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Antioxidants
Special Issues
Plant and Human Sulfur Biology
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Plant and Human Sulfur Biology

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "ROS, RNS and RSS".

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 17970

Special Issue Editors

Dr. Cecilia Gotor

E-Mail Website
Guest Editor
Institute of Plant Biochemistry and Photosynthesis (IBVF), Spanish National Research Council (CSIC), Seville, Spain
Interests: abiotic stress; autophagy; Arabidopsis; cysteine metabolism; sulfide signaling
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Nicolas Rouhier

E-Mail Website
Guest Editor
INRAE, IAM, Université de Lorraine, F-54000 Nancy, France
Interests: redoxins; cysteine modification; iron-sulfur proteins; plants; protein–protein interaction
Dr. Luis Carlos Romero González

E-Mail Website1 Website2
Guest Editor
Instituto de Bioquímica Vegetal y Fotosíntesis, CSIC, 41092-Sevilla, Spain
Interests: cellular signaling; sulfur metabolism; redox regulation; proteomic analysis
Special Issues, Collections and Topics in MDPI journals
Dr. Jeremy Couturier

E-Mail Website
Guest Editor
The Faculty of Sciences and Technologies, University of Lorraine, INRAE, IAM, F-54000 Nancy, France
Interests: sulfur trafficking; sulfurtransferase; cysteine desulfurase; rhodanese; protein persulfidation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Sulfur is an essential element for life, and cysteine represents a key sulfur-containing metabolite in all organisms. In plants, cysteine is synthesized via the photosynthetic assimilation of sulfate and in animals from methionine via the transsulfuration pathway. In both plants and animals, cysteine is crucial for the structure, function and regulation of proteins, and also as a precursor of essential biomolecules and defense compounds. Hence, sulfur compounds have key roles in normal and perturbed physiological processes. In recent years, the physiological effects of hydrogen sulfide, produced in different subcellular compartments of eukaryotes, became emergent, and a role in signaling has notably been proposed to occur via cysteine persulfidation—a redox posttranslational modification (PTM) of cysteine residues that seems to be intricately connected to other redox PTMs.

We invite researchers in the field and the participants of the Joint meeting for Plant and Human Sulfur Biology and Glucosinolates, which will be held in Sevilla (Spain) in September 2021, to submit their latest research findings or review articles to this Special Issue. This will bring together current research concerning cysteine metabolism, sulfur trafficking, hydrogen sulfide formation and signaling, and protein persulfidation in both normal processes and perturbed physiological states of plant and animal cells.

We look forward to your contributions.

Dr. Cecilia Gotor
Prof. Dr. Nicolas Rouhier
Dr. Luis Romero González
Dr. Jeremy Couturier
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

  • hydrogen sulfide
  • signaling
  • protein persulfidation
  • cysteine metabolism
  • redox post-translational modification

Published Papers (5 papers)

