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Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells

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

Deadline for manuscript submissions: closed (31 January 2025) | Viewed by 13781

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Dr. Marcel Zamocky

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1. Laboratory of Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21, SK-84551 Bratislava, Slovakia
2. Department of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, 1190 Wien, Austria
Interests: molecular phylogeny analysis; peroxidases; catalases; phylogenetic analysis; reactive oxygen species; oxidative stress
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Special Issue Information

Dear colleagues,

You are invited to submit your original work and reviews for a new issue of Antioxidants (MDPI), titled “Oxidative stress in various forms and efficient antioxidant pathways in prokaryotic and eukaryotic cells”. The focus of this broadly formulated issue is to present an up-to-date overview of the advances in the discovery of various kinds of reactive species causing oxidative stress. In addition reactive oxygen species, which are already quite well known as “two-faced“ molecules that also have a signaling function, attention must also be paid to reactive nitrogen and reactive sulphur species that are much less investigated but may play important roles in various signaling pathways. One principal aspect is doubtless the mechanism of cellular defence against various forms of oxidative stress. From this perspective, a direct comparison between the behaviour of prokaryotic and eukaryotic cells can give important insight into future directions of exciting molecular research. Furthermore, important updates on the main groups of antioxidant enzymes are welcomed in this collection.

Dr. Marcel Zamocky
Guest Editor

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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.

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Keywords

reactive oxygen species
reactive nitrogen species
reactive sulfur species
antioxidant and prooxidant pathways
signaling molecules
diversity of catalases
diversity of peroxidases
diversity of superoxide dismutases

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Published Papers (7 papers)

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Research

23 pages, 4545 KiB

Open AccessArticle

The Manifestation of the Dual ROS-Processing and Redox Signaling Roles of Glutathione Peroxidase-like Enzymes in Development of Arabidopsis Seedlings

by Krisztina Bela, Bernát Tompa, Riyazuddin Riyazuddin, Edit Horváth, Krisztián Jász, Ádám Hajnal, Sajid Ali Khan Bangash, Ágnes Gallé and Jolán Csiszár

Antioxidants 2025, 14(5), 518; https://doi.org/10.3390/antiox14050518 - 25 Apr 2025

Viewed by 177

Abstract

Plant glutathione peroxidase-like (GPXL) enzymes are thiol-based peroxidases that reduce H₂O₂ or hydroperoxides to water or alcohols using electrons principally from thioredoxin. Arabidopsis thaliana possesses eight isoenzymes (AtGPXL1−8) located in different plant organelles and have various roles in redox-dependent processes. The determination of the redox potential of 6-day-old T-DNA insertional mutants (Atgpxl1–Atgpxl8) using a cytosolic redox-sensitive fluorescent probe (roGFP2) uncovered more oxidized redox status in the shoot and/or root of the untreated mutants, except for Atgpxl5. To investigate the involvement of AtGPXLs in the growth and abiotic stress responses of seedlings, the 4-day-old Atgpxls were exposed to salt and osmotic stresses for two weeks. The evaluation of the reactive oxygen species (ROS) levels of untreated 18-day-old plants using fluorescent microscopy revealed the elevated accumulation of total ROS in the shoots and, in some cases, the roots of the mutants. Regarding the growth of roots, both the length of primary roots and/or the number of lateral roots were affected by the mutation of AtGPXLs. A strong negative correlation was observed between the ROS level of wild type shoots and the development of lateral roots, but it was altered in mutants, while in the case of Atgpxl1, Atgpxl5, and Atgpxl7 seedlings, it disappeared; in other mutants (Atgpxl4, Atgpxl6, and Atgpxl8), the correlation became stronger. Our analysis underpins the discrete role of AtGPXL enzymes in controlling the growth and development of plants by fine tuning the ROS contents and redox status in an organ-specific way. Differences in root phenotype and metabolic activity between Atgpxl mutants and wild type plants highlight the essential role of AtGPXLs in ROS processing to support growth, which is particularly evident when one GPXL isoenzyme is absent or its activity is reduced, both under normal and abiotic stress conditions. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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19 pages, 5160 KiB

Open AccessArticle

First Characterization of a Cyanobacterial Xi-Class Glutathione S-Transferase in Synechocystis PCC 6803

by Fanny Marceau, Marlène Lamothe-Sibold, Sandrine Farci, Soufian Ouchane, Corinne Cassier-Chauvat and Franck Chauvat

Antioxidants 2024, 13(12), 1577; https://doi.org/10.3390/antiox13121577 - 20 Dec 2024

