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Biomolecules
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H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects
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H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (31 March 2020) | Viewed by 57512

Special Issue Editors

Prof. Dr. Noriyuki Nagahara

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Guest Editor
Isotope Research Laboratory, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan
Interests: biochemistry; clinical bichemistry; enzymology; molucular environmental medicine
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Maria Wrobel

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Guest Editor
Chair of Medical Biochemistry, Jagiellonian University Medical College, Kopernika 7 Cracow, 3 1-034 Krakow, Poland
Interests: biochemistry; medical biochemistry; tissue-specific expression and function of sulfurtransferases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We have been studying general aspects of the functions of H2S and polysulfides, and the enzymes involved in their biosynthesis for more than 20 years. Our aim is to elucidate novel physiological and pathological functions of H2S and polysulfides, and unravel the regulation of the enzymes involved in their biosynthesis, including cystathionine β-synthase (EC 4.2.1.22, CBS), cystathionine γ-lyase (EC 4.4.1.1, CSE), thiosulfate sulfurtransferase (EC 2.8.1.1, rhodanese, TST), and 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2, MST).

Aims and scope: We expect this Special Issue to advance scientific knowledge regarding exact functions of H2S and polysulfides, and the general properties and regulation of the enzymes involved in their metabolism.

Topics: We would like to cover four topics—physiological and pathological functions of H2S and polysulfides, mechanisms of the biosynthesis of H2S and polysulfides, properties of the biosynthetic enzymes, and regulation of these enzymes.

Call for papers and guidelines for submission: We encourage scientists who have been studying H2S and polysulfides (mechanisms of biosynthesis, functions, and clinical usage), and related enzymes (structure, reaction mechanisms, and regulation of enzymatic activity) to contribute to this Special Issue. This Special Issue will consider research articles, clinical studies, and reviews, and authors will publish according to the “Author Guidelines” of this journal. We will also consider mini-reviews and perspectives if requested. Papers addressing the properties of H2S and polysulfides, their exact functions, alternative biosynthetic processes, properties of related enzymes, and regulations of enzyme activities are all welcome.

Prof. Dr. Noriyuki Nagahara
Prof. Dr. Maria Wrobel
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. Biomolecules 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 2700 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

  • H2S and polysulfide synthesis
  • physiological and pathological functions
  • biosynthetic enzymes
  • regulation of biosynthetic enzymes

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Published Papers (10 papers)

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Editorial

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8 pages, 276 KiB  
Editorial
H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects
by Noriyuki Nagahara and Maria Wróbel
Biomolecules 2020, 10(4), 640; https://doi.org/10.3390/biom10040640 - 21 Apr 2020
Cited by 9 | Viewed by 3015
Abstract
We have been studying the general aspects of the functions of H2S and polysulfides, and the enzymes involved in their biosynthesis, for more than 20 years. Our aim has been to elucidate novel physiological and pathological functions of H2S [...] Read more.
We have been studying the general aspects of the functions of H2S and polysulfides, and the enzymes involved in their biosynthesis, for more than 20 years. Our aim has been to elucidate novel physiological and pathological functions of H2S and polysulfides, and unravel the regulation of the enzymes involved in their biosynthesis, including cystathionine β-synthase (EC 4.2.1.22), cystathionine γ-lyase (EC 4.4.1.1), thiosulfate sulfurtransferase (rhodanese, EC 2.8.1.1), and 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2). Physiological and pathological functions, alternative biosynthetic processes, and additional functions of H2S and polysulfides have been reported. Further, the structure and reaction mechanisms of related enzymes have also been reported. We expect this issue to advance scientific knowledge regarding the detailed functions of H2S and polysulfides as well as the general properties and regulation of the enzymes involved in their metabolism. We would like to cover four topics: the physiological and pathological functions of H2S and polysulfides, the mechanisms of the biosynthesis of H2S and polysulfides, the properties of the biosynthetic enzymes, and the regulation of enzymatic activity. The knockout mouse technique is a useful tool to determine new physiological functions, especially those of H2S and polysulfides. In the future, we shall take a closer look at symptoms in the human congenital deficiency of each enzyme. Further studies on the regulation of enzymatic activity by in vivo substances may be the key to finding new functions of H2S and polysulfides. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)

