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Antioxidants
Special Issues
Methionine Sulfoxide Reductases and Oxidative Damage
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Methionine Sulfoxide Reductases and Oxidative Damage

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

Deadline for manuscript submissions: closed (31 August 2018) | Viewed by 28688

Special Issue Editors

Dr. Herbert Weissbach

E-Mail Website
Guest Editor
Center for Molecular Biology and Biotechnology, Florida Atlantic University, Jupiter, FL, USA
Interests: methionine sulfoxide reductases; oxidative damage; cellular protective mechanisms
Dr. Nathan Brot

E-Mail Website
Guest Editor
Florida Atlantic University, Center for Molecular Biology and Biotechnology, Jupiter, FL, USA
Interests: effects of methionine oxidation in proteins
Dr. Shailaja Kesaraju Allani

E-Mail Website
Guest Editor
Center for Molecular Biology and Biotechnology, Florida Atlantic University, Jupiter, FL, USA
Interests: oxidative damage; cancer; age-related diseases; drug development

Special Issue Information

Dear Colleagues,

Oxidative damage is one of the hallmarks of aging and age-related diseases. Oxidative damage occurs due to an altered balance between reactive oxygen species (ROS) production and the level of the cellular protective mechanisms. One of the cellular repair mechanisms that protects oxidative damage to proteins is the methionine sulfoxide reductase system (Msr). In mammalian cells the Msr system reduces oxidized methionine residues (Met(O)) present in proteins back to methionine. Further, the Msr system also functions to scavenge ROS by permitting methionine residues in proteins to function as catalytic antioxidants. Bacterial and animal cells lacking MsrA, and MsrA knockout mice, have been shown to be more sensitive to oxidative stress. Conversely, over-expression of MsrA renders cells more resistant to oxidative stress and MsrA overexpression in transgenic Drosophila, results in an increase in life span of the animals.

The goal of this special issue is to publish original research and review articles studying the role of the Msr system in cells. Manuscripts in all areas related to Msr will be considered including the following topics: (1) the possible role of methionine oxidation and the Msr system in age related diseases, (2) activators of the Msr enzymes, (3) the regulation of protein function by methionine oxidation and reduction, (4) Msr as a target for cancer therapy and (5) the role of Msr system in pathogen virulence.

Dr. Herbert Weissbach
Dr. Nathan Brot
Dr. Shailaja Kesaraju Allani
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. 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

  • Methionine oxidation
  • Oxidative damage
  • Aging and age-related diseases
  • Cellular protective mechanisms

Published Papers (6 papers)

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Research

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18 pages, 3542 KiB  
Article
In Vivo Effects of Methionine Sulfoxide Reductase Deficiency in Drosophila melanogaster
by Lindsay Bruce, Diana Singkornrat, Kelsey Wilson, William Hausman, Kelli Robbins, Lingxi Huang, Katie Foss and David Binninger
Antioxidants 2018, 7(11), 155; https://doi.org/10.3390/antiox7110155 - 01 Nov 2018
Cited by 6 | Viewed by 3572
Abstract
The deleterious alteration of protein structure and function due to the oxidation of methionine residues has been studied extensively in age-associated neurodegenerative disorders such as Alzheimer’s and Parkinson’s Disease. Methionine sulfoxide reductases (MSR) have three well-characterized biological functions. The most commonly studied function [...] Read more.
The deleterious alteration of protein structure and function due to the oxidation of methionine residues has been studied extensively in age-associated neurodegenerative disorders such as Alzheimer’s and Parkinson’s Disease. Methionine sulfoxide reductases (MSR) have three well-characterized biological functions. The most commonly studied function is the reduction of oxidized methionine residues back into functional methionine thus, often restoring biological function to proteins. Previous studies have successfully overexpressed and silenced MSR activity in numerous model organisms correlating its activity to longevity and oxidative stress. In the present study, we have characterized in vivo effects of MSR deficiency in Drosophila. Interestingly, we found no significant phenotype in animals lacking either methionine sulfoxide reductase A (MSRA) or methionine sulfoxide reductase B (MSRB). However, Drosophila lacking any known MSR activity exhibited a prolonged larval third instar development and a shortened lifespan. These data suggest an essential role of MSR in key biological processes. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
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16 pages, 5677 KiB  
Article
Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior
by Méry Marimoutou, Danielle A. Springer, Chengyu Liu, Geumsoo Kim and Rodney L. Levine
Antioxidants 2018, 7(10), 140; https://doi.org/10.3390/antiox7100140 - 13 Oct 2018
Cited by 9 | Viewed by 3552
Abstract
Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown. We therefore created a mutant mouse in which wild type calmodulin-1 was replaced by a calmodulin containing a [...] Read more.
Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown. We therefore created a mutant mouse in which wild type calmodulin-1 was replaced by a calmodulin containing a mimic of methionine sulfoxide at residue 77. Total calmodulin levels were unchanged in the homozygous M77Q mutant, which is viable and fertile. No differences were observed on learning tests, including the Morris water maze and associative learning. Cardiac stress test results were also the same for mutant and wild type mice. However, young male and female mice were 20% smaller than wild type mice, although food intake was normal for their weight. Young M77Q mice were notably more active and exploratory than wild type mice. This behavior difference was objectively documented on the treadmill and open field tests. The mutant mice ran 20% longer on the treadmill than controls and in the open field test, the mutant mice explored more than controls and exhibited reduced anxiety. These phenotypic differences bore a similarity to those observed in mice lacking calcium/calmodulin kinase IIα (CaMKIIα). We then showed that MetO77 calmodulin was less effective in activating CaMKIIα than wild type calmodulin. Thus, characterization of the phenotype of a mouse expressing a constitutively active mimic of calmodulin led to the identification of the first calmodulin target that can be differentially regulated by the oxidation state of Met77. We conclude that reversible oxidation of methionine 77 in calmodulin by MSRA has the potential to regulate cellular function. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
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Review