Viewed by 860

Abstract

Glutathione S-transferases (GSTs) are evolutionarily conserved enzymes crucial for cell detoxication. They are viewed as having evolved in cyanobacteria, the ancient photosynthetic prokaryotes that colonize our planet and play a crucial role for its biosphere. Xi-class GSTs, characterized by their specific glutathionyl–hydroquinone reductase activity, have been observed in prokaryotes, fungi and plants, but have not yet been studied in cyanobacteria. In this study, we have analyzed the presumptive Xi-class GST, designated as Slr0605, of the unicellular model cyanobacterium Synechocystis PCC 6803. We report that Slr0605 is a homodimeric protein that has genuine glutathionyl–hydroquinone reductase activity. Though Slr0605 is not essential for cell growth under standard photoautotrophic conditions, it plays a prominent role in the protection against not only benzoquinone, but also cobalt-excess stress. Indeed, Slr0605 acts in defense against the cobalt-elicited disturbances of iron homeostasis, iron–sulfur cluster repair, catalase activity and the level of reactive oxygen species, which are all crucial for cell life. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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13 pages, 3893 KiB

Open AccessArticle

Glutathione S-Transferase Genes Involved in Response to Short-Term Heat Stress in Tetranychus urticae (Koch)

by Tong Zhu, Bin Wei, Yue Wang and Suqin Shang

Antioxidants 2024, 13(4), 442; https://doi.org/10.3390/antiox13040442 - 8 Apr 2024

Cited by 1 | Viewed by 1738

Abstract

Tetranychus urticae, a globally ubiquitous mite, poses a significant threat to agriculture. Elevated temperatures exacerbate the growth, development, and reproduction of T. urticae, leading to substantial crop damage. In this study, we employed comparative transcriptomic approaches with whole-genome information of T. urticae to identify six Glutathione S-transferase genes (GSTs) implicated in heat stress response. Through comprehensive bioinformatics analyses, we elucidated the tertiary structure and active sites of the corresponding proteins, providing a thorough characterization of these GST genes. Furthermore, we investigated the expression patterns of these six GST genes under short-term heat shock conditions. Our findings unveiled the involvement of T. urticae GST genes in combating oxidative stress induced by heat, underscoring their role in antioxidant defense mechanisms. This study contributes valuable insights into the molecular mechanisms underlying the response of T. urticae to heat stress, laying a foundation for the development of strategies aimed at mitigating its impact in high-temperature environments. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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21 pages, 4627 KiB

Open AccessArticle

Novel Roles of the Greatwall Kinase Rim15 in Yeast Oxidative Stress Tolerance through Mediating Antioxidant Systems and Transcriptional Regulation

by Xue-Qing Wang, Bing Yuan, Feng-Li Zhang, Chen-Guang Liu, Choowong Auesukaree and Xin-Qing Zhao

Antioxidants 2024, 13(3), 260; https://doi.org/10.3390/antiox13030260 - 21 Feb 2024

Cited by 4 | Viewed by 2123

Abstract

The Greatwall-family protein kinase Rim15 is associated with the nutrient starvation response, whereas its role in oxidative stress responses remains unclear. Here, acetic acid and peroxide were used as two oxidative stress elicitors. The antioxidant indicator assay under acetic acid stress revealed the impaired growth in rim15Δ related to the regulation of antioxidant systems. Comparative transcriptome analysis revealed that differentially expressed genes (DEGs) are predicted to be mostly regulated by oxidative stress-responsive transcriptional factor Yap1. Among the DEGs, acetic acid stress-induced genes were found, and YAP1 disruption also inhibited their induction. The deletion of Rim15 or the Rim15 kinase domain in yap1Δ did not further decrease the gene expression, suggesting that Rim15 functions together with Yap1 in regulating acetic acid stress-induced genes, which requires Rim15 kinase activity. Additionally, Rim15 regulated H₂O₂ stress tolerance through partially similar but special mechanisms in that Rim15 kinase activity impacted acetic acid and H₂O₂ stress tolerance in different degrees, indicating the different mechanisms underlying Rim15-mediated redox regulation against different stressors. These results benefit the better understanding of stress signaling pathways related to Rim15. Given that Rim15 and some of its target genes are conserved across eukaryotes, these results also provide a basis for studies of oxidative stress-related processes in other organisms. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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14 pages, 4780 KiB

Open AccessArticle

Selection, Identification, and Transcript Expression Analysis of Antioxidant Enzyme Genes in Neoseiulus barkeri after Short-Term Heat Stress

by Tong Zhu, Weizhen Li, He Xue, Shibo Dong, Jianhui Wang, Suqin Shang and Youssef Dewer

Antioxidants 2023, 12(11), 1998; https://doi.org/10.3390/antiox12111998 - 13 Nov 2023