Research

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11 pages, 3515 KiB  
Article
Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System
by Noriyuki Nagahara
Biomolecules 2020, 10(6), 826; https://doi.org/10.3390/biom10060826 - 28 May 2020
Cited by 4 | Viewed by 2195
Abstract
Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide [...] Read more.
Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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15 pages, 2041 KiB  
Article
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation and Cellular Bioenergetics in Human Down Syndrome Fibroblasts
by Theodora Panagaki, Elisa B. Randi and Csaba Szabo
Biomolecules 2020, 10(4), 653; https://doi.org/10.3390/biom10040653 - 23 Apr 2020
Cited by 26 | Viewed by 5010
Abstract
Down syndrome (trisomy of human chromosome 21) is a common genetic disorder. Overproduction of the gaseous mediator hydrogen sulfide (H2S) has been implicated in the pathogenesis of neurological and metabolic deficits associated with Down syndrome. Several lines of data indicate that [...] Read more.
Down syndrome (trisomy of human chromosome 21) is a common genetic disorder. Overproduction of the gaseous mediator hydrogen sulfide (H2S) has been implicated in the pathogenesis of neurological and metabolic deficits associated with Down syndrome. Several lines of data indicate that an important enzyme responsible for H2S overproduction in Down syndrome is cystathionine-β-synthase (CBS), an enzyme localized on chromosome 21. The current study explored the possibility that a second H2S-producing enzyme, 3-mercaptopyruvate sulfurtransferase (3-MST), may also contribute to the development of functional deficits of Down syndrome cells. Western blotting analysis demonstrated a significantly higher level of 3-MST protein expression in human Down syndrome fibroblasts compared to cells from healthy control individuals; the excess 3-MST was mainly localized to the mitochondrial compartment. Pharmacological inhibition of 3-MST activity improved mitochondrial electron transport and oxidative phosphorylation parameters (but did not affect the suppressed glycolytic parameters) and enhanced cell proliferation in Down syndrome cells (but not in healthy control cells). The findings presented in the current report suggest that in addition to the indisputable role of CBS, H2S produced from 3-MST may also contribute to the development of mitochondrial metabolic and functional impairments in Down syndrome cells. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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25 pages, 47208 KiB  
Article
Multidirectional Changes in Parameters Related to Sulfur Metabolism in Frog Tissues Exposed to Heavy Metal-Related Stress
by Marta Kaczor-Kamińska, Piotr Sura and Maria Wróbel
Biomolecules 2020, 10(4), 574; https://doi.org/10.3390/biom10040574 - 9 Apr 2020
Cited by 18 | Viewed by 3572
Abstract
The investigations showed changes of the cystathionine γ-lyase (CTH), 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese (TST) activity and gene expression in the brain, heart, liver, kidney, skeletal muscles and testes in frogs Pelophylax ridibundus, Xenopus laevis and Xenopus tropicalis in response to Pb [...] Read more.
The investigations showed changes of the cystathionine γ-lyase (CTH), 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese (TST) activity and gene expression in the brain, heart, liver, kidney, skeletal muscles and testes in frogs Pelophylax ridibundus, Xenopus laevis and Xenopus tropicalis in response to Pb2+, Hg2+ and Cd2+ stress. The results were analyzed jointly with changes in the expression of selected antioxidant enzymes (cytoplasmic and mitochondrial superoxide dismutase, glutathione peroxidase, catalase and thioredoxin reducatase) and with the level of malondialdehyde (a product of lipid peroxidation). The obtained results allowed for confirming the role of sulfurtransferases in the antioxidant protection of tissues exposed to heavy metal ions. Our results revealed different transcriptional responses of the investigated tissues to each of the examined heavy metals. The CTH, MPST and TST genes might be regarded as heavy metal stress-responsive. The CTH gene expression up-regulation was confirmed in the liver (Pb2+, Hg2+, Cd2+) and skeletal muscle (Hg2+), MPST in the brain (Pb2+, Hg2+), kidney (Pb2+, Cd2+), skeletal muscle (Pb2+, Hg2+,Cd2+) and TST in the brain (Pb2+) and kidney (Pb2+, Hg2+, Cd2+). Lead, mercury and cadmium toxicity was demonstrated to affect the glutathione (GSH) and cysteine levels, the concentration ratio of reduced to oxidized glutathione ([GSH]/[GSSG]) and the level of sulfane sulfur-containing compounds, which in case of enhanced reactive oxygen species generation can reveal their antioxidative properties. The present report is the first to widely describe the role of the sulfane sulfur/H2S generating enzymes and the cysteine/glutathione system in Pb2+, Hg2+ and Cd2+ stress in various frog tissues, and to explore the mechanisms mediating heavy metal-related stress. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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20 pages, 3275 KiB  
