Cellular Sulfur Metabolism and Signaling in Physiology and Pathology

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

Deadline for manuscript submissions: closed (30 November 2023) | Viewed by 2316

Special Issue Editors

Department of Medical Biochemistry, Jagiellonian University Medical College, 31-008 Krakow, Poland
Interests: sulfane sulfur; hydrogen sulfide; sulfurtransferases; oxidoreductases; metabolism of amino acids; biochemistry and pharmacology of lipoic acid
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The Chair of Medical Biochemistry, Jagiellonian University Medical College, 31-008 Krakow, Poland
Interests: sulfane sulfur; hydrogen sulfide; sulfurtransferases; glutathione; thiol redox regulation; S-sulfhydration
Special Issues, Collections and Topics in MDPI journals
Chair of Medical Biochemistry Jagiellonian University Medical College, Swietej Anny 12, 31-008 Krakow
Interests: sulfur biochemistry and chemistry; sulfane sulfur; L-cysteine metabolism; sulfurtransferases; low-molecular-weight antioxidants; heparan sulfate; mucopolysaccharidosis

Special Issue Information

Dear Colleagues,

Sulfur is an element widespread in nature. It is present in the cells of all living organisms in various oxidation states: from -2 to +6. Methionine and cysteine contain sulfur in its lowest oxidation state (-2). The sulfur atom present in sulfhydryl groups of low molecular weight compounds is at a low oxidation state and can protect other compounds form oxygen toxicity and radiation damage. This is possible because sulfhydryl groups are involved in numerous redox reactions due to their ease of oxidation. Reduced sulfur is employed in the activation of substrates in some catalytic molecules and cofactors, such as biotin, coenzymes: A, B, M, glutathione, ferredoxins and other iron-sulfur proteins, molybdenum cofactor, lipoic acid, and thiamine phosphate. At higher oxidation states, sulfur occurs as sulfates (SO42-; 6+) and sulfonates (RSO3-; 4+) which are components of sulfur-containing macromolecules, such as sulfatides and sulfate polysaccharides—major constituents of extracellular structures. The products of the oxidation of the reduced sulfur-containing compounds into higher oxidations states are reactive sulfur species (RSS). Recent discoveries characterize RSS as key players in redox regulation as important as reactive oxygen (ROS) and nitrogen (RNS) species. Examples of RSS include persulfides (RSSH, -1), polysulfides (RS(S)nH; 0), and thiosulfate (S2O32-; +2). Persulfides and polysulfides are oxidation products of hydrogen sulfide (H2S; -2) and they contain one or more sulfur atoms at the zero oxidation state called sulfane sulfur (S; 0). According to some researchers, the definition of RSS is much broader and includes small-molecule biological thiols, such as glutathione, cysteine, homocysteine, and H2S. It is worth mentioning that S-nitrosothiols (RSNO) are also defined as RSS. However, the chemical nature of RSS is complex and remains poorly understood within various pathophysiological conditions. Thus, it seems likely that the presence of other chemical intermediates or derivatives of sulfide may mediate many biological functions. A wide range of sulfide metabolites are produced by sulfur-containing amino acids metabolism via transsulfuration enzymes, such as cystathionine β-synthase (EC 4.2.1.22, CBS) and cystathionine γ-lyase (EC 4.4.1.1, CSE). Moreover, numerous in vitro and in vivo studies indicate that sulfur-containing compounds have great therapeutic potential, and when used supportively, have a positive effect on the treatment of cardiovascular diseases, neurological deficits, metabolic syndrome, disorders of the immune system, and cancer.

In the current Special Issue of Antioxidants, we welcome original research papers and reviews focused on the biological role of sulfur and sulfur-containing compounds in living organisms, the impact of these compounds on changes in sulfur amino acids metabolism, and pathologies resulting from its dysregulation. New therapeutic approaches and strategies are also welcome. Papers that involve studies with humans, animals, plants, bacteria or cell lines can be published. Papers containing new analytical methods for the determination of sulfur compounds in biological samples will also be considered.

