Reactive Oxygen Species in Different Biological Processes—Second Edition

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "ROS, RNS and RSS".

Deadline for manuscript submissions: 10 December 2024 | Viewed by 22722

Special Issue Editors


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Department of Agricultural Sciences, University of Naples Federico II, Via Università 100, 80055 Portici, Italy
Interests: bioactive compounds; food chemistry; dairy products; milk; analytical methods
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Guest Editor
Institute of Biosciences and BioResources-UOS Naples CNR, Via P. Castellino, 111-80131 Naples, Italy
Interests: oxidative stress; G6PD; antioxidants
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Reactive oxygen species (ROS) have an essential role in maintaining cellular redox homeostasis of any living organisms, from prokaryotes to plants and human beings. Although they are produced during normal metabolism, their enhancement causes oxidative stress that damages cellular structure and affects their functional integrity. Oxidative stress is considered to be a relevant direct or indirect cause in many adverse biological processes such as cancer, diabetes, and many degenerative diseases. For this reason, there is increasing interest amongst scientists and in the biotechnological industry to develop natural or synthetic antioxidants to counteract oxidative stress damage and prevent human disease.

For this Special Issue, we invite you to submit original articles describing your latest research data or review papers highlighting the recent findings in the field.

The second edition of this Special Issue will include both in vitro and in vivo studies clarifying the fundamental role of ROS and their modulation in cell signaling, cell metabolism, epigenetic regulation, development, differentiation, microbiota modulation, diseases, or in other biological process in any living organism. Moreover, it is extended to the identification of natural bioactive molecules (such as polyphenols, pigments, vitamins, microRNA, etc.), isolated from vegetable and animal food matrices, that act as antioxidants in food or that modulate cellular redox homeostasis. New methods to recover natural bioactive compounds from food waste and agricultural by-products will also be considered.

Dr. Fabiana Pizzolongo
Dr. Stefania Filosa
Guest Editors

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Published Papers (6 papers)

