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Antioxidants
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Selenium and Selenoproteins for Optimal Health
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Selenium and Selenoproteins for Optimal Health

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Health Outcomes of Antioxidants and Oxidative Stress".

Deadline for manuscript submissions: closed (31 December 2017) | Viewed by 36336

Special Issue Editors

Prof. Dr. Xingen Lei

E-Mail Website
Guest Editor
Department of Animal Science, Cornell University, Ithaca, NY, USA
Interests: molecular nutrition; minerals; alternative protein; global food security; sustainable development; human health; metabolic disease; antioxidant; oxidative stress; signaling; functional genomics
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Wen-Hsing Cheng

E-Mail Website
Guest Editor
Department of Food Science, Nutrition and Health Promotion, College of Agriculture and Life Science, Mississippi State University, Mississippi State, MS 39762, USA
Interests: selenium; aging; geroscience; selenoprotein; genome stability
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Selenium is an essential mineral and mediates physiological and pathophysiological conditions, mainly through selenoproteins. Selenocysteine is co-translationally incorporated into nascent selenoproteins by using the UGA codon. All functionally characterized selenoproteins are oxidoreductases. The 25 human selenoproteins are categorized as glutathione peroxidases (GPX1–4 and 6), thioredoxin reductases (TXNRD1–3), iodothyronine deiodinases (DIO1–3), Rdx family members (SELENOW, SELENOT, SELENOH, and SELENOV), thioredoxin-like fold endoplasmic reticulum proteins (SELENOF and SELENOM), methionine-R-sulfoxide reductase-1, selenophosphate synthetase-2 (SEPHS2), others (SELENOI, SELENOK, SELENOS, SELENOO, SELENON, and SELENOP). GPX6 is not a selenoprotein in rodents. Selenoproteins have been implicated in neurological, cardiovascular, reproductive and infectious diseases, cancer, and diabetes. Pathologies of these diseases are associated with imbalances between generation and elimination of reactive oxygen or nitrogen species. While overproduction of free radicals induces oxidative stress and results in adverse physiological conditions, selenoproteins can paradoxically promote redox stress. Animal or human studies have demonstrated strong linkages of selenium metabolism, selenoprotein functions, and selenoprotein-related genetic aberrations to human health. The field of selenium biology has been advanced tremendously through the employment of various mouse and cell models, functional genomics, and systems biology. This Special Issue welcomes submissions addressing any aspect of selenium and selenoprotein regulations towards optimal health.

Prof. Dr. Xin Gen Lei
Prof. Dr. Wen-Hsing Cheng
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

  • selenium

  • selenoproteins

  • antioxidants

  • reactive oxygen species

  • reactive nitrogen species

  • oxidative stress

  • reductive stress

  • chronic diseases

  • optimal health

  • nutrition

Published Papers (6 papers)

