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Environmental Toxicology and... Mar 2018The function of Cu,Zn-SOD is to dismutate superoxide into hydrogen peroxide and oxygen. This task is fulfilled due to structural nuances of the enzyme. Many... (Review)
Review
The function of Cu,Zn-SOD is to dismutate superoxide into hydrogen peroxide and oxygen. This task is fulfilled due to structural nuances of the enzyme. Many environmental xenobiotics have been proved to inhibit Cu,Zn-SOD. Those compounds could be found not only in industrial sewage, cigarettes and various chemical agents - some of them are used as drugs, drug production substrates or are the product of drug biotransformation. Cu,Zn-SOD exposition to these compounds leads to inhibition due to: copper ion chelation, unfolding the structure of the enzyme, affecting residues vital for activity maintenance. This review covers a selection of Cu,Zn-SOD inhibitors, referring to in vivo and in vitro study.
Topics: Animals; Environmental Pollutants; Humans; Isoenzymes; Protein Conformation; Superoxide Dismutase; Xenobiotics
PubMed: 29310006
DOI: 10.1016/j.etap.2017.12.022 -
Bulletin of Experimental Biology and... Jan 2022The study examined the skin histomorphology and biochemistry in mature ovariectomized rats treated and not treated with estrogen. Biochemical parameters (superoxide...
The study examined the skin histomorphology and biochemistry in mature ovariectomized rats treated and not treated with estrogen. Biochemical parameters (superoxide dismutase, malondialdehyde, and hydroxyproline content) were measured in dorsal skin samples collected in 50 days after surgery. The morphology of dorsal skin was analyzed under a microscope. In ovariectomized rats, the skin levels of superoxide dismutase and hydroxyproline were significantly lower, while the superoxide dismutase content was significantly higher than in shamoperated animals (p<0.05). Estrogen therapy significantly increased the levels of superoxide dismutase and hydroxyproline and reduced superoxide dismutase level in ovariectomized rats in comparison with the corresponding parameters in untreated ovariectomized animals (p<0.05). Histomorphological analysis of the skin from non-treated ovariectomized rats revealed reduced vascularization and lower density of papillary capillaries in comparison with these parameters in sham-operated controls; estrogen treatment prevented these changes. We concluded that ovariectomized rats can be employed as a model of aging skin in menopause.
Topics: Animals; Female; Humans; Malondialdehyde; Menopause; Ovariectomy; Oxidative Stress; Rats; Skin Aging; Superoxide Dismutase
PubMed: 35001317
DOI: 10.1007/s10517-022-05396-4 -
Bioscience Reports Jun 2022In this review, we focus on understanding the structure-function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that... (Review)
Review
In this review, we focus on understanding the structure-function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that various amino acids play to maintain enzyme quaternary structure or the active site structure, catalytic potential and metal homeostasis in MnSOD, which is essential to maintain enzyme activity. We also observe how polymorphisms of MnSOD are linked to pathologies and how post-translational modifications affect the antioxidant properties of MnSOD. Understanding how modified forms of MnSOD may act as tumor promoters or suppressors by altering the redox status in the body, ultimately aid in generating novel therapies that exploit the therapeutic potential of mutant MnSODs or pave the way for the development of synthetic SOD mimics.
Topics: Catalysis; Catalytic Domain; Structure-Activity Relationship; Superoxide Dismutase
PubMed: 35662317
DOI: 10.1042/BSR20220202 -
International Journal of Biological... Sep 2021Superoxide dismutases (SODs) (EC 1.15.1.1) are well known antioxidant enzymes that play critical roles in cellular defenses of living organisms against harmful...
Superoxide dismutases (SODs) (EC 1.15.1.1) are well known antioxidant enzymes that play critical roles in cellular defenses of living organisms against harmful superoxide radicals during oxidative stress. This study details on cloning, biochemical and functional characterization of an iron containing type superoxide dismutase (SOD) from a novel thermophilic bacteria Cohnella sp. A01 (CaSOD). The secondary and three dimensional structure of the protein were predicted. CaSOD gene was subsequently cloned into pET-26b(+) expression vector and expression of the recombinant protein (rCaSOD) was optimized in E. coli BL21 (DE3) and the purified recombinant SOD showed a single band with an apparent molecular weight of 26 kDa by SDS-PAGE. The half-life and thermodynamic parameters including ΔH, ΔS, and ΔG were 187 min at 60 °C, 7.3 kJ.mol, -76.8 kJ.mol.°K, and 84.1 kJ.mol, respectively. The rCaSOD exhibited catalytic activity in a very broad range of pH (6.0-10.0) and temperatures (35-75 °C), as well as stability in a broad pH range, from 3.0 to 11.0, and wide range of temperature, different concentrations of detergent agents, metal ions, organic solvents and other chemicals. The results suggest that this novel enzyme could be used for various industrial applications in cosmetic, food, and pharmaceutical industries.
