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Antioxidants
Special Issues
H2S in Redox Signaling
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H2S in Redox Signaling

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

Deadline for manuscript submissions: closed (31 December 2018) | Viewed by 16536

Special Issue Editor

Dr. Omer Kabil

E-Mail Website
Guest Editor
ANP Therapeutics, Cambridge MA
Interests: H2S metabolism; H2S signaling; sulfur metabolism; Endoplasmic Reticulum Stress; transsulfuration; Integrated Stress Response; mechanistic enzymology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Hydrogen sulfide (H2S) has emerged as a signaling molecule regulating various cellular and physiological processes important in health and disease. While our understanding of the molecular mechanisms underlying H2S action is hampered by significant gaps, recent findings shed light on its mechanism of action in cellular redox signaling and maintenance of redox homeostasis. H2S reacts with oxidized cysteine residues and metal centers that function as switches in various redox signaling pathways, and also with reactive nitrogen and oxygen species forming reactive intermediates with potential roles in redox signaling. Moreover, H2S regulates key components in antioxidantive pathways and alters cellular ROS levels and provides cytoprotection in various model systems of oxidative stress. A better understanding of H2S role in cellular redox signaling pathways will move the field forward and provide opportunities for therapeutic efforts to treat diseases involving redox imbalance.

This Special Issue welcomes original research papers and reviews to expand our understanding and perspective on all aspects of H2S biochemistry and its role in cellular redox signaling in physiological and pathological processes. Special interests include: mechanistic insight into H2S-signaling including persulfidation, its interaction with transition metals, reactive oxygen and nitrogen species; H2S-induced regulation of mitochondrial energetics, ROS production, thiol redox homeostasis, and antioxidative systems; mechanistic insight into H2S-induced modulation of stress response pathways; and regulation of H2S metabolism and tissue polysulfide pools.

Dr. Omer Kabil
Guest Editor

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
  • Redox regulation
  • H2S signaling
  • Reactive oxygen species (ROS)
  • Reactive nitrogen species (RNS)
  • Persulfidation
  • Glutathione
  • Cysteine
  • Transition Metals
  • Transsulfuration
  • Polysulfide
  • Mitochondria

Published Papers (3 papers)

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Research

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17 pages, 1819 KiB  
Article
Hydroxycobalamin Reveals the Involvement of Hydrogen Sulfide in the Hypoxic Responses of Rat Carotid Body Chemoreceptor Cells
by Teresa Gallego-Martin, Jesus Prieto-Lloret, Philip I. Aaronson, Asuncion Rocher and Ana Obeso
Antioxidants 2019, 8(3), 62; https://doi.org/10.3390/antiox8030062 - 13 Mar 2019
Cited by 5 | Viewed by 3624
Abstract
Carotid body (CB) chemoreceptor cells sense arterial blood PO2, generating a neurosecretory response proportional to the intensity of hypoxia. Hydrogen sulfide (H2S) is a physiological gaseous messenger that is proposed to act as an oxygen sensor in CBs, although [...] Read more.
Carotid body (CB) chemoreceptor cells sense arterial blood PO2, generating a neurosecretory response proportional to the intensity of hypoxia. Hydrogen sulfide (H2S) is a physiological gaseous messenger that is proposed to act as an oxygen sensor in CBs, although this concept remains controversial. In the present study we have used the H2S scavenger and vitamin B12 analog hydroxycobalamin (Cbl) as a new tool to investigate the involvement of endogenous H2S in CB oxygen sensing. We observed that the slow-release sulfide donor GYY4137 elicited catecholamine release from isolated whole carotid bodies, and that Cbl prevented this response. Cbl also abolished the rise in [Ca2+]i evoked by 50 µM NaHS in enzymatically dispersed CB glomus cells. Moreover, Cbl markedly inhibited the catecholamine release and [Ca2+]i rise caused by hypoxia in isolated CBs and dispersed glomus cells, respectively, whereas it did not alter these responses when they were evoked by high [K+]e. The L-type Ca2+ channel blocker nifedipine slightly inhibited the rise in CB chemoreceptor cells [Ca2+]i elicited by sulfide, whilst causing a somewhat larger attenuation of the hypoxia-induced Ca2+ signal. We conclude that Cbl is a useful and specific tool for studying the function of H2S in cells. Based on its effects on the CB chemoreceptor cells we propose that endogenous H2S is an amplifier of the hypoxic transduction cascade which acts mainly by stimulating non-L-type Ca2+ channels. Full article
(This article belongs to the Special Issue H2S in Redox Signaling)
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13 pages, 2239 KiB  
Article
Proteomics and Toxicity Analysis of Spinal-Cord Primary Cultures upon Hydrogen Sulfide Treatment
by Viviana Greco, Alida Spalloni, Victor Corasolla Carregari, Luisa Pieroni, Silvia Persichilli, Nicola B. Mercuri, Andrea Urbani and Patrizia Longone
Antioxidants 2018, 7(7), 87; https://doi.org/10.3390/antiox7070087 - 10 Jul 2018
Cited by 16 | Viewed by 4049
Abstract
Hydrogen sulfide (H2S) is an endogenous gasotransmitter recognized as an essential body product with a dual, biphasic action. It can function as an antioxidant and a cytoprotective, but also as a poison with a high probability of causing brain damage when [...] Read more.
Hydrogen sulfide (H2S) is an endogenous gasotransmitter recognized as an essential body product with a dual, biphasic action. It can function as an antioxidant and a cytoprotective, but also as a poison with a high probability of causing brain damage when present at noxious levels. In a previous study, we measured toxic liquoral levels of H2S in sporadic amyotrophic lateral sclerosis (ALS) patients and in the familial ALS (fALS) mouse model, SOD1G93A. In addition, we experimentally demonstrated that H2S is extremely and selectively toxic to motor neurons, and that it is released by glial cells and increases Ca2+ concentration in motor neurons due to a lack of ATP. The presented study further examines the effect of toxic concentrations of H2S on embryonic mouse spinal-cord cultures. We performed a proteomic analysis that revealed a significant H2S-mediated activation of pathways related to oxidative stress and cell death, particularly the Nrf-2-mediated oxidative stress response and peroxiredoxins. Furthermore, we report that Na2S (a stable precursor of H2S) toxicity is, at least in part, reverted by the Bax inhibitor V5 and by necrostatin, a potent necroptosis inhibitor. Full article
(This article belongs to the Special Issue H2S in Redox Signaling)
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Review

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23 pages, 1179 KiB  
Review
Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species
by Dayana Benchoam, Ernesto Cuevasanta, Matías N. Möller and Beatriz Alvarez
Antioxidants 2019, 8(2), 48; https://doi.org/10.3390/antiox8020048 - 22 Feb 2019
Cited by 75 | Viewed by 8173
Abstract
Hydrogen sulfide (H2S/HS–) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH). Reactions with oxidized thiol products form persulfides (RSSH/RSS [...] Read more.
Hydrogen sulfide (H2S/HS–) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH). Reactions with oxidized thiol products form persulfides (RSSH/RSS–). Persulfides have been proposed to transduce the signaling effects of H2S through the modification of critical cysteines. They are more nucleophilic and acidic than thiols and, contrary to thiols, also possess electrophilic character. In this review, we summarize the biochemistry of hydrogen sulfide and persulfides, focusing on redox aspects. We describe biologically relevant one- and two-electron oxidants and their reactions with H2S and persulfides, as well as the fates of the oxidation products. The biological implications are discussed. Full article
(This article belongs to the Special Issue H2S in Redox Signaling)
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