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Antioxidants
Special Issues
Redox Language of the Cell
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Redox Language of the Cell

A special issue of Antioxidants (ISSN 2076-3921).

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 21578

Special Issue Editors

Prof. Dr. Joris Messens

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Guest Editor
Brussels Center for Redox Biology, VIB-VUB Center for Structural Biology, Vrije Universiteit Brussel, Brussels, Belgium
Interests: redox biochemistry; subcellular communication; architecture of peroxide signaling; biosensor design
Dr. Daria Ezeriņa

E-Mail Website
Guest Editor
Brussels Center for Redox Biology, VIB Center for Structural Biology, Vrije Universiteit Brussel, Brussels, Belgium
Interests: redox biology; sulphur biochemistry; fluorescence-based biosensors; metabolism
Dr. Jesalyn Bolduc

E-Mail Website
Guest Editor
Brussels Center for Redox Biology, VIB Center for Structural Biology, Vrije Universiteit Brussel, Brussels, Belgium
Interests: redox biology; cell signaling; peroxiredoxins; structural biology

Special Issue Information

Dear Colleagues,

Every language has an alphabet, and the redox language of the cell is no exception. The letters of this alphabet are oxidants, such as H2O2, H2S, and HOCl, and reductants, like NADH and NADPH. The mitochondria, endoplasmic reticulum, and lysosomes use this alphabet to form and exchange messages that control proteostatic processes, including biogenesis, protein folding, trafficking, and degradation. The nucleus also speaks this language, and upon relay of redox input, adapts transcription in order to translate the received messages to appropriate cellular responses. Redox miscommunication, on the other hand, has been shown to be involved in several pathological processes, including the development of cancer and neurodegenerative diseases, as well as ageing. New biochemical insights, including the elucidation of the proteins involved in redox signaling and their mechanisms, have led to a more thorough, yet still incomplete, understanding of the redox language. Further elucidation of the oxidative and reductive “letters” of the redox alphabet, their intracellular metabolism, trafficking, and the proteins involved in their signaling will open new chapters in the development of redox therapeutics for human diseases. Our objectives for this Special Issue of Antioxidants are to highlight the recent developments in methodological tools and reagents that enable us to monitor cellular redox events, including their contribution to the exciting conceptual advances in our understanding of the cellular redox lexicon in the context of cell biology, physiological processes, life span, disease pathogenesis, and signalling.

Prof. Joris Messens
Dr. Daria Ezeriņa
Dr. Jesalyn Bolduc
Guest Editors

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Published Papers (4 papers)

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Research

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25 pages, 5340 KiB  
Article
Prdx1 Interacts with ASK1 upon Exposure to H2O2 and Independently of a Scaffolding Protein
by Trung Nghia Vo, Julia Malo Pueyo, Khadija Wahni, Daria Ezeriņa, Jesalyn Bolduc and Joris Messens
Antioxidants 2021, 10(7), 1060; https://doi.org/10.3390/antiox10071060 - 30 Jun 2021
Cited by 10 | Viewed by 4941
Abstract
Hydrogen peroxide (H2O2) is a key redox signaling molecule that selectively oxidizes cysteines on proteins. It can accomplish this even in the presence of highly efficient and abundant H2O2 scavengers, peroxiredoxins (Prdxs), as it is the [...] Read more.
Hydrogen peroxide (H2O2) is a key redox signaling molecule that selectively oxidizes cysteines on proteins. It can accomplish this even in the presence of highly efficient and abundant H2O2 scavengers, peroxiredoxins (Prdxs), as it is the Prdxs themselves that transfer oxidative equivalents to specific protein thiols on target proteins via their redox-relay functionality. The first evidence of a mammalian cytosolic Prdx-mediated redox-relay—Prdx1 with the kinase ASK1—was presented a decade ago based on the outcome of a co-immunoprecipitation experiment. A second such redox-relay—Prdx2:STAT3—soon followed, for which further studies provided insights into its specificity, organization, and mechanism. The Prdx1:ASK1 redox-relay, however, has never undergone such a characterization. Here, we combine cellular and in vitro protein–protein interaction methods to investigate the Prdx1:ASK1 interaction more thoroughly. We show that, contrary to the Prdx2:STAT3 redox-relay, Prdx1 interacts with ASK1 at elevated H2O2 concentrations, and that this interaction can happen independently of a scaffolding protein. We also provide evidence of a Prdx2:ASK1 interaction, and demonstrate that it requires a facilitator that, however, is not annexin A2. Our results reveal that cytosolic Prdx redox-relays can be organized in different ways and yet again highlight the differentiated roles of Prdx1 and Prdx2. Full article
(This article belongs to the Special Issue Redox Language of the Cell)
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18 pages, 2838 KiB  
Article
Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State
by Tom E. Forshaw, Julie A. Reisz, Kimberly J. Nelson, Rajesh Gumpena, J. Reed Lawson, Thomas J. Jönsson, Hanzhi Wu, Jill E. Clodfelter, Lynnette C. Johnson, Cristina M. Furdui and W. Todd Lowther
Antioxidants 2021, 10(6), 946; https://doi.org/10.3390/antiox10060946 - 11 Jun 2021
Cited by 12 | Viewed by 3353
Abstract
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decamers and disulfide-linked dimers, [...] Read more.
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decamers and disulfide-linked dimers, with the hyperoxidized inactive state (-SO2H) favoring the multimeric structure of the reduced enzyme. Here, we present a study on the structural requirements for the repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx) and the relative efficacy of physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) in this reaction. The crystal structure of the toroidal Prx1-Srx complex shows an extended active site interface. The loss of this interface within engineered Prx2 and Prx3 dimers yielded variants more resistant to hyperoxidation and repair by Srx. Finally, we reveal for the first time Prx isoform-dependent use of and potential cooperation between GSH and H2S in supporting Srx activity. Full article
(This article belongs to the Special Issue Redox Language of the Cell)
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Review

