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8.8
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Antioxidants
Special Issues
Thioredoxin Family Proteins
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Thioredoxin Family Proteins

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

Deadline for manuscript submissions: closed (30 June 2020) | Viewed by 18245

Special Issue Editors

Prof. Dr. Junji Yodoi

E-Mail Website
Guest Editor
1. Inst. Virus Research, Kyoto University, Kyoto, Japan
2. Japan Biostress Research Promotion Alliance (JBPA), Kyoto, Japan
Interests: redox regulation; thioredoxin family; TXNIP/TBP2/VDUP1; stress signal; retrovirus; infection immunity; allergy
Prof. Dr. Kiichi Hirota

E-Mail Website
Guest Editor
Department of Human Stress Response Science, Institute of Biomedical Science, Kansai Medical University, Hirakata, Japan
Interests: redox biology; transciption factors; TXNIP; inflammation; RNA-Seq; anesthesiology; bioinfomatics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The thioredoxin (Trx) system, comprising nicotinamide adenine dinucleotide phosphate, Trx reductase, and Trx, cooperating with TXNIP/TBP2/VDUP1, is critical for maintaining cellular redox balance and antioxidant function, including control of oxidative stress and cell death.

During the past few decades, it has been widely recognized that reduction–oxidation (redox) responses occurring at the intra- and extra-cellular levels are one of most important biological phenomena, and dysregulated redox responses are involved in the initiation and progression of multiple diseases.

We invite research and review papers in any area of the redox biology research field that are related, but not limited, to fundamental understanding of TRX and its family molecules, such as peroxiredoxin and gluraredoxin, and signaling pathways, diagnostic, prognostic, and pharmacogenomic biomarkers, molecular targets driving the regulation of human physiology and pathophysiology and clinical trial with new agents, and validation in animal models.

We hope that this Special Issue reflects the exciting era that we are living in with respect to the field of the TRX system and its applications in medicine and health science.

Prof. Em. Junji Yodoi
Prof. Kiichi Hirota
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
  • thioredoxin reducatase
  • thioredoxin-interacting protein
  • glutaredoxin
  • peroxiredoxin
  • redoxisome
  • oxidative stress
  • inflammation
  • immunology
  • cancer
  • aging
  • diabetes mellitus

Published Papers (4 papers)

