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S-Glutathionylation in Redox Protein Signaling and Health Outcomes
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S-Glutathionylation in Redox Protein Signaling and Health Outcomes

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 January 2021) | Viewed by 38133

Special Issue Editors

Prof. Sofia Mariotto

E-Mail Website
Guest Editor
Department of Neurosciences, Biomedicine and Movement Sciences, Biological Chemistry Section, Strada le Grazie, 8 37134 Verona, Italy
Interests: protein post-translational modifications; signal transduction; intracellular redox homeostasis; apoptosis; inflammatory response; natural products; cancer cells; microglia-neurons interaction
Dr. Elena Butturini

E-Mail Website
Guest Editor
Department of Neurosciences, Biomedicine and Movement Sciences, Biological Chemistry Section, Strada le Grazie, 8 37134 Verona, Italy
Interests: protein post-translational modifications; signal transduction; intracellular redox homeostasis; apoptosis; inflammatory response; natural products; cancer cells; microglia-neurons interaction

Special Issue Information

Dear Colleagues,

Under oxidative stress, many proteins undergo reversible and irreversible oxidative modifications, which may lead to changes in the structure and/or function of the oxidized protein. These redox-sensitive proteins exhibit a striking differential susceptibility to oxidative stress; while a protein may contain numerous residues, only a minority of them will have the chemical properties to function as a possible target site for oxidants.

S-glutathionylation, the reversible formation of protein mixed disulfides with GSH, represents the most common steady-state derivative due to cellular abundance of GSH.

The importance of S-glutathionylation was initially recognized for its role in protecting proteins from irreversible oxidation; however, more studies indicate that S-glutathionylation is also involved in redox regulation of protein function under physiological and pathological conditions related to oxidative stress. A number of proteins have been reported to undergo glutathionylation, including enzymes, transcription factors, and oncogenes and, as judged by the number of publications in the last years on this topic, further proteins will be identified in the future.

This Special Issue welcomes the submission of original research papers or comprehensive reviews that demonstrate or summarize how the S-glutathionylation influences protein structure/function and biological events, and how these may impact on human diseases.

Prof. Sofia Mariotto
Dr. Elena Butturini
Guest Editors

Manuscript Submission Information

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Keywords

  • S-glutathionylation
  • redox modification
  • protein post-translational modification
  • GSH/GSSH
  • oxidative stress

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Published Papers (5 papers)

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Research

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18 pages, 3712 KiB  
Article
Increased Protein S-Glutathionylation in Leber’s Hereditary Optic Neuropathy (LHON)
by Lei Zhou, James Chun Yip Chan, Stephanie Chupin, Naïg Gueguen, Valérie Desquiret-Dumas, Siew Kwan Koh, Jianguo Li, Yan Gao, Lu Deng, Chandra Verma, Roger W Beuerman, Eric Chun Yong Chan, Dan Milea and Pascal Reynier
Int. J. Mol. Sci. 2020, 21(8), 3027; https://doi.org/10.3390/ijms21083027 - 24 Apr 2020
Cited by 10 | Viewed by 5445
Abstract
Leber’s hereditary optic neuropathy (LHON, MIM#535000) is the most common form of inherited optic neuropathies and mitochondrial DNA-related diseases. The pathogenicity of mutations in genes encoding components of mitochondrial Complex I is well established, but the underlying pathomechanisms of the disease are still [...] Read more.
Leber’s hereditary optic neuropathy (LHON, MIM#535000) is the most common form of inherited optic neuropathies and mitochondrial DNA-related diseases. The pathogenicity of mutations in genes encoding components of mitochondrial Complex I is well established, but the underlying pathomechanisms of the disease are still unclear. Hypothesizing that oxidative stress related to Complex I deficiency may increase protein S-glutathionylation, we investigated the proteome-wide S-glutathionylation profiles in LHON (n = 11) and control (n = 7) fibroblasts, using the GluICAT platform that we recently developed. Glutathionylation was also studied in healthy fibroblasts (n = 6) after experimental Complex I inhibition. The significantly increased reactive oxygen species (ROS) production in the LHON group by Complex I was shown experimentally. Among the 540 proteins which were globally identified as glutathionylated, 79 showed a significantly increased glutathionylation (p < 0.05) in LHON and 94 in Complex I-inhibited fibroblasts. Approximately 42% (33/79) of the altered proteins were shared by the two groups, suggesting that Complex I deficiency was the main cause of increased glutathionylation. Among the 79 affected proteins in LHON fibroblasts, 23% (18/79) were involved in energetic metabolism, 31% (24/79) exhibited catalytic activity, 73% (58/79) showed various non-mitochondrial localizations, and 38% (30/79) affected the cell protein quality control. Integrated proteo-metabolomic analysis using our previous metabolomic study of LHON fibroblasts also revealed similar alterations of protein metabolism and, in particular, of aminoacyl-tRNA synthetases. S-glutathionylation is mainly known to be responsible for protein loss of function, and molecular dynamics simulations and 3D structure predictions confirmed such deleterious impacts on adenine nucleotide translocator 2 (ANT2), by weakening its affinity to ATP/ADP. Our study reveals a broad impact throughout the cell of Complex I-related LHON pathogenesis, involving a generalized protein stress response, and provides a therapeutic rationale for targeting S-glutathionylation by antioxidative strategies. Full article
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
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Review