Topics: Amino Acid Sequence; Bacillales; Bacterial Proteins; Catalysis; Cloning, Molecular; Enzyme Stability; Hydrogen Peroxide; Hydrogen-Ion Concentration; Iron; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Superoxide Dismutase; Superoxides; Temperature
PubMed: 34329665
DOI: 10.1016/j.ijbiomac.2021.07.150 -
Journal of Neurology, Neurosurgery, and... Feb 2022
Topics: Amyotrophic Lateral Sclerosis; Humans; Mutation; Superoxide Dismutase; Superoxide Dismutase-1
PubMed: 34599043
DOI: 10.1136/jnnp-2021-327935 -
Journal of Food Science Apr 2019Superoxide dismutases (SODs) were purified from sea buckthorn and chestnut rose by ammonium sulfate precipitation and anion-exchange chromatography, and the detection...
Superoxide dismutases (SODs) were purified from sea buckthorn and chestnut rose by ammonium sulfate precipitation and anion-exchange chromatography, and the detection methods of water-soluble tetrazolium-1 (WST-1), nitrobluetetrazolium (NBT) and pyrogallol autoxidation (PA) for SOD activity were compared. WST-1 method was selected due to its coefficient of variation (CV) <6% in this study. Two SODs exhibited similar characteristics. Their molecular mass and isoelectric point were about 30 kDa and 4.8 to 5.0 estimated by electrophoresis, and the K was 0.05 to 0.08 mmol/L, respectively. Dynamic light scattering analysis suggested their hydrodynamic radius distributes from 60 to 1500 nm. The activity of two SODs was unchanged at <80 °C or pH 2 to 9 or in simulated human gastric fluid. Their circular dichroism spectra suggested a main β-sheet structure, the fluorescence spectra reflected that the tryptophan residues of two SODs is partially exposed, these structures were rather stable at pH 2 to 9 or 50 to 90 °C. PRACTICAL APPLICATION: Superoxide dismutase (SOD) is an important antioxidant enzyme. SODs from sea buckthorn and chestnut rose were stable at high temperature or low pH or simulated gastric fluid. This result can provide a new approach for the potential application of SOD in the food and pharmaceutical fields.
Topics: Circular Dichroism; Enzyme Stability; Hippophae; Plant Proteins; Rosa; Superoxide Dismutase
PubMed: 30861132
DOI: 10.1111/1750-3841.14441 -
Analytical Chemistry Aug 20221,4-Dithiothreitol (DTT), a highly water-soluble and well-known reducing agent for preservation and regeneration of sulfhydryl groups in biomedical applications, has...
1,4-Dithiothreitol (DTT), a highly water-soluble and well-known reducing agent for preservation and regeneration of sulfhydryl groups in biomedical applications, has been developed as an efficient and stable coreactant of lucigenin for the first time. DTT efficiently reacts with lucigenin to generate intense chemiluminescence (CL), eliminating the need for external catalysts to facilitate the lucigenin CL. The DTT-lucigenin CL is approximately 15-fold more intense when compared with the lucigenin-HO classical system. Superoxide dismutase (SOD) remarkably quenches the DTT-lucigenin CL. Based on this phenomenon, a newly developed CL approach for the determination of SOD was proposed with a linear range of 0.01-1.5 μg/mL and a limit of detection of 2.2 ng/mL. Various factors affecting the CL emission of the DTT-lucigenin probe were studied and optimized. Plausible mechanistic pathways for the CL coreaction of lucigenin with DTT were proposed and fully discussed. Our proposed method not only has the merit of being selective toward the target analytes but also eliminates the need for the complex synthesis of luminescent probes and facilitates the sensitive detection of SOD in human serum and cosmetics SOD raw material with satisfactory recoveries.
Topics: Acridines; Dithiothreitol; Humans; Hydrogen Peroxide; Luminescent Agents; Luminescent Measurements; Superoxide Dismutase
PubMed: 35878317
DOI: 10.1021/acs.analchem.2c01690 -
International Journal of Molecular... Jun 2021Quantum dots (QDs) have a broad range of applications in cell biolabeling, cancer treatment, metastasis imaging, and therapeutic drug monitoring. Despite their wide use,...