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Research

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21 pages, 4475 KiB  
Article
Ergothioneine-Mediated Neuroprotection of Human iPSC-Derived Dopaminergic Neurons
by Damien Meng-Kiat Leow, Irwin Kee-Mun Cheah, Lucrecia Chen, Yang-Kai Ng, Crystal Jing-Jing Yeo, Barry Halliwell and Wei-Yi Ong
Antioxidants 2024, 13(6), 693; https://doi.org/10.3390/antiox13060693 - 5 Jun 2024
Cited by 1 | Viewed by 1716
Abstract
Cell death involving oxidative stress and mitochondrial dysfunction is a major cause of dopaminergic neuronal loss in the substantia nigra (SN) of Parkinson’s disease patients. Ergothioneine (ET), a natural dietary compound, has been shown to have cytoprotective functions, but neuroprotective actions against PD [...] Read more.
Cell death involving oxidative stress and mitochondrial dysfunction is a major cause of dopaminergic neuronal loss in the substantia nigra (SN) of Parkinson’s disease patients. Ergothioneine (ET), a natural dietary compound, has been shown to have cytoprotective functions, but neuroprotective actions against PD have not been well established. 6-Hydroxydopamine (6-OHDA) is a widely used neurotoxin to simulate the degeneration of dopaminergic (DA) neurons in Parkinson’s disease. In this study, we investigated the protective effect of ET on 6-OHDA treated iPSC-derived dopaminergic neurons (iDAs) and further confirmed the protective effects in 6-OHDA-treated human neuroblastoma SH-SY5Y cells. In 6-OHDA-treated cells, decreased mitochondrial membrane potential (ΔΨm), increased mitochondrial reactive oxygen species (mROS), reduced cellular ATP levels, and increased total protein carbonylation levels were observed. 6-OHDA treatment also significantly decreased tyrosine hydroxylase levels. These effects were significantly decreased when ET was present. Verapamil hydrochloride (VHCL), a non-specific inhibitor of the ET transporter OCTN1 abrogated ET’s cytoprotective effects, indicative of an intracellular action. These results suggest that ET could be a potential therapeutic for Parkinson’s disease. Full article
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14 pages, 4653 KiB  
Communication
Redox Regulation of Phosphatase and Tensin Homolog by Bicarbonate and Hydrogen Peroxide: Implication of Peroxymonocarbonate in Cell Signaling
by Vu Hoang Trinh, Jin-Myung Choi, Thang Nguyen Huu, Dhiraj Kumar Sah, Hyun-Joong Yoon, Sang-Chul Park, Yu-Seok Jung, Young-Keun Ahn, Kun-Ho Lee and Seung-Rock Lee
Antioxidants 2024, 13(4), 473; https://doi.org/10.3390/antiox13040473 - 17 Apr 2024
Cited by 1 | Viewed by 1227
Abstract
Phosphatase and tensin homolog (PTEN) is a negative regulator of the phosphoinositide 3-kinases/protein kinase B (PI3K/AKT) signaling pathway. Notably, its active site contains a cysteine residue that is susceptible to oxidation by hydrogen peroxide (H2O2). This oxidation inhibits the [...] Read more.
Phosphatase and tensin homolog (PTEN) is a negative regulator of the phosphoinositide 3-kinases/protein kinase B (PI3K/AKT) signaling pathway. Notably, its active site contains a cysteine residue that is susceptible to oxidation by hydrogen peroxide (H2O2). This oxidation inhibits the phosphatase function of PTEN, critically contributing to the activation of the PI3K/AKT pathway. Upon the stimulation of cell surface receptors, the activity of NADPH oxidase (NOX) generates a transient amount of H2O2, serving as a mediator in this pathway by oxidizing PTEN. The mechanism underlying this oxidation, occurring despite the presence of highly efficient and abundant cellular oxidant-protecting and reducing systems, continues to pose a perplexing conundrum. Here, we demonstrate that the presence of bicarbonate (HCO3) promoted the rate of H2O2-mediated PTEN oxidation, probably through the formation of peroxymonocarbonate (HCO4), and consequently potentiated the phosphorylation of AKT. Acetazolamide (ATZ), a carbonic anhydrase (CA) inhibitor, was shown to diminish the oxidation of PTEN. Thus, CA can also be considered as a modulator in this context. In essence, our findings consolidate the crucial role of HCO3 in the redox regulation of PTEN by H2O2, leading to the presumption that HCO4 is a signaling molecule during cellular physiological processes. Full article
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Review