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16 pages, 4154 KiB  
Review
Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal
by Tsuyoshi Takata, Shoma Araki, Yukihiro Tsuchiya and Yasuo Watanabe
Int. J. Mol. Sci. 2020, 21(22), 8750; https://doi.org/10.3390/ijms21228750 - 19 Nov 2020
Cited by 60 | Viewed by 5438
Abstract
Reactive oxygen species (ROS) are not only harmful to cell survival but also essential to cell signaling through cysteine-based redox switches. In fact, ROS triggers the potential activation of mitogen-activated protein kinases (MAPKs). The 90 kDa ribosomal S6 kinase 1 (RSK1), one of [...] Read more.
Reactive oxygen species (ROS) are not only harmful to cell survival but also essential to cell signaling through cysteine-based redox switches. In fact, ROS triggers the potential activation of mitogen-activated protein kinases (MAPKs). The 90 kDa ribosomal S6 kinase 1 (RSK1), one of the downstream mediators of the MAPK pathway, is implicated in various cellular processes through phosphorylating different substrates. As such, RSK1 associates with and phosphorylates neuronal nitric oxide (NO) synthase (nNOS) at Ser847, leading to a decrease in NO generation. In addition, the RSK1 activity is sensitive to inhibition by reversible cysteine-based redox modification of its Cys223 during oxidative stress. Aside from oxidative stress, nitrosative stress also contributes to cysteine-based redox modification. Thus, the protein kinases such as Ca2+/calmodulin (CaM)-dependent protein kinase I (CaMKI) and II (CaMKII) that phosphorylate nNOS could be potentially regulated by cysteine-based redox modification. In this review, we focus on the role of post-translational modifications in regulating nNOS and nNOS-phosphorylating protein kinases and communication among themselves. Full article
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
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25 pages, 1266 KiB  
Review
Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
by Aysenur Musaogullari and Yuh-Cherng Chai
Int. J. Mol. Sci. 2020, 21(21), 8113; https://doi.org/10.3390/ijms21218113 - 30 Oct 2020
Cited by 67 | Viewed by 10062
Abstract
S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function [...] Read more.
S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases. Full article
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
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18 pages, 2704 KiB  
Review
Redox Regulation of STAT1 and STAT3 Signaling
by Elena Butturini, Alessandra Carcereri de Prati and Sofia Mariotto
Int. J. Mol. Sci. 2020, 21(19), 7034; https://doi.org/10.3390/ijms21197034 - 24 Sep 2020
Cited by 109 | Viewed by 10984
Abstract
STAT1 and STAT3 are nuclear transcription factors that regulate genes involved in cell cycle, cell survival and immune response. The cross-talk between these signaling pathways determines how cells integrate the environmental signals received ultimately translating them in transcriptional regulation of specific sets of [...] Read more.
STAT1 and STAT3 are nuclear transcription factors that regulate genes involved in cell cycle, cell survival and immune response. The cross-talk between these signaling pathways determines how cells integrate the environmental signals received ultimately translating them in transcriptional regulation of specific sets of genes. Despite being activated downstream of common cytokine and growth factors, STAT1 and STAT3 play essentially antagonistic roles and the disruption of their balance directs cells from survival to apoptotic cell death or from inflammatory to anti-inflammatory responses. Different mechanisms are proposed to explain this yin-yang relationship. Considering the redox aspect of STATs proteins, this review attempts to summarize the current knowledge of redox regulation of STAT1 and STAT3 signaling focusing the attention on the post-translational modifications that affect their activity. Full article
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
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18 pages, 1128 KiB  
Review
Role of Glutaredoxin-1 and Glutathionylation in Cardiovascular Diseases
by Mannix Burns, Syed Husain Mustafa Rizvi, Yuko Tsukahara, David R. Pimentel, Ivan Luptak, Naomi M. Hamburg, Reiko Matsui and Markus M. Bachschmid
Int. J. Mol. Sci. 2020, 21(18), 6803; https://doi.org/10.3390/ijms21186803 - 16 Sep 2020
Cited by 29 | Viewed by 5369
Abstract
Cardiovascular diseases are the leading cause of death worldwide, and as rates continue to increase, discovering mechanisms and therapeutic targets become increasingly important. An underlying cause of most cardiovascular diseases is believed to be excess reactive oxygen or nitrogen species. Glutathione, the most [...] Read more.
Cardiovascular diseases are the leading cause of death worldwide, and as rates continue to increase, discovering mechanisms and therapeutic targets become increasingly important. An underlying cause of most cardiovascular diseases is believed to be excess reactive oxygen or nitrogen species. Glutathione, the most abundant cellular antioxidant, plays an important role in the body’s reaction to oxidative stress by forming reversible disulfide bridges with a variety of proteins, termed glutathionylation (GSylation). GSylation can alter the activity, function, and structure of proteins, making it a major regulator of cellular processes. Glutathione-protein mixed disulfide bonds are regulated by glutaredoxins (Glrxs), thioltransferase members of the thioredoxin family. Glrxs reduce GSylated proteins and make them available for another redox signaling cycle. Glrxs and GSylation play an important role in cardiovascular diseases, such as myocardial ischemia and reperfusion, cardiac hypertrophy, peripheral arterial disease, and atherosclerosis. This review primarily concerns the role of GSylation and Glrxs, particularly glutaredoxin-1 (Glrx), in cardiovascular diseases and the potential of Glrx as therapeutic agents. Full article
(This article belongs to the Special Issue S-Glutathionylation in Redox Protein Signaling and Health Outcomes)
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