Article
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation, Migration, and Bioenergetics in Murine Colon Cancer Cells
by Fiona Augsburger, Elisa B. Randi, Mathieu Jendly, Kelly Ascencao, Nahzli Dilek and Csaba Szabo
Biomolecules 2020, 10(3), 447; https://doi.org/10.3390/biom10030447 - 13 Mar 2020
Cited by 47 | Viewed by 5088
Abstract
3-mercaptopyruvate sulfurtransferase (3-MST) has emerged as one of the significant sources of biologically active sulfur species in various mammalian cells. The current study was designed to investigate the functional role of 3-MST’s catalytic activity in the murine colon cancer cell line CT26. The [...] Read more.
3-mercaptopyruvate sulfurtransferase (3-MST) has emerged as one of the significant sources of biologically active sulfur species in various mammalian cells. The current study was designed to investigate the functional role of 3-MST’s catalytic activity in the murine colon cancer cell line CT26. The novel pharmacological 3-MST inhibitor HMPSNE was used to assess cancer cell proliferation, migration and bioenergetics in vitro. Methods included measurements of cell viability (MTT and LDH assays), cell proliferation and in vitro wound healing (IncuCyte) and cellular bioenergetics (Seahorse extracellular flux analysis). 3-MST expression was detected by Western blotting; H2S production was measured by the fluorescent dye AzMC. The results show that CT26 cells express 3-MST protein and mRNA, as well as several enzymes involved in H2S degradation (TST, ETHE1). Pharmacological inhibition of 3-MST concentration-dependently suppressed H2S production and, at 100 and 300 µM, attenuated CT26 proliferation and migration. HMPSNE exerted a bell-shaped effect on several cellular bioenergetic parameters related to oxidative phosphorylation, while other bioenergetic parameters were either unaffected or inhibited at the highest concentration of the inhibitor tested (300 µM). In contrast to 3-MST, the expression of CBS (another H2S producing enzyme which has been previously implicated in the regulation of various biological parameters in other tumor cells) was not detectable in CT26 cells and pharmacological inhibition of CBS exerted no significant effects on CT26 proliferation or bioenergetics. In summary, 3-MST catalytic activity significantly contributes to the regulation of cellular proliferation, migration and bioenergetics in CT26 murine colon cancer cells. The current studies identify 3-MST as the principal source of biologically active H2S in this cell line. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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14 pages, 2492 KiB  
Article
Generation and Characterization of a CRISPR/Cas9—Induced 3-mst Deficient Zebrafish
by Antonia Katsouda, Maria Peleli, Antonia Asimakopoulou, Andreas Papapetropoulos and Dimitris Beis
Biomolecules 2020, 10(2), 317; https://doi.org/10.3390/biom10020317 - 17 Feb 2020
Cited by 7 | Viewed by 3959
Abstract
3-mercaptopyruvate sulfurtransferase (3-MST) is an enzyme capable of synthesizing hydrogen sulfide (H2S) and polysulfides. In spite of its ubiquitous presence in mammalian cells, very few studies have investigated its contribution to homeostasis and disease development, thus the role of 3-MST remains [...] Read more.
3-mercaptopyruvate sulfurtransferase (3-MST) is an enzyme capable of synthesizing hydrogen sulfide (H2S) and polysulfides. In spite of its ubiquitous presence in mammalian cells, very few studies have investigated its contribution to homeostasis and disease development, thus the role of 3-MST remains largely unexplored. Here, we present a clustered, regularly interspaced, short palindromic repeats (CRISPR)/CRISPR–associated protein-9 (Cas9) induced 3-mst mutant zebrafish line, which will allow the study of 3-MST’s role in several biological processes. The 3-mst zebrafish orthologue was identified using a bioinformatic approach and verified by its ability to produce H2S in the presence of 3-mercaptopyruvate (3-MP). Its expression pattern was analyzed during zebrafish early development, indicating predominantly an expression in the heart and central nervous system. As expected, no detectable levels of 3-Mst protein were observed in homozygous mutant larvae. In line with this, H2S levels were reduced in 3-mst−/− zebrafish. Although the mutants showed no obvious morphological deficiencies, they exhibited increased lethality under oxidative stress conditions. The elevated levels of reactive oxygen species, detected following 3-mst deletion, are likely to drive this phenotype. In line with the increased ROS, we observed accelerated fin regenerative capacity in 3-mst deficient zebrafish. Overall, we provide evidence for the expression of 3-mst in zebrafish, confirm its important role in redox homeostasis and indicate the enzyme’s possible involvement in the regeneration processes. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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Review

