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Antioxidants
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Thioredoxin
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Thioredoxin

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 2023) | Viewed by 8888

Special Issue Editors

Dr. José Godoy

E-Mail Website
Guest Editor
Department of Veterinary Biomedical Sciences, Long Island University College of Veterinary Medicine, 720 Northern Boulevard, Brookville, NY 11548, USA
Interests: redox proteins; thioredoxin; age-related diseases; oxidative stress; veterinary
Prof. Dr. Luciana Azevedo

E-Mail Website
Guest Editor
Faculty of Nutrition, Federal University of Alfenas, Alfenas, MG, Brazil
Interests: food toxicology; mutagenicity; cancer; functional foods; using in vivo and in vitro protocols

Special Issue Information

Dear Colleagues,

Thioredoxin 1 (Trx1) was originally discovered as an electron donor for E. coli’s enzyme ribonucleotide reductase. Since then, intensive research conducted at the molecular, cellular, and organismic level has elucidated the very diverse facets of Trx1. Today, Trx1 is recognized as a key regulator of posttranslational modification of protein thiol groups. Thioredoxin 1 is ubiquitously expressed in the body and exerts its oxidoreductase function with other proteins, building redox networks in specific cellular compartments, for instance, Trx1/thioredoxin reductase (TrxR1) in the cytosol and Trx2/TrxR2 in the mitochondria. Thioredoxin 1 has also been involved in essential cellular processes such as apoptosis, cell proliferation, and the inflammatory response. The potential diagnostic and therapeutic applications of Trx1 have been studied in numerous animal models of disease, with the results being translated into both human and veterinary medicine.  

For this Special Issue, we invite researchers to provide original research articles reporting novel insights into the role of thioredoxin in physiological as well as in pathological processes. Studies involving in vitro or in vivo models showing potential therapeutic applications of thioredoxin are especially encouraged. We also invite the submission of clinical studies as well as review articles discussing the current knowledge and potential applications of thioredoxin 1 in health and disease.

Dr. José Godoy
Prof. Dr. Luciana Azevedo
Guest Editors

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

  • thioredoxin (Trx) 
  • reactive oxygen species (ROS)
  • redox signaling 
  • thiol switches 
  • animal models

Published Papers (4 papers)

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Research

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14 pages, 7273 KiB  
Article
Caffeine Inhibits Oxidative Stress- and Low Dose Endotoxemia-Induced Senescence—Role of Thioredoxin-1
by Dennis Merk, Jan Greulich, Annika Vierkant, Fiona Cox, Olaf Eckermann, Florian von Ameln, Nadine Dyballa-Rukes, Joachim Altschmied, Niloofar Ale-Agha, Philipp Jakobs and Judith Haendeler
Antioxidants 2023, 12(6), 1244; https://doi.org/10.3390/antiox12061244 - 09 Jun 2023
Cited by 2 | Viewed by 1417
Abstract
The maintenance of Thioredoxin-1 (Trx-1) levels, and thus of cellular redox homeostasis, is vital for endothelial cells (ECs) to prevent senescence induction. One hallmark of EC functionality, their migratory capacity, which depends on intact mitochondria, is reduced in senescence. Caffeine improves the migratory [...] Read more.
The maintenance of Thioredoxin-1 (Trx-1) levels, and thus of cellular redox homeostasis, is vital for endothelial cells (ECs) to prevent senescence induction. One hallmark of EC functionality, their migratory capacity, which depends on intact mitochondria, is reduced in senescence. Caffeine improves the migratory capacity and mitochondrial functionality of ECs. However, the impact of caffeine on EC senescence has never been investigated. Moreover, a high-fat diet, which can induce EC senescence, results in approximately 1 ng/mL lipopolysaccharide (LPS) in the blood. Therefore, we investigated if low dose endotoxemia induces EC senescence and concomitantly reduces Trx-1 levels, and if caffeine prevents or even reverses senescence. We show that caffeine precludes H2O2-triggered senescence induction by maintaining endothelial NO synthase (eNOS) levels and preventing the elevation of p21. Notably, 1 ng/mL LPS also increases p21 levels and reduces eNOS and Trx-1 amounts. These effects are completely blocked by co-treatment with caffeine. This prevention of senescence induction is similarly accomplished by the permanent expression of mitochondrial p27, a downstream effector of caffeine. Most importantly, after senescence induction by LPS, a single bolus of caffeine inhibits the increase in p21. This treatment also blocks Trx-1 degradation, suggesting that the reversion of senescence is intimately associated with a normalized redox balance. Full article
(This article belongs to the Special Issue Thioredoxin)
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Review