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16 pages, 1823 KiB  
Review
Redox Regulation of Mitochondrial Potassium Channels Activity
by Joanna Lewandowska, Barbara Kalenik, Antoni Wrzosek and Adam Szewczyk
Antioxidants 2024, 13(4), 434; https://doi.org/10.3390/antiox13040434 - 3 Apr 2024
Cited by 2 | Viewed by 2765
Abstract
Redox reactions exert a profound influence on numerous cellular functions with mitochondria playing a central role in orchestrating these processes. This pivotal involvement arises from three primary factors: (1) the synthesis of reactive oxygen species (ROS) by mitochondria, (2) the presence of a [...] Read more.
Redox reactions exert a profound influence on numerous cellular functions with mitochondria playing a central role in orchestrating these processes. This pivotal involvement arises from three primary factors: (1) the synthesis of reactive oxygen species (ROS) by mitochondria, (2) the presence of a substantial array of redox enzymes such as respiratory chain, and (3) the responsiveness of mitochondria to the cellular redox state. Within the inner mitochondrial membrane, a group of potassium channels, including ATP-regulated, large conductance calcium-activated, and voltage-regulated channels, is present. These channels play a crucial role in conditions such as cytoprotection, ischemia/reperfusion injury, and inflammation. Notably, the activity of mitochondrial potassium channels is intricately governed by redox reactions. Furthermore, the regulatory influence extends to other proteins, such as kinases, which undergo redox modifications. This review aims to offer a comprehensive exploration of the modulation of mitochondrial potassium channels through diverse redox reactions with a specific focus on the involvement of ROS. Full article
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24 pages, 2797 KiB  
Review
Reactive Oxygen Species Signaling and Oxidative Stress: Transcriptional Regulation and Evolution
by Yuhang Hong, Alessandra Boiti, Daniela Vallone and Nicholas S. Foulkes
Antioxidants 2024, 13(3), 312; https://doi.org/10.3390/antiox13030312 - 1 Mar 2024
Cited by 34 | Viewed by 9280
Abstract
Since the evolution of the aerobic metabolism, reactive oxygen species (ROS) have represented significant challenges to diverse life forms. In recent decades, increasing knowledge has revealed a dual role for ROS in cell physiology, showing they serve as a major source of cellular [...] Read more.
Since the evolution of the aerobic metabolism, reactive oxygen species (ROS) have represented significant challenges to diverse life forms. In recent decades, increasing knowledge has revealed a dual role for ROS in cell physiology, showing they serve as a major source of cellular damage while also functioning as important signaling molecules in various biological processes. Our understanding of ROS homeostasis and ROS-mediated cellular signaling pathways has presumed that they are ancient and highly conserved mechanisms shared by most organisms. However, emerging evidence highlights the complexity and plasticity of ROS signaling, particularly in animals that have evolved in extreme environments. In this review, we focus on ROS generation, antioxidative systems and the main signaling pathways that are influenced by ROS. In addition, we discuss ROS’s responsive transcription regulation and how it may have been shaped over the course of evolution. Full article
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93 pages, 5460 KiB  
Review
NADPH Oxidase 3: Beyond the Inner Ear
by Marc Herb
Antioxidants 2024, 13(2), 219; https://doi.org/10.3390/antiox13020219 - 8 Feb 2024
Viewed by 4684
Abstract
Reactive oxygen species (ROS) were formerly known as mere byproducts of metabolism with damaging effects on cellular structures. The discovery and description of NADPH oxidases (Nox) as a whole enzyme family that only produce this harmful group of molecules was surprising. After intensive [...] Read more.
Reactive oxygen species (ROS) were formerly known as mere byproducts of metabolism with damaging effects on cellular structures. The discovery and description of NADPH oxidases (Nox) as a whole enzyme family that only produce this harmful group of molecules was surprising. After intensive research, seven Nox isoforms were discovered, described and extensively studied. Among them, the NADPH oxidase 3 is the perhaps most underrated Nox isoform, since it was firstly discovered in the inner ear. This stigma of Nox3 as “being only expressed in the inner ear” was also used by me several times. Therefore, the question arose whether this sentence is still valid or even usable. To this end, this review solely focuses on Nox3 and summarizes its discovery, the structural components, the activating and regulating factors, the expression in cells, tissues and organs, as well as the beneficial and detrimental effects of Nox3-mediated ROS production on body functions. Furthermore, the involvement of Nox3-derived ROS in diseases progression and, accordingly, as a potential target for disease treatment, will be discussed. Full article
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17 pages, 5453 KiB  
Review
Redox Regulation of PTEN by Reactive Oxygen Species: Its Role in Physiological Processes
by Vu Hoang Trinh, Thang Nguyen Huu, Dhiraj Kumar Sah, Jin Myung Choi, Hyun Joong Yoon, Sang Chul Park, Yu Seok Jung and Seung-Rock Lee
Antioxidants 2024, 13(2), 199; https://doi.org/10.3390/antiox13020199 - 4 Feb 2024
Cited by 2 | Viewed by 2031
Abstract
Phosphatase and tensin homolog (PTEN) is a tumor suppressor due to its ability to regulate cell survival, growth, and proliferation by downregulating the PI3K/AKT signaling pathway. In addition, PTEN plays an essential role in other physiological events associated with cell growth demands, such [...] Read more.
Phosphatase and tensin homolog (PTEN) is a tumor suppressor due to its ability to regulate cell survival, growth, and proliferation by downregulating the PI3K/AKT signaling pathway. In addition, PTEN plays an essential role in other physiological events associated with cell growth demands, such as ischemia-reperfusion, nerve injury, and immune responsiveness. Therefore, recently, PTEN inhibition has emerged as a potential therapeutic intervention in these situations. Increasing evidence demonstrates that reactive oxygen species (ROS), especially hydrogen peroxide (H2O2), are produced and required for the signaling in many important cellular processes under such physiological conditions. ROS have been shown to oxidize PTEN at the cysteine residue of its active site, consequently inhibiting its function. Herein, we provide an overview of studies that highlight the role of the oxidative inhibition of PTEN in physiological processes. Full article
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