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13 pages, 2415 KiB  
Review
Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides
by Tomohiro Sawa, Hozumi Motohashi, Hideshi Ihara and Takaaki Akaike
Biomolecules 2020, 10(9), 1245; https://doi.org/10.3390/biom10091245 - 27 Aug 2020
Cited by 45 | Viewed by 5736
Abstract
Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSSnH, n > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that CysSSH and related species such [...] Read more.
Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSSnH, n > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that CysSSH and related species such as glutathione persulfide occur physiologically and are prevalent in prokaryotes, eukaryotes, and mammals in vivo. The chemical properties and abundance of these compounds suggest a central role for reactive persulfides in cell-regulatory processes. CysSSH and related species have been suggested to act as powerful antioxidants and cellular protectants and may serve as redox signaling intermediates. It was recently shown that cysteinyl-tRNA synthetase (CARS) is a new cysteine persulfide synthase. In addition, we discovered that CARS is involved in protein polysulfidation that is coupled with translation. Mitochondrial activity in biogenesis and bioenergetics is supported and upregulated by CysSSH derived from mitochondrial CARS. In this review article, we discuss the mechanisms of the biosynthesis of CysSSH and related persulfide species, with a particular focus on the roles of CARS. We also review the antioxidative and anti-inflammatory actions of persulfides. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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82 pages, 15127 KiB  
Review
Cystathionine-β-synthase: Molecular Regulation and Pharmacological Inhibition
by Karim Zuhra, Fiona Augsburger, Tomas Majtan and Csaba Szabo
Biomolecules 2020, 10(5), 697; https://doi.org/10.3390/biom10050697 - 30 Apr 2020
Cited by 142 | Viewed by 13401
Abstract
Cystathionine-β-synthase (CBS), the first (and rate-limiting) enzyme in the transsulfuration pathway, is an important mammalian enzyme in health and disease. Its biochemical functions under physiological conditions include the metabolism of homocysteine (a cytotoxic molecule and cardiovascular risk factor) and the generation of hydrogen [...] Read more.
Cystathionine-β-synthase (CBS), the first (and rate-limiting) enzyme in the transsulfuration pathway, is an important mammalian enzyme in health and disease. Its biochemical functions under physiological conditions include the metabolism of homocysteine (a cytotoxic molecule and cardiovascular risk factor) and the generation of hydrogen sulfide (H2S), a gaseous biological mediator with multiple regulatory roles in the vascular, nervous, and immune system. CBS is up-regulated in several diseases, including Down syndrome and many forms of cancer; in these conditions, the preclinical data indicate that inhibition or inactivation of CBS exerts beneficial effects. This article overviews the current information on the expression, tissue distribution, physiological roles, and biochemistry of CBS, followed by a comprehensive overview of direct and indirect approaches to inhibit the enzyme. Among the small-molecule CBS inhibitors, the review highlights the specificity and selectivity problems related to many of the commonly used “CBS inhibitors” (e.g., aminooxyacetic acid) and provides a comprehensive review of their pharmacological actions under physiological conditions and in various disease models. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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Graphical abstract

