Special Issue "Redox Regulation of Cell Signalling"

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

Deadline for manuscript submissions: closed (31 January 2020).

Special Issue Editors

Prof. Dr. Elizabeth C. Ledgerwood
E-Mail Website
Guest Editor
Department of Biochemistry, University of Otago, Dunedin, New Zealand
Interests: redox singalling; peroxiredoxin; thiol peroxidases; cytochrome c; apoptosis
Prof. Dr. Mark B. Hampton
E-Mail Website
Guest Editor
Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago, Christchurch, New Zealand
Tel. 64 3 3786225
Interests: redox signalling; oxidative stress; peroxiredoxins; cell death pathways; mitochondria; neutrophils

Special Issue Information

Dear Colleagues,

Over the last two decades, significant advances have been made in our understanding of the role of redox systems in controlling cell signalling in both physiological and pathological settings. This has been driven by both the identification of relevant signal transduction cascades and the development of more specific tools to assess redox signalling at the levels of oxidants, reductants, and specific cellular targets. However, much remains to be discovered, including the regulation of oxidant generation in response to physiological stimuli, how the selective oxidation of target proteins occurs, and how redox signalling interfaces with more established signalling paradigms such as phosphorylation/dephosphorylation and ubiquitylation/deubiquitylation.

This Special Issue will publish original research papers and reviews on aspects of redox signalling that relate to the physiological production of reactive oxidants, specific post-translational modifications that occur and how these can be monitored, the relationship between redox signalling and other signal transduction pathways, the involvement of redox signalling in disease, and the therapeutic targeting of redox signalling pathways.

Prof. Dr. Elizabeth C. Ledgerwood
Prof. Dr. Mark B. Hampton
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 papers will be 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 1400 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

  • Redox signalling
  • Thiol peroxidase
  • Reactive oxygen and nitrogen species
  • Mitochondria
  • NADPH oxidase

Published Papers (3 papers)

