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Antioxidants
Special Issues
Modifications of Cysteine Proteins Redox Status in Cell Signalling
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Modifications of Cysteine Proteins Redox Status in Cell Signalling

A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Aberrant Oxidation of Biomolecules".

Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 11754

Special Issue Editor

Prof. Dr. Antonella Del Corso

E-Mail Website
Guest Editor
Biochemistry Unit, Department of Biology, University of Pisa, 56126 Pisa, Italy
Interests: oxidative stress; protein thiolation; carbonyl metabolism; enzyme inhibition; diabetic complications; drug discovery
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

A huge number of proteins, including enzymes, transcription factors and cytoskeletal proteins, may undergo changes in the redox status of their cysteines. These modifications, including glutathionylation (and the more general thiolation), often lead to stable protein-mixed disulphides or to a rearrangement into intra/intermolecular disulphides. Although the first evidence of protein-mixed disulphides dates back to the 1980s, exactly how they are generated is still not clear and, consequently, whether reduced or oxidized glutathione is involved. In addition, there is increasing evidence that proteins may contain cysteine in different oxidation states, such as cysteine sulphenic and sulphinic acid (through the occurrence of sulphenylation and sulphinylation processes, respectively), and that these modifications are reversible. In fact, specific catalysts of de-modification events, such as glutaredoxins for the reverse of glutathionylation and sulfiredoxins for the reverse of sulphenylation and sulphinylation, have been described. This evidence, together with the fact that such post-translational modifications often result in alterations of the functional properties of target proteins, strongly suggests that they may have a regulatory role. Along with the increase in experimental evidence, these proposals have been refined over the years and we are now at the point of a fascinating concept: the cellular “thiolstat”. This is based on the assumption that the different redox states observed for cysteine proteins may represent sensors for different extents of oxidative stress, which are consequently able to affect cell fate. However, the factors that play a role in promoting/catalyzing or hindering these modifications and de-modifications are still not fully clear and neither is the extent of reversibility or the actual significance of these modifications in terms of cell signaling.

We invite authors to contribute, with research articles or reviews, to shed light on the above points. Thus, this Special Issue welcomes submissions on all aspects related to modifications in the redox status of cysteine proteins, including (but not limited to) their role and occurrence in diseases, the characterization of enzymes able to catalyze both the modification and the de-modification steps, and the methodological approaches for detecting their occurrence.

Prof. Antonella Del Corso
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

  • Cysteine redox status
  • Glutathionylation
  • Thiolation
  • Protein-mixed disulphides
  • Sulfenylation
  • Sulphinylation
  • Glutaredoxin
  • Sulfiredoxin

Published Papers (3 papers)