Cited by 5 | Viewed by 2230

Abstract

Phytoseiid mite Neoseiulus barkeri is a crucial biological control agent utilized to control pest mites and many insects in crops all over the world. However, they are vulnerable to multiple environmental pressures, with high-temperature stress being the most significant challenge. Heat stress disrupts the balance of reactive oxygen species (ROS) levels in organisms, resulting in oxidative stress within the body. Antioxidant enzymes play a crucial role in effectively neutralizing and clearing ROS. In this study, comparative transcriptomics and quantitative real-time PCR (qRT-PCR) were employed to assess the impact of short-term heat stress on the transcript expression of antioxidant enzyme genes in N. barkeri. We primarily identified four antioxidant enzyme genes (NbSOD, NbPrx, NbCAT, and NbGPX) in N. barkeri after exposure to short-term heat stress. Then, new data on the expression patterns of these genes were generated. RNA sequencing and bioinformatics analysis revealed that NbSOD belongs to the Fe/Mn family of superoxide dismutase (SOD), which was identified as MnSOD. NbPrx was classified as a 1-Cys peroxiredoxin of the peroxidase family, whereas NbCAT was recognized as a classical catalase, and NbGPX was determined as cytoplasmic glutathione peroxidase-1 (GPX1). Transcriptional expression analysis of these four genes was conducted at different high temperatures: 36 °C, 38 °C, and 40 °C for 2, 4, and 6 h. The results also showed that all four genes exhibited significant up-regulation in response to short-term heat stress. Similarly, the highest expression levels for NbSOD, NbPrx, and NbCAT were observed at 40 °C for 4 h. However, NbGPX displayed its maximum expression value at 38 °C for 4 h. Overall, the obtained data suggest that short-term heat stress increases levels of ROS generated inside living organisms, which disrupts the oxidative balance and leads to alterations in the expression levels of antioxidant enzyme genes. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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13 pages, 1767 KiB

Open AccessArticle

Acute Oxidative Stress Can Paradoxically Suppress Human NRF2 Protein Synthesis by Inhibiting Global Protein Translation

by Kaitlin M. Pensabene, Joseph LaMorte, Amanda E. Allender, Janessa Wehr, Prabhjot Kaur, Matthew Savage and Aimee L. Eggler

Antioxidants 2023, 12(9), 1735; https://doi.org/10.3390/antiox12091735 - 7 Sep 2023

Cited by 8 | Viewed by 2070

Abstract

The NRF2 transcription factor is a master regulator of the cellular oxidant/electrophile response and a drug target for the prevention/treatment of chronic diseases. A major mechanism of NRF2 activation is its escape from rapid degradation, and newly synthesized NRF2 induces cytoprotective protein expression through its cognate antioxidant response elements (AREs). However, oxidative stress can also inhibit global protein translation, thereby potentially inhibiting NRF2 protein accumulation. H₂O₂ has been shown to be a relatively weak inducer of NRF2 in comparison with electrophiles. In the current study, we evaluated whether levels of H₂O₂ that activate the NRF2/ARE pathway inhibit NRF2 protein synthesis in HaCaT keratinocytes. A weak maximum induction was observed for H₂O₂ in comparison with electrophiles, both for NRF2 protein accumulation and ARE reporter activation (~10-fold compared to ≥100-fold activation). At similar H₂O₂ concentrations, both NRF2 protein synthesis and global protein synthesis were inhibited. The manganese porphyrin antioxidant MnTMPyP rescued both global protein synthesis and NRF2 protein synthesis from H₂O₂ inhibition and increased ARE reporter activation. Similar results were observed for the diphenol di-tert-butylhydroquinone (dtBHQ). In conclusion, induction of the NRF2/ARE pathway by H₂O₂ and dtBHQ-derived oxidative species can be limited by inhibition of NRF2 protein synthesis, likely by arrest of global protein synthesis. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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19 pages, 11637 KiB

Open AccessArticle

Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties

by Andrej Poljovka, Miloš Musil, David Bednář, Katarína Chovanová, Vladena Bauerová-Hlinková, Jana Bellová, Lenka Kohútová, Peter Baráth and Marcel Zámocký

Antioxidants 2023, 12(7), 1382; https://doi.org/10.3390/antiox12071382 - 4 Jul 2023

Cited by 1 | Viewed by 3258

Abstract

Catalase–peroxidases (KatGs) are unique bifunctional oxidoreductases that contain heme in their active centers allowing both the peroxidatic and catalatic reaction modes. These originally bacterial enzymes are broadly distributed among various fungi allowing them to cope with reactive oxygen species present in the environment or inside the cells. We used various biophysical, biochemical, and bioinformatics methods to investigate differences between catalase–peroxidases originating in thermophilic and mesophilic fungi from different habitats. Our results indicate that the architecture of the active center with a specific post-translational modification is highly similar in mesophilic and thermophilic KatG and also the peroxidatic acitivity with ABTS, guaiacol, and L-DOPA. However, only the thermophilic variant CthedisKatG reveals increased manganese peroxidase activity at elevated temperatures. The catalatic activity releasing molecular oxygen is comparable between CthedisKatG and mesophilic MagKatG1 over a broad temperature range. Two constructed point mutations in the active center were performed selectively blocking the formation of described post-translational modification in the active center. They exhibited a total loss of catalatic activity and changes in the peroxidatic activity. Our results indicate the capacity of bifunctional heme enzymes in the variable reactivity for potential biotech applications. Full article

(This article belongs to the Special Issue Oxidative Stress in Various Forms and Efficient Antioxidant Pathways in Prokaryotic and Eukaryotic Cells)

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