Quantum dots (QDs) have a broad range of applications in cell biolabeling, cancer treatment, metastasis imaging, and therapeutic drug monitoring. Despite their wide use, relatively little is known about their influence on other molecules. Interactions between QDs and proteins can influence the properties of both nanoparticles and proteins. The effect of mercaptosuccinic acid-capped CdTe QDs on intercellular copper-zinc superoxide dismutase (SOD1)-one of the main enzymatic antioxidants-was investigated. Incubation of SOD1 with QDs caused an increase in SOD1 activity, unlike in the case of CdCl, which inhibited SOD1. Moreover, this effect on SOD1 increased with the size and potential of QDs, although the effect became clearly visible in higher concentrations of QDs. The intensity of QD-SOD1 fluorescence, analyzed with the use of capillary electrophoresis with laser-induced fluorescence detection, was dependent on SOD1 concentration. In the case of green QDs, the fluorescence signal decreased with increasing SOD1 concentration. In contrast, the signal strength for Y-QD complexes was not dependent on SOD1 dilutions. The migration time of QDs and their complexes with SOD1 varied depending on the type of QD used. The migration time of G-QD complexes with SOD1 differed slightly. However, in the case of Y-QD complexes with SOD1, the differences in the migration time were not dependent on SOD concentration. This research shows that QDs interact with SOD1 and the influence of QDs on SOD activity is size-dependent. With this knowledge, one might be able to control the activation/inhibition of specific enzymes, such as SOD1.
Topics: Cadmium Compounds; Electrophoresis, Capillary; Fluorescence; Humans; Nanoparticles; Quantum Dots; Spectrometry, Fluorescence; Superoxide Dismutase; Tellurium
PubMed: 34200401
DOI: 10.3390/ijms22116156 -
Molecules (Basel, Switzerland) Apr 2022This study aimed to elucidate the responses of a novel characterized WJL-G4 against citric acid stress by performing physiological analysis, morphology observation, and...
This study aimed to elucidate the responses of a novel characterized WJL-G4 against citric acid stress by performing physiological analysis, morphology observation, and structural and membrane fatty acid composition analysis. The results showed that under citric acid stress, the cell vitality of WJL-G4 was reduced. The cell morphology changed with the unclear, uncompleted and thinner cell wall, and degraded the cell structure. When the citric acid concentration was 20 g/L, WJL-G4 could tolerate citric acid and maintain the cell structure by increasing the intracellular pH, superoxide dismutase activity, and contents of unsaturated fatty acids. As the citric acid concentration was ≥80 g/L, the stress has exceeded the cellular anti-stress ability, causing substantial cell damage. The cell membrane permeability, the content of membrane lipids, malondialdehyde and superoxide anion increased, but the intracellular pH and superoxide dismutase activities decreased, accompanying the increase of citric acid concentrations. The findings of this work provided a theoretical basis for the responsive mechanism of WJL-G4 under high concentrations of citric acid, and can serve as a reference for biological acid reduction in fruit processing.
Topics: Acids; Citric Acid; Malondialdehyde; Pichia; Superoxide Dismutase
PubMed: 35566015
DOI: 10.3390/molecules27092664 -
Animal Biotechnology Dec 2023The aim of this study is to determine the effects of 50% of 96 h LC (5.25 ppm) diazinon on the expression of superoxide dismutase (SOD) enzyme genes (, , and ) and...
The aim of this study is to determine the effects of 50% of 96 h LC (5.25 ppm) diazinon on the expression of superoxide dismutase (SOD) enzyme genes (, , and ) and SOD enzyme activity at the end of 24, 48, 72, and 96 h in platyfish liver and gill tissues. To this end, we determined the tissue-specific distribution of , , and genes and performed analyses in platyfish (). It was determined that malondialdehyde (MDA) level and SOD enzyme activity were increased in the liver [(43.90 EU mg protein (control), 62.45 EU mg protein (24 h), 73.17 EU mg protein (48 h), 82.18 EU mg protein (72 h), 92.93 EU mg protein (96 h)] and gill [(16.44 EU mg protein (control), 33.47 EU mg protein (24 h), 50.38 EU mg protein (48 h), 64.62 EU mg protein (72 h), 74.04 EU mg protein (96 h)] tissues of platyfish exposed to diazinon, while the expression of the genes was down-regulated. The tissue-specific distribution of the genes varied, with the tissues and the genes expression were being predominant in the liver (628.32 in , 637.59 in , 888.5 in ). Thus, the liver was considered a suitable tissue for further gene expression studies. Based on the phylogenetic analyses, platyfish genes can be reported to be orthologs of / genes from other vertebrates. Identity/similarity analyses supported this determination. Conserved gene synteny proved that there are conserved genes in platyfish, zebrafish, and humans.
Topics: Humans; Animals; Diazinon; Phylogeny; Zebrafish; Superoxide Dismutase; Superoxide Dismutase-1; Genomics; Cyprinodontiformes
PubMed: 36811494
DOI: 10.1080/10495398.2023.2178931