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Review

22 pages, 682 KiB  
Review
Biological Mechanisms of S-Nitrosothiol Formation and Degradation: How Is Specificity of S-Nitrosylation Achieved?
by Christopher M. Massa, Ziping Liu, Sheryse Taylor, Ashley P. Pettit, Marena N. Stakheyeva, Elena Korotkova, Valentina Popova, Elena N. Atochina-Vasserman and Andrew J. Gow
Antioxidants 2021, 10(7), 1111; https://doi.org/10.3390/antiox10071111 - 12 Jul 2021
Cited by 13 | Viewed by 3416
Abstract
The modification of protein cysteine residues underlies some of the diverse biological functions of nitric oxide (NO) in physiology and disease. The formation of stable nitrosothiols occurs under biologically relevant conditions and time scales. However, the factors that determine the selective nature of [...] Read more.
The modification of protein cysteine residues underlies some of the diverse biological functions of nitric oxide (NO) in physiology and disease. The formation of stable nitrosothiols occurs under biologically relevant conditions and time scales. However, the factors that determine the selective nature of this modification remain poorly understood, making it difficult to predict thiol targets and thus construct informatics networks. In this review, the biological chemistry of NO will be considered within the context of nitrosothiol formation and degradation whilst considering how specificity is achieved in this important post-translational modification. Since nitrosothiol formation requires a formal one-electron oxidation, a classification of reaction mechanisms is proposed regarding which species undergoes electron abstraction: NO, thiol or S-NO radical intermediate. Relevant kinetic, thermodynamic and mechanistic considerations will be examined and the impact of sources of NO and the chemical nature of potential reaction targets is also discussed. Full article
(This article belongs to the Special Issue Modifications of Cysteine Proteins Redox Status in Cell Signalling)
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18 pages, 366 KiB  
Review
Peroxiredoxins—The Underrated Actors during Virus-Induced Oxidative Stress
by Inna L. Karpenko, Vladimir T. Valuev-Elliston, Olga N. Ivanova, Olga A. Smirnova and Alexander V. Ivanov
Antioxidants 2021, 10(6), 977; https://doi.org/10.3390/antiox10060977 - 18 Jun 2021
Cited by 15 | Viewed by 3251
Abstract
Enhanced production of reactive oxygen species (ROS) triggered by various stimuli, including viral infections, has attributed much attention in the past years. It has been shown that different viruses that cause acute or chronic diseases induce oxidative stress in infected cells and dysregulate [...] Read more.
Enhanced production of reactive oxygen species (ROS) triggered by various stimuli, including viral infections, has attributed much attention in the past years. It has been shown that different viruses that cause acute or chronic diseases induce oxidative stress in infected cells and dysregulate antioxidant its antioxidant capacity. However, most studies focused on catalase and superoxide dismutases, whereas a family of peroxiredoxins (Prdx), the most effective peroxide scavengers, were given little or no attention. In the current review, we demonstrate that peroxiredoxins scavenge hydrogen and organic peroxides at their physiological concentrations at various cell compartments, unlike many other antioxidant enzymes, and discuss their recycling. We also provide data on the regulation of their expression by various transcription factors, as they can be compared with the imprint of viruses on transcriptional machinery. Next, we discuss the involvement of peroxiredoxins in transferring signals from ROS on specific proteins by promoting the oxidation of target cysteine groups, as well as briefly demonstrate evidence of nonenzymatic, chaperone, functions of Prdx. Finally, we give an account of the current state of research of peroxiredoxins for various viruses. These data clearly show that Prdx have not been given proper attention despite all the achievements in general redox biology. Full article
(This article belongs to the Special Issue Modifications of Cysteine Proteins Redox Status in Cell Signalling)
23 pages, 3192 KiB  
Review
Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations
by Nicholas J. Day, Matthew J. Gaffrey and Wei-Jun Qian
Antioxidants 2021, 10(3), 499; https://doi.org/10.3390/antiox10030499 - 23 Mar 2021
Cited by 18 | Viewed by 4156
Abstract
Post-translational modifications regulate the structure and function of proteins that can result in changes to the activity of different pathways. These include modifications altering the redox state of thiol groups on protein cysteine residues, which are sensitive to oxidative environments. While mass spectrometry [...] Read more.
Post-translational modifications regulate the structure and function of proteins that can result in changes to the activity of different pathways. These include modifications altering the redox state of thiol groups on protein cysteine residues, which are sensitive to oxidative environments. While mass spectrometry has advanced the identification of protein thiol modifications and expanded our knowledge of redox-sensitive pathways, the quantitative aspect of this technique is critical for the field of redox proteomics. In this review, we describe how mass spectrometry-based redox proteomics has enabled researchers to accurately quantify the stoichiometry of reversible oxidative modifications on specific cysteine residues of proteins. We will describe advancements in the methodology that allow for the absolute quantitation of thiol modifications, as well as recent reports that have implemented this approach. We will also highlight the significance and application of such measurements and why they are informative for the field of redox biology. Full article
(This article belongs to the Special Issue Modifications of Cysteine Proteins Redox Status in Cell Signalling)
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