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Biomedicine & Pharmacotherapy =... Jun 2024The recent Global Burden of Disease results have demonstrated that oral diseases are some of the most significant public health challenges facing the world. Owing to its... (Review)
Review
The recent Global Burden of Disease results have demonstrated that oral diseases are some of the most significant public health challenges facing the world. Owing to its specific localization advantage, superoxide dismutase 2 (SOD2 or MnSOD) has the ability to process the reactive oxygen species (ROS) produced by mitochondrial respiration before anything else, thereby impacting the occurrence and development of diseases. In this review, we summarize the processes of common oral diseases in which SOD2 is involved. SOD2 is upregulated in periodontitis to protect the tissue from the distant damage caused by excessive ROS and further reduce inflammatory progression. SOD2 also participates in the specific pathogenesis of oral cancers and dental diseases. The clinical application prospects of SOD2 in oral diseases will be discussed further, referencing the differences and relationship between oral diseases and other clinical systemic diseases.
Topics: Humans; Superoxide Dismutase; Reactive Oxygen Species; Disease Progression; Animals; Mouth Diseases; Oxidative Stress; Mitochondria
PubMed: 38688168
DOI: 10.1016/j.biopha.2024.116605 -
Microbial Biotechnology Sep 2020Heavy metal contamination is a serious environmental problem. Understanding the toxicity mechanisms may allow to lower concentration of metals in the metal-based...
Heavy metal contamination is a serious environmental problem. Understanding the toxicity mechanisms may allow to lower concentration of metals in the metal-based antimicrobial treatments of crops, and reduce metal content in soil and groundwater. Here, we investigate the interplay between metal efflux systems and the superoxide dismutase (SOD) in the purple bacterium Rubrivivax gelatinosus and other bacteria through analysis of the impact of metal accumulation. Exposure of the Cd -efflux mutant ΔcadA to Cd caused an increase in the amount and activity of the cytosolic Fe-Sod SodB, thereby suggesting a role of SodB in the protection against Cd . In support of this conclusion, inactivation of sodB gene in the ΔcadA cells alleviated detoxification of superoxide and enhanced Cd toxicity. Similar findings were described in the Cu -efflux mutant with Cu . Induction of the Mn-Sod or Fe-Sod in response to metals in other bacteria, including Escherichia coli, Pseudomonas aeruginosa, Pseudomonas putida, Vibrio cholera and Bacillus subtilis, was also shown. Both excess Cd or Cu and superoxide can damage [4Fe-4S] clusters. The additive effect of metal and superoxide on the [4Fe-4S] could therefore explain the hypersensitive phenotype in mutants lacking SOD and the efflux ATPase. These findings underscore that ROS defence system becomes decisive for bacterial survival under metal excess.
Topics: Burkholderiales; Metals, Heavy; Superoxide Dismutase; Superoxides
PubMed: 32558268
DOI: 10.1111/1751-7915.13589 -
Molecular Plant Pathology Apr 2017Reactive oxygen species (ROS), including superoxide ( O2·-/ HO2·) and hydrogen peroxide (H O ), are differentially produced during resistance responses to biotrophic...
Reactive oxygen species (ROS), including superoxide ( O2·-/ HO2·) and hydrogen peroxide (H O ), are differentially produced during resistance responses to biotrophic pathogens and during susceptible responses to necrotrophic and hemi-biotrophic pathogens. Superoxide dismutase (SOD) is responsible for the catalysis of the dismutation of O2·-/ HO2· to H O , regulating the redox status of plant cells. Increased SOD activity has been correlated previously with resistance in barley to the hemi-biotrophic pathogen Pyrenophora teres f. teres (Ptt, the causal agent of the net form of net blotch disease), but the role of individual isoforms of SOD has not been studied. A cytosolic CuZnSOD, HvCSD1, was isolated from barley and characterized as being expressed in tissue from different developmental stages. HvCSD1 was up-regulated during the interaction with Ptt and to a greater extent during the resistance response. Net blotch disease symptoms and fungal growth were not as pronounced in transgenic HvCSD1 knockdown lines in a susceptible background (cv. Golden Promise), when compared with wild-type plants, suggesting that cytosolic O2·-/ HO2· contributes to the signalling required to induce a defence response to Ptt. There was no effect of HvCSD1 knockdown on infection by the hemi-biotrophic rice blast pathogen Magnaporthe oryzae or the biotrophic powdery mildew pathogen Blumeria graminis f. sp. hordei, but HvCSD1 also played a role in the regulation of lesion development by methyl viologen. Together, these results suggest that HvCSD1 could be important in the maintenance of the cytosolic redox status and in the differential regulation of responses to pathogens with different lifestyles.