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Research

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18 pages, 3295 KiB  
Article
The Gasotransmitter Hydrogen Sulfide (H2S) Prevents Pathologic Calcification (PC) in Cartilage
by Sonia Nasi, Driss Ehirchiou, Jessica Bertrand, Mariela Castelblanco, James Mitchell, Isao Ishii, Alexander So and Nathalie Busso
Antioxidants 2021, 10(9), 1433; https://doi.org/10.3390/antiox10091433 - 08 Sep 2021
Cited by 7 | Viewed by 2629
Abstract
Pathologic calcification (PC) is a painful and disabling condition whereby calcium-containing crystals deposit in tissues that do not physiologically calcify: cartilage, tendons, muscle, vessels and skin. In cartilage, compression and inflammation triggered by PC leads to cartilage degradation typical of osteoarthritis (OA). The [...] Read more.
Pathologic calcification (PC) is a painful and disabling condition whereby calcium-containing crystals deposit in tissues that do not physiologically calcify: cartilage, tendons, muscle, vessels and skin. In cartilage, compression and inflammation triggered by PC leads to cartilage degradation typical of osteoarthritis (OA). The PC process is poorly understood and treatments able to target the underlying mechanisms of the disease are lacking. Here we show a crucial role of the gasotransmitter hydrogen sulfide (H2S) and, in particular, of the H2S-producing enzyme cystathionine γ-lyase (CSE), in regulating PC in cartilage. Cse deficiency (Cse KO mice) exacerbated calcification in both surgically-induced (menisectomy) and spontaneous (aging) murine models of cartilage PC, and augmented PC was closely associated with cartilage degradation (OA). On the contrary, Cse overexpression (Cse tg mice) protected from these features. In vitro, Cse KO chondrocytes showed increased calcification, potentially via enhanced alkaline phosphatase (Alpl) expression and activity and increased IL-6 production. The opposite results were obtained in Cse tg chondrocytes. In cartilage samples from patients with OA, CSE expression inversely correlated with the degree of tissue calcification and disease severity. Increased cartilage degradation in murine and human tissues lacking or expressing low CSE levels may be accounted for by dysregulated catabolism. We found higher levels of matrix-degrading metalloproteases Mmp-3 and -13 in Cse KO chondrocytes, whereas the opposite results were obtained in Cse tg cells. Finally, by high-throughput screening, we identified a novel small molecule CSE positive allosteric modulator (PAM), and demonstrated that it was able to increase cellular H2S production, and decrease murine and human chondrocyte calcification and IL-6 secretion. Together, these data implicate impaired CSE-dependent H2S production by chondrocytes in the etiology of cartilage PC and worsening of secondary outcomes (OA). In this context, enhancing CSE expression and/or activity in chondrocytes could represent a potential strategy to inhibit PC. Full article
(This article belongs to the Special Issue Plant and Human Sulfur Biology)
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17 pages, 2811 KiB  
Article
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H2S Signaling by Protein Persulfidation
by Ana Jurado-Flores, Luis C. Romero and Cecilia Gotor
Antioxidants 2021, 10(4), 508; https://doi.org/10.3390/antiox10040508 - 24 Mar 2021
Cited by 33 | Viewed by 3714
Abstract
Hydrogen sulfide (H2S)-mediated signaling pathways regulate many physiological and pathophysiological processes in mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the posttranslational modification of cysteine residues to form a persulfidated thiol motif. We developed [...] Read more.
Hydrogen sulfide (H2S)-mediated signaling pathways regulate many physiological and pathophysiological processes in mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the posttranslational modification of cysteine residues to form a persulfidated thiol motif. We developed a comparative and label-free quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in N-starved Arabidopsis thaliana roots by using the tag-switch method. In this work, we identified 5214 unique proteins from root tissue that were persulfidated, 1674 of which were quantitatively analyzed and found to show altered persulfidation levels in vivo under N deprivation. These proteins represented almost 13% of the entire annotated proteome in Arabidopsis. Bioinformatic analysis revealed that persulfidated proteins were involved in a wide range of biological functions, regulating important processes such as primary metabolism, plant responses to stresses, growth and development, RNA translation and protein degradation. Quantitative mass spectrometry analysis allowed us to obtain a comprehensive view of hydrogen sulfide signaling via changes in the persulfidation levels of key protein targets involved in ubiquitin-dependent protein degradation and autophagy, among others. Full article
(This article belongs to the Special Issue Plant and Human Sulfur Biology)
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Review

