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Alzheimer's disease's brain is prone to a significant oxidative attack by reactive oxygen species that can result in methionine oxidation. Oxidation of beta-amyloid's sole methionine residues of other extracellular proteins, as well as other inflammatory proteins in vivo may be one of the first events contributing to A and other proteins' toxicity in vivo. We immunized transgenic AD mice at 4 months of age with a recombinant methionine sulfoxide-rich protein from Zea mays, according to the current study. These results, which were obtained in a preclinical AD model, are likely translational, and they indicate that injecting active immunization may prolong or prevent AD onset.
Source link: https://doi.org/10.3390/antiox11040775
Selenium is a chemical component of the synthesis of selenocysteine residues that play a vital role in selenoproteine's enzymatic activity efficiencies. The methionine sulfoxide reductase system that converts methionine sulfoxide to methionine comprises the selenoprotein MsrB and non-selenoprotein MsrA, which respectively decrease MetO's R- and S- forms of MetO.
Source link: https://doi.org/10.3390/molecules14072337
Covalent modifications of methionine residues giving methionine sulfoxide have caused a major loss to ROS to proteins, which has resulted in ROS' failures. After oxidative damage, Methionine sulfoxide reductases are enzymes that can regenerate methionine and restore protein structure. In Bacillus subtilis, we identified the methionine sulfoxide reductase genes msrA and msrB, resulting in an operon transcribed from a single sigma A-dependent promoter. An spx deletion mutant with PQ was extremely sensitive to PQ, and an increased amount of msrA has been found in a clpX mutant in which Spx accumulated, supporting this finding. The Spx effect was also apparent under conditions where the protein did not accumulate, indicating a specific molecular function at the Spx protein level. Conclusion According to B. subtilis, Spx mediated PQ-specific regulatory pathway of the msrAB operon.
Source link: https://doi.org/10.1186/1471-2180-8-128
Insulin dysregulation in horses is a metabolic disorder characterized by elevated insulin levels in the blood and peripheral insulin resistance. However, we currently lack detailed information about the potential involvement of particular metabolic pathways in pathophysiological mechanisms and effects of equine insulin dysregulation. This report sought to investigate novel metabolites related to insulin dysregulation by a targeted metabolomics approach in insulin-sensitive and insulin-dysregulated horses. Oral glucose testing triggered changes in serum insulin and plasma glucose levels compared to baseline and stimulated conditions after 180 min. Conclusion orally glucose supplementation in horses during OGT resulted in dramatic metabolic and proinflammatory changes. Insulin dysregulation has been detected in basal samples by enzymes related to trans-hydroxyproline and methionine sulfoxide, implying that metabolic stress and oxidant–antioxidant disequilibrium are contributing factors to insulin dysregulation.
Source link: https://doi.org/10.1186/s12917-018-1479-z
Met sulfoxide is reduced back to Met by methionine sulfoxide reductases A and B, respectively, due to the synthesis of two S- and R-diastemidomers of Met sulfoxide. Plant MSRs could help maintain the stability of stress sensitive effectors such as glutathione-S-transferases and chaperones in addition to a global defense role against oxidative damage in proteins. Moreover, multiple lines of evidence show that MSRs play key signaling functions by interplaying with Ca2+- and phosphorylation-dependent cascades, thus conveying ROS-related results in transduction pathways.
Source link: https://doi.org/10.3390/antiox7090114
Methionine sulfoxide reductases are present in virtually all domains of life and are instrumental in preventing the oxidative damage of the free and protein forms of methionine, a sulfur-containing amino acid particularly susceptible to reactive oxygen species. The methionine sulfoxide reductases of archaea are not limited to methionine sulfoxide reduction but also in the ubiquitin-like modification of protein targets under oxidative stress, which seems to have been conserved in eukaryotes, according to new results.
Source link: https://doi.org/10.3390/antiox7100124
Methionine can be reversibly oxidized to methionine sulfoxide under physiological conditions. Organisms evolved two specific methionine sulfoxide reductase families to restore oxidized methionine residues. MSRB activity toward protein-based MetO with either DTT or thioredoxin as reducetants was shown by MSRB, although GmMSRB1 was only active with DTT. Plants evolved MSRBs for the reduction of both free and protein-based MetO, together, show that, in comparison to mammals that cannot reduce free Met-R-O and microorganisms that use fRMSR for this purpose, plants evolved MSRBs for the reduction of both free and protein-based MetO.
Source link: https://doi.org/10.1371/journal.pone.0065637
Met sulfoxide can be converted into Met sulfoxide, which can be converted into proteins. MetO is reduced by the ubiquitous methionine sulfoxide reductases A and B. MetO reductases were shown to reduce MetO within proteins, but their ability to reduce MetO within proteins was unknown. Organisms use enzymatic methods that have yet to be discovered to control protein oxidation states, as shown by the discovery of this fourth type of enzyme that can reduce MetO in proteins, which have been conserved in proteobacteria and actinobacteria.
Source link: https://doi.org/10.3390/antiox9070616
Due to the emergence of multidrug resistant strains of Neisseria gonorrhoeae, a big public health issue is being tackled, and there is urgent need for novel therapies or a vaccine to avoid gonococcal disease. We analyzed methionine sulfoxide reductase of N. gonorrhoeae as a potential vaccine candidate in terms of its expression, sequence preservation, localization, immunogenicity, and functional activity of antibodies raised to it in this research. Methionine sulfoxide [Met] was previously shown to be reduced in oxidized proteins and shield against oxidative stress, according to Gonococcal MsrA/B. Here we have found that MsrA/B is present, highly conserved, and present in all N. gonorrhoeae strains investigated, and that MsrA/B is a surface-exposing marker for N. gonorrhoeae. MsrA/B, a recombinant MsrA/B is a promising vaccine antigen for N. gonorrhoeae.
Source link: https://doi.org/10.3389/fimmu.2019.00137
Sulfenic acid can be converted to disulfide or sulfenamide or even oxidized to sulfinic acid. Reactive oxygen species can also oxidize Methionine side chains, according to Methionine side chains. Methionine oxidation, triggered by the addition of an additional oxygen atom, leads to the production of methionine sulfoxide. Methionine sulfoxide reductase A or methionine sulfoxide reductase B can be used to achieve a methionine sulfoxide reductase A or methionine sulfoxide reductase B, which also refers to the methionine sulfoxide reductases system.
Source link: https://doi.org/10.3390/antiox7120191
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