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Research

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21 pages, 3511 KiB  
Article
Interplay between Selenium Levels and Replicative Senescence in WI-38 Human Fibroblasts: A Proteomic Approach
by Ghania Hammad, Yona Legrain, Zahia Touat-Hamici, Stéphane Duhieu, David Cornu, Anne-Laure Bulteau and Laurent Chavatte
Antioxidants 2018, 7(1), 19; https://doi.org/10.3390/antiox7010019 - 20 Jan 2018
Cited by 21 | Viewed by 5055
Abstract
Selenoproteins are essential components of antioxidant defense, redox homeostasis, and cell signaling in mammals, where selenium is found in the form of a rare amino acid, selenocysteine. Selenium, which is often limited both in food intake and cell culture media, is a strong [...] Read more.
Selenoproteins are essential components of antioxidant defense, redox homeostasis, and cell signaling in mammals, where selenium is found in the form of a rare amino acid, selenocysteine. Selenium, which is often limited both in food intake and cell culture media, is a strong regulator of selenoprotein expression and selenoenzyme activity. Aging is a slow, complex, and multifactorial process, resulting in a gradual and irreversible decline of various functions of the body. Several cellular aspects of organismal aging are recapitulated in the replicative senescence of cultured human diploid fibroblasts, such as embryonic lung fibroblast WI-38 cells. We previously reported that the long-term growth of young WI-38 cells with high (supplemented), moderate (control), or low (depleted) concentrations of selenium in the culture medium impacts their replicative lifespan, due to rapid changes in replicative senescence-associated markers and signaling pathways. In order to gain insight into the molecular link between selenium levels and replicative senescence, in the present work, we have applied a quantitative proteomic approach based on 2-Dimensional Differential in-Gel Electrophoresis (2D-DIGE) to the study of young and presenescent cells grown in selenium-supplemented, control, or depleted media. Applying a restrictive cut-off (spot intensity ±50% and a p value < 0.05) to the 2D-DIGE analyses revealed 81 differentially expressed protein spots, from which 123 proteins of interest were identified by mass spectrometry. We compared the changes in protein abundance for three different conditions: (i) spots varying between young and presenescent cells, (ii) spots varying in response to selenium concentration in young cells, and (iii) spots varying in response to selenium concentration in presenescent cells. Interestingly, a 72% overlap between the impact of senescence and selenium was observed in our proteomic results, demonstrating a strong interplay between selenium, selenoproteins, and replicative senescence. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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3198 KiB  
Article
Selenoprotein K Increases Efficiency of DHHC6 Catalyzed Protein Palmitoylation by Stabilizing the Acyl-DHHC6 Intermediate
by Gregory J. Fredericks, FuKun W. Hoffmann, Robert J. Hondal, Sharon Rozovsky, Johann Urschitz and Peter R. Hoffmann
Antioxidants 2018, 7(1), 4; https://doi.org/10.3390/antiox7010004 - 29 Dec 2017
Cited by 23 | Viewed by 5338
Abstract
Selenoprotein K (SELENOK) is a selenocysteine (Sec)-containing protein localized in the endoplasmic reticulum (ER) membrane where it interacts with the DHHC6 (where single letter symbols represent Asp-His-His-Cys amino acids) enzyme to promote protein acyl transferase (PAT) reactions. PAT reactions involve the DHHC enzymatic [...] Read more.
Selenoprotein K (SELENOK) is a selenocysteine (Sec)-containing protein localized in the endoplasmic reticulum (ER) membrane where it interacts with the DHHC6 (where single letter symbols represent Asp-His-His-Cys amino acids) enzyme to promote protein acyl transferase (PAT) reactions. PAT reactions involve the DHHC enzymatic capture of palmitate via a thioester bond to cysteine (Cys) residues that form an unstable palmitoyl-DHHC intermediate, followed by transfer of palmitate to Cys residues of target proteins. How SELENOK facilitates this reaction has not been determined. Splenocyte microsomal preparations from wild-type mice versus SELENOK knockout mice were used to establish PAT assays and showed decreased PAT activity (~50%) under conditions of SELENOK deficiency. Using recombinant, soluble versions of DHHC6 along with SELENOK containing Sec92, Cys92, or alanine (Ala92), we evaluated the stability of the acyl-DHHC6 intermediate and its capacity to transfer the palmitate residue to Cys residues on target peptides. Versions of SELENOK containing either Ala or Cys residues in place of Sec were equivalently less effective than Sec at stabilizing the acyl-DHHC6 intermediate or promoting PAT activity. These data suggest that Sec92 in SELENOK serves to stabilize the palmitoyl-DHHC6 intermediate by reducing hydrolyzation of the thioester bond until transfer of the palmitoyl group to the Cys residue on the target protein can occur. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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881 KiB  
Article
Selenium Concentrations for Maximisation of Thioredoxin Reductase 2 Activity and Upregulation of Its Gene Transcripts in Senescent Human Fibroblasts
by Hazem K. Ghneim
Antioxidants 2017, 6(4), 83; https://doi.org/10.3390/antiox6040083 - 30 Oct 2017
Cited by 6 | Viewed by 3875
Abstract
Thioredoxin reductase 2 (TR2) activity, its gene transcripts, and hydrogen peroxide (H2O2) generation were examined in biochemically identified early-senescent P20 and senescent P30 fibroblasts subcultured in media (MEM2–MEM8) containing Se concentrations at 1.25, 2.5, 3.5, 5.0, 6.0, 7.0, and [...] Read more.