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18 pages, 929 KiB  
Review
Protein Persulfidation in Plants: Function and Mechanism
by Peng Wang, Hua Fang, Rong Gao and Weibiao Liao
Antioxidants 2021, 10(10), 1631; https://doi.org/10.3390/antiox10101631 - 16 Oct 2021
Cited by 10 | Viewed by 2524
Abstract
As an endogenous gaseous transmitter, the function of hydrogen sulfide (H2S) has been extensively studied in plants. Once synthesized, H2S may be involved in almost all life processes of plants. Among them, a key route for H2S [...] Read more.
As an endogenous gaseous transmitter, the function of hydrogen sulfide (H2S) has been extensively studied in plants. Once synthesized, H2S may be involved in almost all life processes of plants. Among them, a key route for H2S bioactivity occurs via protein persulfidation, in which process oxidizes cysteine thiol (R-SH) groups into persulfide (R-SSH) groups. This process is thought to underpin a myriad of cellular processes in plants linked to growth, development, stress responses, and phytohormone signaling. Multiple lines of emerging evidence suggest that this redox-based reversible post-translational modification can not only serve as a protective mechanism for H2S in oxidative stress, but also control a variety of biochemical processes through the allosteric effect of proteins. Here, we collate emerging evidence showing that H2S-mediated persulfidation modification involves some important biochemical processes such as growth and development, oxidative stress, phytohormone and autophagy. Additionally, the interaction between persulfidation and S-nitrosylation is also discussed. In this work, we provide beneficial clues for further exploration of the molecular mechanism and function of protein persulfidation in plants in the future. Full article
(This article belongs to the Special Issue Plant and Human Sulfur Biology)
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13 pages, 1998 KiB  
Review
Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
by Vivian Kitainda and Joseph M. Jez
Antioxidants 2021, 10(9), 1500; https://doi.org/10.3390/antiox10091500 - 21 Sep 2021
Cited by 6 | Viewed by 3970
Abstract
Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a [...] Read more.
Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a diverse class of natural products. Glucosinolate function stems from their hydrolysis products, which are responsible for the strong flavors of Brassicales plants, such as mustard, and serve as plant defense molecules by repelling insects, fighting fungal infections, and discouraging herbivory. Additionally, certain hydrolysis products such as isothiocyanates can potentially serve as cancer prevention agents in humans. The breadth of glucosinolate function is a result of its great structural diversity, which comes from the use of aliphatic, aromatic and indole amino acids as precursors and elongation of some side chains by up to nine carbons, which, after the formation of the core glucosinolate structure, can undergo further chemical modifications. Aliphatic methionine-derived glucosinolates are the most abundant form of these compounds. Although both elongation and chemical modification of amino acid side chains are important for aliphatic glucosinolate diversity, its elongation process has not been well described at the molecular level. Here, we summarize new insights on the iterative chain-elongation enzymes methylthioalkylmalate synthase (MAMS) and isopropylmalate dehydrogenase (IPMDH). Full article
(This article belongs to the Special Issue Plant and Human Sulfur Biology)
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23 pages, 2061 KiB  
Review
The Impact of H2S on Obesity-Associated Metabolic Disturbances
by Ferran Comas and José María Moreno-Navarrete
Antioxidants 2021, 10(5), 633; https://doi.org/10.3390/antiox10050633 - 21 Apr 2021
Cited by 15 | Viewed by 3718
Abstract
Over the last several decades, hydrogen sulfide (H2S) has gained attention as a new signaling molecule, with extensive physiological and pathophysiological roles in human disorders affecting vascular biology, immune functions, cellular survival, metabolism, longevity, development, and stress resistance. Apart from its [...] Read more.
Over the last several decades, hydrogen sulfide (H2S) has gained attention as a new signaling molecule, with extensive physiological and pathophysiological roles in human disorders affecting vascular biology, immune functions, cellular survival, metabolism, longevity, development, and stress resistance. Apart from its known functions in oxidative stress and inflammation, new evidence has emerged revealing that H2S carries out physiological functions by targeting proteins, enzymes, and transcription factors through a post-translational modification known as persulfidation. This review article provides a critical overview of the current state of the literature addressing the role of H2S in obesity-associated metabolic disturbances, with particular emphasis on its mechanisms of action in obesity, diabetes, non-alcoholic fatty liver disease (NAFLD), and cardiovascular diseases. Full article
(This article belongs to the Special Issue Plant and Human Sulfur Biology)
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