Topics: Amino Acid Sequence; Ascomycota; Base Sequence; Cell Death; Cytosol; Gene Expression Profiling; Gene Expression Regulation, Plant; Gene Knockdown Techniques; Hordeum; Host-Pathogen Interactions; Magnaporthe; Plant Diseases; Plant Proteins; Plants, Genetically Modified; RNA Interference; RNA, Messenger; Reactive Oxygen Species; Superoxide Dismutase; Time Factors; Nicotiana
PubMed: 26992055
DOI: 10.1111/mpp.12399 -
International Journal of Molecular... Nov 2022The circadian system synchronizes daily with the day-night cycle of our environment. Disruption of this rhythm impacts the emergence and development of many diseases...
The circadian system synchronizes daily with the day-night cycle of our environment. Disruption of this rhythm impacts the emergence and development of many diseases caused, for example, by the overproduction of free radicals, leading to oxidative damage of cellular components. The goal of this study was to determine the activity of superoxide dismutase (SOD), glutathione peroxidase (GPx), catalase (CAT), glutathione transferase (GST), glutathione reductase (R-GSSG), and the concentration of glutathione (GSH) in the circadian rhythm. The study group comprised 66 healthy volunteers (20-50 years; 33 women; 33 men). The blood was collected at 2, 8 a.m., and 2, 8 p.m. All samples marked the serum melatonin concentration to confirm the correct sleeping rhythm and wakefulness throughout the day. The activity of study enzymes and the concentration of GSH were measured by the spectrophotometric method. Confirmed the existence of circadian regulation of oxidative stress enzymes except for GST activity. The peak of activity of study enzymes and GSH concentration was observed at 2 a.m. The increased activity of enzymes and the increase in GSH concentration observed at night indicate that during sleep, processes allowing to maintain of the redox balance are intensified, thus limiting the formation of oxidative stress.
Topics: Female; Animals; Circadian Rhythm; Oxidative Stress; Glutathione Peroxidase; Superoxide Dismutase; Glutathione
PubMed: 36430753
DOI: 10.3390/ijms232214275 -
Molecular Biology and Evolution Aug 2021Internalization of a bacteria by an archaeal cell expedited eukaryotic evolution. An important feature of the species that diversified into the great variety of...
Internalization of a bacteria by an archaeal cell expedited eukaryotic evolution. An important feature of the species that diversified into the great variety of eukaryotic life visible today was the ability to combat oxidative stress with a copper-zinc superoxide dismutase (CuZnSOD) enzyme activated by a specific, high-affinity copper chaperone. Adoption of a single protein interface that facilitates homodimerization and heterodimerization was essential; however, its evolution has been difficult to rationalize given the structural differences between bacterial and eukaryotic enzymes. In contrast, no consistent strategy for the maturation of periplasmic bacterial CuZnSODs has emerged. Here, 34 CuZnSODs are described that closely resemble the eukaryotic form but originate predominantly from aquatic bacteria. Crystal structures of a Bacteroidetes bacterium CuZnSOD portray both prokaryotic and eukaryotic characteristics and propose a mechanism for self-catalyzed disulfide maturation. Unification of a bacterial but eukaryotic-like CuZnSOD along with a ferredoxin-fold MXCXXC copper-binding domain within a single polypeptide created the advanced copper delivery system for CuZnSODs exemplified by the human copper chaperone for superoxide dismutase-1. The development of this system facilitated evolution of large and compartmentalized cells following endosymbiotic eukaryogenesis.