15 pages, 1994 KiB  
Review
Synergisms, Discrepancies and Interactions between Hydrogen Sulfide and Carbon Monoxide in the Gastrointestinal and Digestive System Physiology, Pathophysiology and Pharmacology
by Urszula Głowacka, Tomasz Brzozowski and Marcin Magierowski
Biomolecules 2020, 10(3), 445; https://doi.org/10.3390/biom10030445 - 13 Mar 2020
Cited by 19 | Viewed by 4732
Abstract
Endogenous gas transmitters, hydrogen sulfide (H2S), carbon monoxide (CO) and nitric oxide (NO) are important signaling molecules known to exert multiple biological functions. In recent years, the role of H2S, CO and NO in regulation of cardiovascular, neuronal and [...] Read more.
Endogenous gas transmitters, hydrogen sulfide (H2S), carbon monoxide (CO) and nitric oxide (NO) are important signaling molecules known to exert multiple biological functions. In recent years, the role of H2S, CO and NO in regulation of cardiovascular, neuronal and digestive systems physiology and pathophysiology has been emphasized. Possible link between these gaseous mediators and multiple diseases as well as potential therapeutic applications has attracted great attention from biomedical scientists working in many fields of biomedicine. Thus, various pharmacological tools with ability to release CO or H2S were developed and implemented in experimental animal in vivo and in vitro models of many disorders and preliminary human studies. This review was designed to review signaling functions, similarities, dissimilarities and a possible cross-talk between H2S and CO produced endogenously or released from chemical donors, with special emphasis on gastrointestinal digestive system pathologies prevention and treatment. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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26 pages, 3716 KiB  
Review
Hydrogen Sulfide in Pharmacotherapy, Beyond the Hydrogen Sulfide-Donors
by Ewelina Zaorska, Lenka Tomasova, Dominik Koszelewski, Ryszard Ostaszewski and Marcin Ufnal
Biomolecules 2020, 10(2), 323; https://doi.org/10.3390/biom10020323 - 18 Feb 2020
Cited by 78 | Viewed by 9678
Abstract
Hydrogen sulfide (H2S) is one of the important biological mediators involved in physiological and pathological processes in mammals. Recently developed H2S donors show promising effects against several pathological processes in preclinical and early clinical studies. For example, H2 [...] Read more.
Hydrogen sulfide (H2S) is one of the important biological mediators involved in physiological and pathological processes in mammals. Recently developed H2S donors show promising effects against several pathological processes in preclinical and early clinical studies. For example, H2S donors have been found to be effective in the prevention of gastrointestinal ulcers during anti-inflammatory treatment. Notably, there are well-established medicines used for the treatment of a variety of diseases, whose chemical structure contains sulfur moieties and may release H2S. Hence, the therapeutic effect of these drugs may be partly the result of the release of H2S occurring during drug metabolism and/or the effect of these drugs on the production of endogenous hydrogen sulfide. In this work, we review data regarding sulfur drugs commonly used in clinical practice that can support the hypothesis about H2S-dependent pharmacotherapeutic effects of these drugs. Full article
(This article belongs to the Special Issue H2S, Polysulfides, and Enzymes: Physiological and Pathological Aspects)
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