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11 pages, 2565 KiB  
Review
Molecular Mechanisms of the Methionine Sulfoxide Reductase System from Neisseria meningitidis
by Sandrine Boschi-Muller
Antioxidants 2018, 7(10), 131; https://doi.org/10.3390/antiox7100131 - 01 Oct 2018
Cited by 11 | Viewed by 3169
Abstract
Neisseria meningitidis, an obligate pathogenic bacterium in humans, has acquired different defense mechanisms to detect and fight the oxidative stress generated by the host’s defense during infection. A notable example of such a mechanism is the PilB reducing system, which repairs oxidatively-damaged [...] Read more.
Neisseria meningitidis, an obligate pathogenic bacterium in humans, has acquired different defense mechanisms to detect and fight the oxidative stress generated by the host’s defense during infection. A notable example of such a mechanism is the PilB reducing system, which repairs oxidatively-damaged methionine residues. This review will focus on the catalytic mechanism of the two methionine sulfoxide reductase (MSR) domains of PilB, which represent model enzymes for catalysis of the reduction of a sulfoxide function by thiols through sulfenic acid chemistry. The mechanism of recycling of these MSR domains by various “Trx-like” disulfide oxidoreductases will also be discussed. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
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10 pages, 247 KiB  
Review
The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria
by Vineet K. Singh, Kuldeep Singh and Kyle Baum
Antioxidants 2018, 7(10), 128; https://doi.org/10.3390/antiox7100128 - 28 Sep 2018
Cited by 35 | Viewed by 3920
Abstract
Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics. Later studies identified the presence of two additional MSRA proteins (MSRA2 and MSRA3) in S. aureus. These MSR proteins have been characterized in many [...] Read more.
Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics. Later studies identified the presence of two additional MSRA proteins (MSRA2 and MSRA3) in S. aureus. These MSR proteins have been characterized in many other bacteria as well. This review provides the current knowledge about the conditions and regulatory network that mimic the expression of these MSR encoding genes and their role in defense from oxidative stress and virulence. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
12 pages, 1935 KiB  
Review
Methionine Sulfoxide Reductases of Archaea
by Julie A. Maupin-Furlow
Antioxidants 2018, 7(10), 124; https://doi.org/10.3390/antiox7100124 - 20 Sep 2018
Cited by 16 | Viewed by 6861
Abstract
Methionine sulfoxide reductases are found in all domains of life and are important in reversing the oxidative damage of the free and protein forms of methionine, a sulfur containing amino acid particularly sensitive to reactive oxygen species (ROS). Archaea are microbes of a [...] Read more.
Methionine sulfoxide reductases are found in all domains of life and are important in reversing the oxidative damage of the free and protein forms of methionine, a sulfur containing amino acid particularly sensitive to reactive oxygen species (ROS). Archaea are microbes of a domain of life distinct from bacteria and eukaryotes. Archaea are well known for their ability to withstand harsh environmental conditions that range from habitats of high ROS, such as hypersaline lakes of intense ultraviolet (UV) radiation and desiccation, to hydrothermal vents of low concentrations of dissolved oxygen at high temperature. Recent evidence reveals the methionine sulfoxide reductases of archaea function not only in the reduction of methionine sulfoxide but also in the ubiquitin-like modification of protein targets during oxidative stress, an association that appears evolutionarily conserved in eukaryotes. Here is reviewed methionine sulfoxide reductases and their distribution and function in archaea. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
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9 pages, 407 KiB  
Review
The Functions of the Mammalian Methionine Sulfoxide Reductase System and Related Diseases
by Beichen Jiang and Jackob Moskovitz
Antioxidants 2018, 7(9), 122; https://doi.org/10.3390/antiox7090122 - 18 Sep 2018
Cited by 41 | Viewed by 6480
Abstract
This review article describes and discusses the current knowledge on the general role of the methionine sulfoxide reductase (MSR) system and the particular role of MSR type A (MSRA) in mammals. A powerful tool to investigate the contribution of MSRA to molecular processes [...] Read more.
This review article describes and discusses the current knowledge on the general role of the methionine sulfoxide reductase (MSR) system and the particular role of MSR type A (MSRA) in mammals. A powerful tool to investigate the contribution of MSRA to molecular processes within a mammalian system/organism is the MSRA knockout. The deficiency of MSRA in this mouse model provides hints and evidence for this enzyme function in health and disease. Accordingly, the potential involvement of MSRA in the processes leading to neurodegenerative diseases, neurological disorders, cystic fibrosis, cancer, and hearing loss will be deliberated and evaluated. Full article
(This article belongs to the Special Issue Methionine Sulfoxide Reductases and Oxidative Damage)
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