Thioredoxin reductase 2 (TR2) activity, its gene transcripts, and hydrogen peroxide (H2O2) generation were examined in biochemically identified early-senescent P20 and senescent P30 fibroblasts subcultured in media (MEM2–MEM8) containing Se concentrations at 1.25, 2.5, 3.5, 5.0, 6.0, 7.0, and 8.0 µM, respectively. Although TR2 activity was moderately increased in P20 and P30 cells subcultured in routine growth medium (MEM1), there were progressive significant activity increases in the same cells subcultured in MEM2–MEM8. Such increases were proportional to Se concentration and peaked in P30 cells incubated with MEM7 and MEM8. H2O2 generation underwent progressive increases in MEM1-incubated P20 and P30 cells, peaking in the latter, but was gradually lowered in those incubated with MEM2–MEM8, reaching its lowest values when cells were incubated with MEM7 and MEM8. In parallel, TR2 gene transcripts underwent significant upregulation in P20 cells and higher magnitude upregulation in P30 cells subcultured in MEM2, MEM4, and MEM8 compared to those recorded for P5 pre-senescent cells subcultured in the same media. The computed Km Se values with respect to TR2 activity equaled 3.34 and 4.98 µM for P20 and P30 cells, respectively, with corresponding Vmax activities of 55.9 and 96.2 nmol/min/mg protein. It is concluded that senescent P30 cells utilize more Se and achieve maximal TR2 activity to combat oxidative injury. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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2507 KiB  
Article
Antioxidant Properties of Selenophene, Thiophene and Their Aminocarbonitrile Derivatives
by Levon A. Tavadyan, Zaruhi H. Manukyan, Lusik H. Harutyunyan, Makich V. Musayelyan, Adrine D. Sahakyan and Hakob G. Tonikyan
Antioxidants 2017, 6(2), 22; https://doi.org/10.3390/antiox6020022 - 24 Mar 2017
Cited by 32 | Viewed by 5970
Abstract
The oxygen radical absorbance capacity (ORAC) method was used to detect the antiperoxyradical ability of organoselenium compounds: selenophene and its derivative, 2-amino-4,5,6,7-tetrahydro-1-selenophene-3-carbonitrile (ATSe); while as a comparison, the sulfur-containing analogue of selenophene—thiophene and its derivative—2-amino-4,5,6,7-tetrahydro-1-thiophene-3-carbonitrile (ATS)—was selected. Cyclic voltammetry (CV), differential pulse voltammetry [...] Read more.
The oxygen radical absorbance capacity (ORAC) method was used to detect the antiperoxyradical ability of organoselenium compounds: selenophene and its derivative, 2-amino-4,5,6,7-tetrahydro-1-selenophene-3-carbonitrile (ATSe); while as a comparison, the sulfur-containing analogue of selenophene—thiophene and its derivative—2-amino-4,5,6,7-tetrahydro-1-thiophene-3-carbonitrile (ATS)—was selected. Cyclic voltammetry (CV), differential pulse voltammetry (DPV) and squarewave voltammetry (SWV) methods were used to determine the redox characteristics of organoselenium and organosulfur compounds. The antiradical activity and capacity of the studied compounds were also measured by using stable radical 2,2ʹ-diphenyl-1-picrylhydrazyl (DPPH). Detected anodic peaks of the oxidation of selenophene, thiophene and their derivatives in CV, DPV and SWV in the interval of −1200 ÷ (+1600) mV potentials in regard to the Ag/Ag+ medium of acetonitrile prove the presence of antiperoxyradical activity in regard to oxidizers, i.e., peroxyradicals. The chemical mechanism of the antiperoxyradical ability of selenophene, thiophene and their organic derivatives is proposed. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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3326 KiB  
Article
Selenium- and Tellurium-Based Antioxidants for Modulating Inflammation and Effects on Osteoblastic Activity
by Xi Lu, Gemma Mestres, Vijay Pal Singh, Pedram Effati, Jia-Fei Poon, Lars Engman and Marjam Karlsson Ott
Antioxidants 2017, 6(1), 13; https://doi.org/10.3390/antiox6010013 - 14 Feb 2017
Cited by 22 | Viewed by 6459
Abstract
Increased oxidative stress plays a significant role in the etiology of bone diseases. Heightened levels of H2O2 disrupt bone homeostasis, leading to greater bone resorption than bone formation. Organochalcogen compounds could act as free radical trapping agents or glutathione peroxidase mimetics, reducing oxidative [...] Read more.
Increased oxidative stress plays a significant role in the etiology of bone diseases. Heightened levels of H2O2 disrupt bone homeostasis, leading to greater bone resorption than bone formation. Organochalcogen compounds could act as free radical trapping agents or glutathione peroxidase mimetics, reducing oxidative stress in inflammatory diseases. In this report, we synthesized and screened a library of organoselenium and organotellurium compounds for hydrogen peroxide scavenging activity, using macrophagic cell lines RAW264.7 and THP-1, as well as human mono- and poly-nuclear cells. These cells were stimulated to release H2O2, using phorbol 12-myristate 13-acetate, with and without organochalogens. Released H2O2 was then measured using a chemiluminescent assay over a period of 2 h. The screening identified an organoselenium compound which scavenged H2O2 more effectively than the vitamin E analog, Trolox. We also found that this organoselenium compound protected MC3T3 cells against H2O2-induced toxicity, whereas Trolox did not. The organoselenium compound exhibited no cytotoxicity to the cells and had no deleterious effects on cell proliferation, viability, or alkaline phosphatase activity. The rapidity of H2O2 scavenging and protection suggests that the mechanism of protection is due to the direct scavenging of extracellular H2O2. This compound is a promising modulators of inflammation and could potentially treat diseases involving high levels of oxidative stress. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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Review