Topics: Bacteria; Copper; Eukaryota; Humans; Superoxide Dismutase; Zinc
PubMed: 34021750
DOI: 10.1093/molbev/msab157 -
BMC Plant Biology Mar 2021The main objectives of this study were to find the possible structural association between the activity of enzymatic antioxidants and the grain yield of triticale plants...
Superoxide dismutase (SOD) as a selection criterion for triticale grain yield under drought stress: a comprehensive study on genomics and expression profiling, bioinformatics, heritability, and phenotypic variability.
BACKGROUND
The main objectives of this study were to find the possible structural association between the activity of enzymatic antioxidants and the grain yield of triticale plants as well as identifying the genotypic variability which might be effective on this association. Accordingly, expression levels of superoxide dismutase (SOD) isozymes (Mn-SOD, Cu/Zn-SOD, and Fe-SOD) were appraised to distinguish any possible relationship between SOD expression and drought resistance of triticale. A novel analytical method for distinguishing elite genotypes based on measured features was proposed. Additionally, a new programing based on SAS-language (IML) was introduced to estimate the genetic parameters rooted from combined ANOVA model (linear mixed model), which is capable of being used in any field study other than the current one.
METHODS
Thirty genotypes of triticale were studied under normal and drought stress conditions during 6 years (three different locations). Accordingly, based on the results of genetic variability, heatmap analysis, biplot graph, and clustering technique, two genotypes with the highest genetic distance were selected to appraise the differential expression profiling of three SOD isozyme in shoot and root organs.
RESULTS
Field experiments and bioinformatics results showed that superoxide dismutase (SOD) was the most influential antioxidant in resistance of triticale to drought stress; therefore, it could be used as an indirect selection index in early stages to distinguish resistant genotypes to drought stress. Additionally, Mn-SOD and Fe-SOD showed roughly similar expression levels for both genotypes under drought stress. However, Cu/Zn-SOD expression level was higher in root and shoot of the tolerant genotype than the susceptible genotype.
CONCLUSION
Heatmap analysis that is applied for the first time to screen suitable genotypes, showed to be highly capable of distinguishing elite genotypes and pointing out the proper features for selection criteria. Bioinformatics results indicated that SOD is more important than other enzymatic antioxidant for being considered as selection criteria or candidate gene for transgenic purposes. Based on expressional results, Mn-SOD announced as a general isozyme that is probably highly expressed in most of the species, while, Cu/Zn-SOD was introduced as a genotype specific isozyme that is likely more expressed in tolerant genotypes.
Topics: Antioxidants; Biological Variation, Population; Computational Biology; Droughts; Gene Expression Profiling; Inheritance Patterns; Isoenzymes; Plant Breeding; Selection, Genetic; Stress, Physiological; Superoxide Dismutase; Triticale
PubMed: 33752615
DOI: 10.1186/s12870-021-02919-5 -
FEBS Open Bio Feb 2022Endothelial cell apoptosis is an important pathophysiology in many cardiovascular diseases. The gasotransmitter nitric oxide (NO) is known to regulate cell survival and...
Endothelial cell apoptosis is an important pathophysiology in many cardiovascular diseases. The gasotransmitter nitric oxide (NO) is known to regulate cell survival and apoptosis. However, the mechanism underlying the effect of NO remains unclear. In this research, by targeting cytosolic copper/zinc superoxide dismutase (SOD1) monomerization, we aimed to explore how NO inhibited endothelial cell apoptosis. We showed that treatment with the NO synthase (NOS) inhibitor nomega-nitro-l-arginine methyl ester hydrochloride (L-NAME) significantly decreased the endogenous NO content of endothelial cells, facilitated the formation of SOD1 monomers, inhibited dismutase activity, and promoted reactive oxygen species (ROS) accumulation in human umbilical vein endothelial cells (HUVECs); by contrast, supplementation with the NO donor sodium nitroprusside (SNP) upregulated NO content, prevented the formation of SOD1 monomers, enhanced dismutase activity, and reduced ROS accumulation in L-NAME-treated HUVECs. Mechanistically, tris(2-carboxyethyl) phosphine hydrochloride (TCEP), a specific reducer of cysteine thiol, increased SOD1 monomer formation, thus preventing the NO-induced increase in dismutase activity and the decrease in ROS. Furthermore, SNP inhibited HUVEC apoptosis caused by the decrease in endogenous NO, whereas TCEP abolished this protective effect of SNP. In summary, our data reveal that NO protects endothelial cells against apoptosis by inhibiting cysteine-dependent SOD1 monomerization to enhance SOD1 activity and inhibit oxidative stress.