Dr. Anna Bilska-Wilkosz
Dr. Małgorzata B. Iciek
Dr. Marta Kaczor-Kaminska
Guest Editors

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Published Papers (2 papers)

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Research

19 pages, 3957 KiB  
Article
Selenium Compounds Affect Differently the Cytoplasmic Thiol/Disulfide State in Dermic Fibroblasts and Improve Cell Migration by Interacting with the Extracellular Matrix
by Christine Kreindl, Sandra A. Soto-Alarcón, Miltha Hidalgo, Ana L. Riveros, Carolina Añazco, Rodrigo Pulgar and Omar Porras
Antioxidants 2024, 13(2), 159; https://doi.org/10.3390/antiox13020159 - 26 Jan 2024
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Abstract
Deficient wound healing is frequently observed in patients diagnosed with diabetes, a clinical complication that compromises mobility and leads to limb amputation, decreasing patient autonomy and family lifestyle. Fibroblasts are crucial for secreting the extracellular matrix (ECM) to pave the wound site for [...] Read more.
Deficient wound healing is frequently observed in patients diagnosed with diabetes, a clinical complication that compromises mobility and leads to limb amputation, decreasing patient autonomy and family lifestyle. Fibroblasts are crucial for secreting the extracellular matrix (ECM) to pave the wound site for endothelial and keratinocyte regeneration. The biosynthetic pathways involved in collagen production and crosslinking are intimately related to fibroblast redox homeostasis. In this study, two sets of human dermic fibroblasts were cultured in normal (5 mM) and high (25 mM)-glucose conditions in the presence of 1 µM selenium, as sodium selenite (inorganic) and the two selenium amino acids (organic), Se-cysteine and Se-methionine, for ten days. We investigated the ultrastructural changes in the secreted ECM induced by these conditions using scanning electron microscopy (SEM). In addition, we evaluated the redox impact of these three compounds by measuring the basal state and real-time responses of the thiol-based HyPer biosensor expressed in the cytoplasm of these fibroblasts. Our results indicate that selenium compound supplementation pushed the redox equilibrium towards a more oxidative tone in both sets of fibroblasts, and this effect was independent of the type of selenium. The kinetic analysis of biosensor responses allowed us to identify Se-cysteine as the only compound that simultaneously improved the sensitivity to oxidative stimuli and augmented the disulfide bond reduction rate in high-glucose-cultured fibroblasts. The redox response profiles showed no clear association with the ultrastructural changes observed in matrix fibers secreted by selenium-treated fibroblasts. However, we found that selenium supplementation improved the ECM secreted by high-glucose-cultured fibroblasts according to endothelial migration assessed with a wound healing assay. Direct application of sodium selenite and Se-cysteine on purified collagen fibers subjected to glycation also improved cellular migration, suggesting that these selenium compounds avoid the undesired effect of glycation. Full article
(This article belongs to the Special Issue Cellular Sulfur Metabolism and Signaling in Physiology and Pathology)
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17 pages, 1899 KiB  
Article
The Rhodanese PspE Converts Thiosulfate to Cellular Sulfane Sulfur in Escherichia coli
by Qiaoli Yu, Mingxue Ran, Yuping Xin, Huaiwei Liu, Honglei Liu, Yongzhen Xia and Luying Xun
Antioxidants 2023, 12(5), 1127; https://doi.org/10.3390/antiox12051127 - 20 May 2023
Cited by 1 | Viewed by 1323
Abstract
Hydrogen sulfide (H2S) and its oxidation product zero-valent sulfur (S0) play important roles in animals, plants, and bacteria. Inside cells, S0 exists in various forms, including polysulfide and persulfide, which are collectively referred to as sulfane sulfur. Due [...] Read more.
Hydrogen sulfide (H2S) and its oxidation product zero-valent sulfur (S0) play important roles in animals, plants, and bacteria. Inside cells, S0 exists in various forms, including polysulfide and persulfide, which are collectively referred to as sulfane sulfur. Due to the known health benefits, the donors of H2S and sulfane sulfur have been developed and tested. Among them, thiosulfate is a known H2S and sulfane sulfur donor. We have previously reported that thiosulfate is an effective sulfane sulfur donor in Escherichia coli; however, it is unclear how it converts thiosulfate to cellular sulfane sulfur. In this study, we showed that one of the various rhodaneses, PspE, in E. coli was responsible for the conversion. After the thiosulfate addition, the ΔpspE mutant did not increase cellular sulfane sulfur, but the wild type and the complemented strain ΔpspE::pspE increased cellular sulfane sulfur from about 92 μM to 220 μM and 355 μM, respectively. LC-MS analysis revealed a significant increase in glutathione persulfide (GSSH) in the wild type and the ΔpspE::pspE strain. The kinetic analysis supported that PspE was the most effective rhodanese in E. coli in converting thiosulfate to glutathione persulfide. The increased cellular sulfane sulfur alleviated the toxicity of hydrogen peroxide during E. coli growth. Although cellular thiols might reduce the increased cellular sulfane sulfur to H2S, increased H2S was not detected in the wild type. The finding that rhodanese is required to convert thiosulfate to cellular sulfane sulfur in E. coli may guide the use of thiosulfate as the donor of H2S and sulfane sulfur in human and animal tests. Full article
(This article belongs to the Special Issue Cellular Sulfur Metabolism and Signaling in Physiology and Pathology)
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