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12 pages, 466 KiB  
Review
Selenium and Selenoproteins in Gut Inflammation—A Review
by Shaneice K. Nettleford and K. Sandeep Prabhu
Antioxidants 2018, 7(3), 36; https://doi.org/10.3390/antiox7030036 - 01 Mar 2018
Cited by 55 | Viewed by 8934
Abstract
Inflammatory bowel disease (IBD), characterized by severe flares and remissions, is a debilitating condition. While the etiology is unknown, many immune cells, such as macrophages, T cells and innate lymphoid cells, are implicated in the pathogenesis of the disease. Previous studies have shown [...] Read more.
Inflammatory bowel disease (IBD), characterized by severe flares and remissions, is a debilitating condition. While the etiology is unknown, many immune cells, such as macrophages, T cells and innate lymphoid cells, are implicated in the pathogenesis of the disease. Previous studies have shown the ability of micronutrient selenium (Se) and selenoproteins to impact inflammatory signaling pathways implicated in the pathogenesis of the disease. In particular, two transcription factors, nuclear factor-κB (NF-κB), and peroxisome proliferator activated receptor (PPAR)γ, which are involved in the activation of immune cells, and are also implicated in various stages of inflammation and resolution, respectively, are impacted by Se status. Available therapies for IBD produce detrimental side effects, resulting in the need for alternative therapies. Here, we review the current understanding of the role of NF-κB and PPARγ in the activation of immune cells during IBD, and how Se and selenoproteins modulate effective resolution of inflammation to be considered as a promising alternative to treat IBD. Full article
(This article belongs to the Special Issue Selenium and Selenoproteins for Optimal Health)
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