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26 pages, 2834 KiB  
Review
Thioredoxin/Glutaredoxin Systems and Gut Microbiota in NAFLD: Interplay, Mechanism, and Therapeutical Potential
by Minghui Zhu, Omer M. A. Dagah, Billton Bryson Silaa and Jun Lu
Antioxidants 2023, 12(9), 1680; https://doi.org/10.3390/antiox12091680 - 28 Aug 2023
Cited by 3 | Viewed by 1431
Abstract
Non-alcoholic fatty liver disease (NAFLD) is a common clinical disease, and its pathogenesis is closely linked to oxidative stress and gut microbiota dysbiosis. Recently accumulating evidence indicates that the thioredoxin and glutaredoxin systems, the two thiol-redox dependent antioxidant systems, are the key players [...] Read more.
Non-alcoholic fatty liver disease (NAFLD) is a common clinical disease, and its pathogenesis is closely linked to oxidative stress and gut microbiota dysbiosis. Recently accumulating evidence indicates that the thioredoxin and glutaredoxin systems, the two thiol-redox dependent antioxidant systems, are the key players in the NAFLD’s development and progression. However, the effects of gut microbiota dysbiosis on the liver thiol-redox systems are not well clarified. This review explores the role and mechanisms of oxidative stress induced by bacteria in NAFLD while emphasizing the crucial interplay between gut microbiota dysbiosis and Trx mediated-redox regulation. The paper explores how dysbiosis affects the production of specific gut microbiota metabolites, such as trimethylamine N-oxide (TMAO), lipopolysaccharides (LPS), short-chain fatty acids (SCFAs), amino acids, bile acid, and alcohol. These metabolites, in turn, significantly impact liver inflammation, lipid metabolism, insulin resistance, and cellular damage through thiol-dependent redox signaling. It suggests that comprehensive approaches targeting both gut microbiota dysbiosis and the thiol-redox antioxidant system are essential for effectively preventing and treating NAFLD. Overall, comprehending the intricate relationship between gut microbiota dysbiosis and thiol-redox systems in NAFLD holds significant promise in enhancing patient outcomes and fostering the development of innovative therapeutic interventions. Full article
(This article belongs to the Special Issue Thioredoxin)
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21 pages, 1697 KiB  
Review
The Importance of Thioredoxin-1 in Health and Disease
by Tina Oberacker, Leonie Kraft, Moritz Schanz, Jörg Latus and Severin Schricker
Antioxidants 2023, 12(5), 1078; https://doi.org/10.3390/antiox12051078 - 11 May 2023
Cited by 7 | Viewed by 3157
Abstract
Thioredoxin-1 (Trx-1) is a multifunctional protein ubiquitously found in the human body. Trx-1 plays an important role in various cellular functions such as maintenance of redox homeostasis, proliferation, and DNA synthesis, but also modulation of transcription factors and control of cell death. Thus, [...] Read more.
Thioredoxin-1 (Trx-1) is a multifunctional protein ubiquitously found in the human body. Trx-1 plays an important role in various cellular functions such as maintenance of redox homeostasis, proliferation, and DNA synthesis, but also modulation of transcription factors and control of cell death. Thus, Trx-1 is one of the most important proteins for proper cell and organ function. Therefore, modulation of Trx gene expression or modulation of Trx activity by various mechanisms, including post-translational modifications or protein–protein interactions, could cause a transition from the physiological state of cells and organs to various pathologies such as cancer, and neurodegenerative and cardiovascular diseases. In this review, we not only discuss the current knowledge of Trx in health and disease, but also highlight its potential function as a biomarker. Full article
(This article belongs to the Special Issue Thioredoxin)
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18 pages, 1395 KiB  
Review
Evolutionarily Conserved Role of Thioredoxin Systems in Determining Longevity
by Abdelrahman AlOkda and Jeremy M. Van Raamsdonk
Antioxidants 2023, 12(4), 944; https://doi.org/10.3390/antiox12040944 - 17 Apr 2023
Cited by 3 | Viewed by 2248
Abstract
Thioredoxin and thioredoxin reductase are evolutionarily conserved antioxidant enzymes that protect organisms from oxidative stress. These proteins also play roles in redox signaling and can act as a redox-independent cellular chaperone. In most organisms, there is a cytoplasmic and mitochondrial thioredoxin system. A [...] Read more.
Thioredoxin and thioredoxin reductase are evolutionarily conserved antioxidant enzymes that protect organisms from oxidative stress. These proteins also play roles in redox signaling and can act as a redox-independent cellular chaperone. In most organisms, there is a cytoplasmic and mitochondrial thioredoxin system. A number of studies have examined the role of thioredoxin and thioredoxin reductase in determining longevity. Disruption of either thioredoxin or thioredoxin reductase is sufficient to shorten lifespan in model organisms including yeast, worms, flies and mice, thereby indicating conservation across species. Similarly, increasing the expression of thioredoxin or thioredoxin reductase can extend longevity in multiple model organisms. In humans, there is an association between a specific genetic variant of thioredoxin reductase and lifespan. Overall, the cytoplasmic and mitochondrial thioredoxin systems are both important for longevity. Full article
(This article belongs to the Special Issue Thioredoxin)
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