Topics: Apoptosis; Cells, Cultured; Cysteine; Human Umbilical Vein Endothelial Cells; Humans; Nitric Oxide; Nitric Oxide Synthase Type III; Superoxide Dismutase; Superoxide Dismutase-1
PubMed: 34986524
DOI: 10.1002/2211-5463.13362 -
Biophysical Journal Apr 2020The folding reaction of a stable monomeric variant of Cu/Zn superoxide dismutase (mSOD1), an enzyme responsible for the conversion of superoxide free radicals into...
The folding reaction of a stable monomeric variant of Cu/Zn superoxide dismutase (mSOD1), an enzyme responsible for the conversion of superoxide free radicals into hydrogen peroxide and oxygen, is known to be among the slowest folding processes that adhere to two-state behavior. The long lifetime, ∼10 s, of the unfolded state presents ample opportunities for the polypeptide chain to transiently sample nonnative structures before the formation of the productive folding transition state. We recently observed the formation of a nonnative structure in a peptide model of the C-terminus of SOD1, a sequence that might serve as a potential source of internal chain friction-limited folding. To test for friction-limited folding, we performed a comprehensive thermodynamic and kinetic analysis of the folding mechanism of mSOD1 in the presence of the viscogens glycerol and glucose. Using a, to our knowledge, novel analysis of the folding reactions, we found the disulfide-reduced form of the protein that exposes the C-terminal sequence, but not its disulfide-oxidized counterpart that protects it, experiences internal chain friction during folding. The sensitivity of the internal friction to the disulfide bond status suggests that one or both of the cross-linked regions play a critical role in driving the friction-limited folding. We speculate that the molecular mechanisms giving rise to the internal friction of disulfide-reduced mSOD1 might play a role in the amyotrophic lateral sclerosis-linked aggregation of SOD1.
Topics: Amyotrophic Lateral Sclerosis; Disulfides; Friction; Humans; Kinetics; Mutation; Protein Folding; Superoxide Dismutase; Superoxide Dismutase-1
PubMed: 32191862
DOI: 10.1016/j.bpj.2020.02.028 -
Aging Mar 2021
Topics: Aging; Antioxidants; Humans; Metabolic Flux Analysis; Superoxide Dismutase
PubMed: 33713400
DOI: 10.18632/aging.202821 -
Cell Chemical Biology Jul 2018Shared molecular pathologies between distinct neurodegenerative disorders offer unique opportunities to identify common mechanisms of neuron death, and apply lessons... (Review)
Review
Shared molecular pathologies between distinct neurodegenerative disorders offer unique opportunities to identify common mechanisms of neuron death, and apply lessons learned from one disease to another. Neurotoxic superoxide dismutase 1 (SOD1) proteinopathy in SOD1-associated familial amyotrophic lateral sclerosis (fALS) is recapitulated in idiopathic Parkinson disease (PD), suggesting that these two phenotypically distinct disorders share an etiological pathway, and tractable therapeutic target(s). Despite 25 years of research, the molecular determinants underlying SOD1 misfolding and toxicity in fALS remain poorly understood. The absence of SOD1 mutations in PD highlights mounting evidence that SOD1 mutations are not the sole cause of SOD1 protein misfolding occasioning oligomerization and toxicity, reinforcing the importance of non-genetic factors, including protein metallation and post-translational modification in determining SOD1 stability and function. We propose that these non-genetic factors underlie the misfolding and dysfunction of SOD1 and other proteins in both PD and fALS, constituting a shared and tractable pathway to neurodegeneration.
Topics: Animals; Homeostasis; Humans; Metals; Movement Disorders; Mutation; Oxidative Stress; Superoxide Dismutase-1
PubMed: 29861271
DOI: 10.1016/j.chembiol.2018.05.004