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Research

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12 pages, 4642 KiB  
Article
Functional Characterization of a Rice Thioredoxin Protein OsTrxm and Its Cysteine Mutant Variant with Antifungal Activity
by Seong-Cheol Park, Il Ryong Kim, Jin-Young Kim, Yongjae Lee, Su-Hyang Yoo, Ji Hyun Jung, Gang-Won Cheong, Sang Yeol Lee, Mi-Kyeong Jang and Jung Ro Lee
Antioxidants 2019, 8(12), 598; https://doi.org/10.3390/antiox8120598 - 29 Nov 2019
Cited by 8 | Viewed by 2433
Abstract
Although there are many antimicrobial proteins in plants, they are not well-explored. Understanding the mechanism of action of plant antifungal proteins (AFPs) may help combat fungal infections that impact crop yields. In this study, we aimed to address this gap by screening Oryza [...] Read more.
Although there are many antimicrobial proteins in plants, they are not well-explored. Understanding the mechanism of action of plant antifungal proteins (AFPs) may help combat fungal infections that impact crop yields. In this study, we aimed to address this gap by screening Oryza sativa leaves to isolate novel AFPs. We identified a thioredoxin protein with antioxidant properties. Being ubiquitous, thioredoxins (Trxs) function in the redox balance of all living organisms. Sequencing by Edman degradation method revealed the AFP to be O. sativa Thioredoxin m-type isoform (OsTrxm). We purified the recombinant OsTrxm and its cysteine mutant proteins (OsTrxm C/S) in Escherichia coli. The recombinant OsTrxm proteins inhibited the growth of various pathogenic fungal cells. Interestingly, OsTrxm C/S mutant showed higher antifungal activity than OsTrxm. A growth inhibitory assay against various fungal pathogens and yeasts confirmed the pertinent role of cysteine residues. The OsTrxm protein variants penetrated the fungal cell wall and membrane, accumulated in the cells and generated reactive oxygen species. Although the role of OsTrxm in chloroplast development is known, its biochemical and molecular functions have not been elucidated. These findings suggest that in addition to redox regulation, OsTrxm also functions as an antimicrobial agent. Full article
(This article belongs to the Special Issue Thioredoxin Family Proteins)
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18 pages, 3990 KiB  
Article
Thioredoxin Downregulation Enhances Sorafenib Effects in Hepatocarcinoma Cells
by María José López-Grueso, Raúl González, Jordi Muntané, José Antonio Bárcena and C. Alicia Padilla
Antioxidants 2019, 8(10), 501; https://doi.org/10.3390/antiox8100501 - 22 Oct 2019
Cited by 13 | Viewed by 2904
Abstract
Sorafenib is the first-line recommended therapy for patients with advanced hepatocarcinoma (HCC) in de-differentiation stage (presenting epithelial–mesenchymal transition, EMT). We studied the role of the thioredoxin system (Trx1/TrxR1) in the sensitivity or resistance of HCC cells to the treatment with Sorafenib. As a [...] Read more.
Sorafenib is the first-line recommended therapy for patients with advanced hepatocarcinoma (HCC) in de-differentiation stage (presenting epithelial–mesenchymal transition, EMT). We studied the role of the thioredoxin system (Trx1/TrxR1) in the sensitivity or resistance of HCC cells to the treatment with Sorafenib. As a model, we used a set of three established HCC cell lines with different degrees of de-differentiation as occurs in metastasis. By quantitative proteomics, we found that the expression levels of Trx1 and TrxR1 followed the same trend as canonical EMT markers in these cell lines. Treatment with Sorafenib induced thiol redox reductive changes in critical elements of oncogenic pathways in all three cell lines but induced drastic proteome reprograming only in HCC cell lines of intermediate stage. Trx1 downregulation counteracted the thiol reductive effect of Sorafenib on Signal Transducer and Activator of Transcription 3 (STAT3) but not on Mitogen-Activated Protein Kinase (MAPK) or Protein Kinase B (Akt) and transformed advanced HCC cells into Sorafenib-sensitive cells. Ten targets of the combined Sorafenib–siRNATrx1 treatment were identified that showed a gradually changing expression trend in parallel to changes in the expression of canonical EMT markers, likely as a result of the activation of Hippo signaling. These findings support the idea that a combination of Sorafenib with thioredoxin inhibitors should be taken into account in the design of therapies against advanced HCC. Full article
(This article belongs to the Special Issue Thioredoxin Family Proteins)
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14 pages, 3123 KiB  
Article
C-Terminal Redox Domain of Arabidopsis APR1 Is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function
by Fang-Fang Chen, Chia-Yu Chien, Chao-Cheng Cho, Yu-Yung Chang and Chun-Hua Hsu
Antioxidants 2019, 8(10), 461; https://doi.org/10.3390/antiox8100461 - 08 Oct 2019
Cited by 3 | Viewed by 3020
Abstract
Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5′-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have [...] Read more.
Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5′-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved α/β thioredoxin fold, but not a glutaredoxin fold. Further biochemical studies of the redox domain from AtAPR1 provided evidence to support the structural observation. Collectively, our results provide structural and biochemical information to explain how the thioredoxin fold exerts the glutaredoxin function in APR. Full article
(This article belongs to the Special Issue Thioredoxin Family Proteins)
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Review

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20 pages, 1460 KiB  
Review
TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis
by Eiji Yoshihara
Antioxidants 2020, 9(8), 765; https://doi.org/10.3390/antiox9080765 - 18 Aug 2020
Cited by 56 | Viewed by 9297
Abstract
Identification of thioredoxin binding protein-2 (TBP-2), which is currently known as thioredoxin interacting protein (TXNIP), as an important binding partner for thioredoxin (TRX) revealed that an evolutionarily conserved reduction-oxidation (redox) signal complex plays an important role for pathophysiology. Due to the reducing activity [...] Read more.
Identification of thioredoxin binding protein-2 (TBP-2), which is currently known as thioredoxin interacting protein (TXNIP), as an important binding partner for thioredoxin (TRX) revealed that an evolutionarily conserved reduction-oxidation (redox) signal complex plays an important role for pathophysiology. Due to the reducing activity of TRX, the TRX/TXNIP signal complex has been shown to be an important regulator for redox-related signal transduction in many types of cells in various species. In addition to its role in redox-dependent regulation, TXNIP has cellular functions that are performed in a redox-independent manner, which largely rely on their scaffolding function as an ancestral α-Arrestin family. Both the redox-dependent and -independent TXNIP functions serve as regulatory pathways in glucose metabolism. This review highlights the key advances in understanding TXNIP function as a master regulator for whole-body glucose homeostasis. The potential for therapeutic advantages of targeting TXNIP in diabetes and the future direction of the study are also discussed. Full article
(This article belongs to the Special Issue Thioredoxin Family Proteins)
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