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Research

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Open AccessArticle
Manganese Porphyrin-Based SOD Mimetics Produce Polysulfides from Hydrogen Sulfide
Antioxidants 2019, 8(12), 639; https://doi.org/10.3390/antiox8120639 - 12 Dec 2019
Abstract
Manganese-centered porphyrins (MnPs), MnTE-2-PyP5+ (MnTE), MnTnHex-2-PyP5+ (MnTnHex), and MnTnBuOE-2-PyP5+ (MnTnBuOE) have received considerable attention because of their ability to serve as superoxide dismutase (SOD) mimetics thereby producing hydrogen peroxide (H2O2), and oxidants of ascorbate and simple [...] Read more.
Manganese-centered porphyrins (MnPs), MnTE-2-PyP5+ (MnTE), MnTnHex-2-PyP5+ (MnTnHex), and MnTnBuOE-2-PyP5+ (MnTnBuOE) have received considerable attention because of their ability to serve as superoxide dismutase (SOD) mimetics thereby producing hydrogen peroxide (H2O2), and oxidants of ascorbate and simple aminothiols or protein thiols. MnTE-2-PyP5+ and MnTnBuOE-2-PyP5+ are now in five Phase II clinical trials warranting further exploration of their rich redox-based biology. Previously, we reported that SOD is also a sulfide oxidase catalyzing the oxidation of hydrogen sulfide (H2S) to hydrogen persulfide (H2S2) and longer-chain polysulfides (H2Sn, n = 3–7). We hypothesized that MnPs may have similar actions on sulfide metabolism. H2S and polysulfides were monitored in fluorimetric assays with 7-azido-4-methylcoumarin (AzMC) and 3′,6′-di(O-thiosalicyl)fluorescein (SSP4), respectively, and specific polysulfides were further identified by mass spectrometry. MnPs concentration-dependently consumed H2S and produced H2S2 and subsequently longer-chain polysulfides. This reaction appeared to be O2-dependent. MnP absorbance spectra exhibited wavelength shifts in the Soret and Q bands characteristic of sulfide-mediated reduction of Mn. Taken together, our results suggest that MnPs can become efficacious activators of a variety of cytoprotective processes by acting as sulfide oxidation catalysts generating per/polysulfides. Full article
(This article belongs to the Special Issue Redox Regulation of Cell Signalling)
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Open AccessArticle
Fibroblasts to Keratinocytes Redox Signaling: The Possible Role of ROS in Psoriatic Plaque Formation
Antioxidants 2019, 8(11), 566; https://doi.org/10.3390/antiox8110566 - 18 Nov 2019
Abstract
Although the role of reactive oxygen species-mediated (ROS-mediated) signalling in physiologic and pathologic skin conditions has been proven, no data exist on the skin cells ROS-mediated communication. Primary fibroblasts were obtained from lesional and non-lesional skin of psoriatic patients. ROS, superoxide anion, calcium [...] Read more.
Although the role of reactive oxygen species-mediated (ROS-mediated) signalling in physiologic and pathologic skin conditions has been proven, no data exist on the skin cells ROS-mediated communication. Primary fibroblasts were obtained from lesional and non-lesional skin of psoriatic patients. ROS, superoxide anion, calcium and nitric oxide levels and lipoperoxidation markers and total antioxidant content were measured in fibroblasts. NADPH oxidase activity and NOX1, 2 and 4 expressions were assayed and NOX4 silencing was performed. Fibroblasts and healthy keratinocytes co-culture was performed. MAPK pathways activation was studied in fibroblasts and in co-cultured healthy keratinocytes. Increased intracellular calcium, •NO and ROS levels as well as an enhanced NADPH oxidase 4 (NOX4)–mediated extracellular ROS release was shown in lesional psoriatic vs. control fibroblasts. Upon co-culture with lesional fibroblasts, keratinocytes showed p38 and ERK MAPKs pathways activation, ROS, Ca2+ and •NO increase and cell cycle acceleration. Notably, NOX4 knockdown significantly reduced the observed effects of lesional fibroblasts on keratinocyte cell cycle progression. Co-culture with non-lesional psoriatic and control fibroblasts induced slight cell cycle acceleration, but notable intracellular ROS accumulation and ERK MAPK activation in keratinocytes. Collectively, our data demonstrate that NOX4 expressed in dermal fibroblasts is essential for the redox paracrine regulation of epidermal keratinocytes proliferation. Full article
(This article belongs to the Special Issue Redox Regulation of Cell Signalling)
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Review

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Open AccessReview
Role of Cytosolic 2-Cys Prx1 and Prx2 in Redox Signaling
Antioxidants 2019, 8(6), 169; https://doi.org/10.3390/antiox8060169 - 10 Jun 2019
Cited by 2
Abstract
Peroxiredoxins (Prxs), a family of peroxidases, are reactive oxygen species scavengers that hydrolyze H2O2 through catalytic cysteine. Mammalian Prxs comprise six isoforms (typical 2-Cys Prxs; Prx1–4, atypical 2-Cys Prx; Prx5, and 1-Cys Prx; Prx6) that are distributed over various cellular [...] Read more.
Peroxiredoxins (Prxs), a family of peroxidases, are reactive oxygen species scavengers that hydrolyze H2O2 through catalytic cysteine. Mammalian Prxs comprise six isoforms (typical 2-Cys Prxs; Prx1–4, atypical 2-Cys Prx; Prx5, and 1-Cys Prx; Prx6) that are distributed over various cellular compartments as they are classified according to the position and number of conserved cysteine. 2-Cys Prx1 and Prx2 are abundant proteins that are ubiquitously expressed mainly in the cytosol, and over 90% of their amino acid sequences are homologous. Prx1 and Prx2 protect cells from ROS-mediated oxidative stress through the elimination of H2O2 and regulate cellular signaling through redox-dependent mechanism. In addition, Prx1 and Prx2 are able to bind to a diversity of interaction partners to regulate other various cellular processes in cancer (i.e., regulation of the protein redox status, cell growth, apoptosis, and tumorigenesis). Thus, Prx1 and Prx2 can be potential therapeutic targets and it is particularly important to control their level or activity. This review focuses on cytosolic 2-Cys Prx1 and Prx2 and their role in the regulation of redox signaling based on protein-protein interaction. Full article
(This article belongs to the Special Issue Redox Regulation of Cell Signalling)
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