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22 pages, 1485 KiB  
Review
The Writers, Readers, and Erasers in Redox Regulation of GAPDH
by Maria-Armineh Tossounian, Bruce Zhang and Ivan Gout
Antioxidants 2020, 9(12), 1288; https://doi.org/10.3390/antiox9121288 - 16 Dec 2020
Cited by 45 | Viewed by 6047
Abstract
Glyceraldehyde 3–phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme, which is crucial for the breakdown of glucose to provide cellular energy. Over the past decade, GAPDH has been reported to be one of the most prominent cellular targets of post-translational modifications (PTMs), which [...] Read more.
Glyceraldehyde 3–phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme, which is crucial for the breakdown of glucose to provide cellular energy. Over the past decade, GAPDH has been reported to be one of the most prominent cellular targets of post-translational modifications (PTMs), which divert GAPDH toward different non-glycolytic functions. Hence, it is termed a moonlighting protein. During metabolic and oxidative stress, GAPDH is a target of different oxidative PTMs (oxPTM), e.g., sulfenylation, S-thiolation, nitrosylation, and sulfhydration. These modifications alter the enzyme’s conformation, subcellular localization, and regulatory interactions with downstream partners, which impact its glycolytic and non-glycolytic functions. In this review, we discuss the redox regulation of GAPDH by different redox writers, which introduce the oxPTM code on GAPDH to instruct a redox response; the GAPDH readers, which decipher the oxPTM code through regulatory interactions and coordinate cellular response via the formation of multi-enzyme signaling complexes; and the redox erasers, which are the reducing systems that regenerate the GAPDH catalytic activity. Human pathologies associated with the oxidation-induced dysregulation of GAPDH are also discussed, featuring the importance of the redox regulation of GAPDH in neurodegeneration and metabolic disorders. Full article
(This article belongs to the Special Issue Redox Language of the Cell)
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39 pages, 7431 KiB  
Review
Looking Back at the Early Stages of Redox Biology
by Leopold Flohé
Antioxidants 2020, 9(12), 1254; https://doi.org/10.3390/antiox9121254 - 9 Dec 2020
Cited by 49 | Viewed by 6075
Abstract
The beginnings of redox biology are recalled with special emphasis on formation, metabolism and function of reactive oxygen and nitrogen species in mammalian systems. The review covers the early history of heme peroxidases and the metabolism of hydrogen peroxide, the discovery of selenium [...] Read more.
The beginnings of redox biology are recalled with special emphasis on formation, metabolism and function of reactive oxygen and nitrogen species in mammalian systems. The review covers the early history of heme peroxidases and the metabolism of hydrogen peroxide, the discovery of selenium as integral part of glutathione peroxidases, which expanded the scope of the field to other hydroperoxides including lipid hydroperoxides, the discovery of superoxide dismutases and superoxide radicals in biological systems and their role in host defense, tissue damage, metabolic regulation and signaling, the identification of the endothelial-derived relaxing factor as the nitrogen monoxide radical (more commonly named nitric oxide) and its physiological and pathological implications. The article highlights the perception of hydrogen peroxide and other hydroperoxides as signaling molecules, which marks the beginning of the flourishing fields of redox regulation and redox signaling. Final comments describe the development of the redox language. In the 18th and 19th century, it was highly individualized and hard to translate into modern terminology. In the 20th century, the redox language co-developed with the chemical terminology and became clearer. More recently, the introduction and inflationary use of poorly defined terms has unfortunately impaired the understanding of redox events in biological systems. Full article
(This article belongs to the Special Issue Redox Language of the Cell)
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