell signaling, transcription, and ribosome biogenesis. Notably, SOD1 is localized in the nucleus under both normal and pathological conditions, contributing to oxidative stress response and growth control. Moreover, increasing evidence points to the importance of nuclear SOD1 in the pathogenesis of ALS and cancer. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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18 pages, 1335 KiB  
Review
Superoxide Dismutases in Eukaryotic Microorganisms: Four Case Studies
by Alvaro de Obeso Fernandez del Valle and Christian Quintus Scheckhuber
Antioxidants 2022, 11(2), 188; https://doi.org/10.3390/antiox11020188 - 19 Jan 2022
Cited by 9 | Viewed by 2563
Abstract
Various components in the cell are responsible for maintaining physiological levels of reactive oxygen species (ROS). Several different enzymes exist that can convert or degrade ROS; among them are the superoxide dismutases (SODs). If left unchecked, ROS can cause damage that leads to [...] Read more.
Various components in the cell are responsible for maintaining physiological levels of reactive oxygen species (ROS). Several different enzymes exist that can convert or degrade ROS; among them are the superoxide dismutases (SODs). If left unchecked, ROS can cause damage that leads to pathology, can contribute to aging, and may, ultimately, cause death. SODs are responsible for converting superoxide anions to hydrogen peroxide by dismutation. Here we review the role of different SODs on the development and pathogenicity of various eukaryotic microorganisms relevant to human health. These include the fungal aging model, Podospora anserina; various members of the genus Aspergillus that can potentially cause aspergillosis; the agents of diseases such as Chagas and sleeping disease, Trypanosoma cruzi and Trypanosoma brucei, respectively; and, finally, pathogenic amoebae, such as Acanthamoeba spp. In these organisms, SODs fulfill essential and often regulatory functions that come into play during processes such as the development, host infection, propagation, and control of gene expression. We explore the contribution of SODs and their related factors in these microorganisms, which have an established role in health and disease. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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16 pages, 2152 KiB  
Review
Impact of EcSOD Perturbations in Cancer Progression
by Brianne R. O’Leary, Rory S. Carroll, Garett J. Steers, Jennifer Hrabe, Frederick E. Domann and Joseph J. Cullen
Antioxidants 2021, 10(8), 1219; https://doi.org/10.3390/antiox10081219 - 29 Jul 2021
Cited by 5 | Viewed by 2320
Abstract
Reactive oxygen species (ROS) are a normal byproduct of cellular metabolism and are required components in cell signaling and immune responses. However, an imbalance of ROS can lead to oxidative stress in various pathological states. Increases in oxidative stress are one of the [...] Read more.
Reactive oxygen species (ROS) are a normal byproduct of cellular metabolism and are required components in cell signaling and immune responses. However, an imbalance of ROS can lead to oxidative stress in various pathological states. Increases in oxidative stress are one of the hallmarks in cancer cells, which display an altered metabolism when compared to corresponding normal cells. Extracellular superoxide dismutase (EcSOD) is an antioxidant enzyme that catalyzes the dismutation of superoxide anion (O2−) in the extracellular environment. By doing so, this enzyme provides the cell with a defense against oxidative damage by contributing to redox balance. Interestingly, EcSOD expression has been found to be decreased in a variety of cancers, and this loss of expression may contribute to the development and progression of malignancies. In addition, recent compounds can increase EcSOD activity and expression, which has the potential for altering this redox signaling and cellular proliferation. This review will explore the role that EcSOD expression plays in cancer in order to better understand its potential as a tool for the detection, predicted outcomes and potential treatment of malignancies. Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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Other

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16 pages, 5892 KiB  
Systematic Review
A Systematic Review and Meta-Analysis of the Effect of Statins on Glutathione Peroxidase, Superoxide Dismutase, and Catalase
by Angelo Zinellu and Arduino A. Mangoni
Antioxidants 2021, 10(11), 1841; https://doi.org/10.3390/antiox10111841 - 19 Nov 2021
Cited by 16 | Viewed by 2617
Abstract
Statins may exert protective effects against oxidative stress by upregulating specific antioxidant mechanisms. We conducted a systematic review and meta-analysis of the effect of statins on three key antioxidant enzymes: glutathione peroxidase (GPx), superoxide dismutase (SOD), and catalase. The electronic databases PubMed, Web [...] Read more.
Statins may exert protective effects against oxidative stress by upregulating specific antioxidant mechanisms. We conducted a systematic review and meta-analysis of the effect of statins on three key antioxidant enzymes: glutathione peroxidase (GPx), superoxide dismutase (SOD), and catalase. The electronic databases PubMed, Web of Science, and Scopus were searched from inception to July 2021. The risk of bias was assessed with the Joanna Briggs Institute Critical Appraisal Checklist and certainty of evidence was assessed using the GRADE framework. In 15 studies, reporting 17 treatment arms in 773 patients (mean age 53 years, 54% males), statins significantly increased the concentrations of both GPx (standardized mean difference, SMD = 0.80, 95% confidence interval, CI 0.13 to 1.46, p = 0.018; high certainty of evidence) and SOD (SMD = 1.54, 95% CI 0.71 to 2.36, p < 0.001; high certainty of evidence), but not catalase (SMD = −0.16, 95% CI −0.51 to 0.20, p = 0.394; very low certainty of evidence). The pooled SMD values were not altered in sensitivity analysis. There was no publication bias. In conclusion, statin treatment significantly increases the circulating concentrations of GPx and SOD, suggesting an antioxidant effect of these agents (PROSPERO registration number: CRD42021271589). Full article
(This article belongs to the Special Issue Superoxide Dismutase in Health and Disease)
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