Microbial superoxide dismutase enzyme as therapeutic agent and future gene therapy (original) (raw)
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Biosynthesis and regulation of superoxide dismutases
Free Radical Biology and Medicine, 1988
The past two decades have witnessed an explosion in our understanding of oxygen toxicity. The discovery of superoxide dismutases (SODs) (EC. 1.15.1.1), which specifically catalyze the dismutation of superoxide radicals (02-) to hydrogen peroxide (H202) and oxygen, has indicated that O2-is a normal and common byproduct of oxygen metabolism. There is an increasing evidence to support the conclusion that superoxide radicals play a major role in cellular injury, mutagenesis, and many diseases. In all cases SODs have been shown to protect the cells against these deleterious effects. Recent advances in molecular biology and the isolation of different SOD genes and SOD c-DNAs have been useful in. proving beyond doubt the physiological function of the enzyme. The biosynthesis of SODs, in most biological systems, is under rigorous controls. In general, exposure to increased pO2, increased intracellular fluxes of O2-, metal ions perturbation, and exposures to several environmental oxidants have been shown to influence the rate of SOD synthesis in both prokaryotic and eukaryotic organisms. Recent developments in the mechanism of regulation of the manganese-containing superoxide dismutase of Escherichia coli will certainly open new research avenues to better understand the regulation of SODs in other organisms.
The basic and applied aspects of superoxide dismutase
Journal of Molecular Catalysis B: Enzymatic, 2011
Superoxide dismutase (SOD) is among the most potent antioxidants known in nature and is an important constituent of cellular defence against oxidative stress. The enzyme shows several interesting properties like very high catalytic rate of reaction and high stability to physico-chemical stress. It has also attracted widespread interest due to its therapeutic potential. Oxidative stress is known to be involved in pathophysiology of several diseases and SOD supplementation has been shown to be beneficial in treatment or prevention of such diseases. However, it is yet to be developed into effective, reliable and safe antioxidant therapy. Current review focuses on the physiological importance of SOD, and developments and obstacles in its therapeutic applications for treatment of various disorders. The review also summarizes SOD-based products and patents, its potentiation to improve efficacy, and major clinical trials of SOD in human subjects. Besides, latest literature on phylogeny and biochemistry of the enzyme is also reviewed.
Deleted Journal, 2017
During the course of routine metabolic activities of a cell, it produces different harmful byproducts esp. reactive oxygen species. Superoxide dismutase (SOD; EC 1.15.1.1) is a cellular defense enzyme that neutralizes these free radicals and protects the cell from deleterious effects and increases longevity. In the present work, superoxide dismutase enzyme, purified from a thermophilic bacterium Bacillus licheniformis SPB-13, was assessed for its antioxidative effect on HeLa cell lines. An experimental design was constructed in which the animal cells were first of all exposed to an oxidative stress generated using chemical stressors like H 2 O 2 and Menadione, a vitamin K analogue. Then the MTT assay was performed to assess the cell viability in the presence of high oxidative stress. In final experiment, the menadione preincubated HeLa cells were treated with purified SOD and kept for an interval for detoxification of ROS. Viability assay was performed and it showed an increase in cell viability by 65 % at a concentration of 30 μg/ml of SOD. This confirmed the antioxidative and antiaging property of thermostable SOD from Bacillus licheniformis SPB-13. This potential can be harvested by pharmaceutical industry for topical antiaging formulations.
Production And Characterization Of Recombinant Superoxide Dismutase Protein Expressed In E.Coli
2018
Superoxide dismutases are currently attracting enormous attention because of their biotechnological potential. Superoxide dismutase is an enzyme that catalyzes the dismutation of superoxide radicals (O2−) to H2O2 and water in cells. It was thus aimed in the present study to isolate gene for the Cu, Zn -superoxide dismutase (SOD) from the Bacillus cereus was cloned, characterized and expressed in the Escherichia coli BL21 (DE3) and the desired enzyme was purified. The SOD gene sequence obtained has an open reading frame of 540 bp and encodes 179 amino acid residues and estimated molecular size of 19.6 kDa. The SOD gene sequence was cloned into the pET 24a and pET 28a vector. The linearized DNA, digested with restriction enzymes Nde1 and BamH1, which was transformed into Escherichia coli BL21 (DE3). The expressed SOD protein exhibited 46.2% inhibition. Non-His tagged SOD (pET 24a) showed fold purity of 8.18 by ammonium sulfate precipitation and also showed 48.5% inhibition at 60% satu...
Superoxide dismutases : recent advances and clinical applications
1999
The Escherichia coli iron superoxide dismutase (FeSOD) gene was expressed, at two different levels (using episomal and centromeric plasmid systems), in Saccharomyces cerevisiae cells deficient in copper, zinc superoxide dismutase. Levels of antioxidant enzymes were studied in the recombinant strains in the presence and absence of 1 mM paraquat in minimal medium. Exposure to paraquat resulted in: (1) increase in the levels of total SOD, FeSOD, and catalase activities in both yeast strains expressing the FeSOD gene, and (2) decrease in the levels of glutathione reductase in yeast cells expressing the cloned FeSOD gene on the episomal, but not on the centromeric, plasmid The increase in FeSOD activity suggested that there is stimulation of the yeast 3-phosphoglycerate kinase gene (PGK) promoter controlling the cloned FeSOD gene in the presence of paraquat This could be either due to the oxidative stress induced by paraquat, or as a result of an inherent effect of paraquat itself. This ...
Journal of Biotechnology, 2019
Highlights SODs are essential enzymes in all living cells, protecting against oxidant aggressions; The use of SODs in the dermo-cosmetic sector is limited due to the instability of the enzymes in skin care formulas and once exposed to environmental factors, in particular to UV radiations; A Mn-SOD derived from the extremophilic organism Deinococcus radiodurans, once expressed in E.coli and plant cells, was characterized for its extraordinary features of resistance to high temperature and UV radiations; A plant cell culture extract, enriched in the Deinococcus MnSOD, showed promising potentialities for skin care applications, thus it can be proposed as novel active ingredient for cosmetic-dermatological formulas
Artificial superoxide dismutase for cosmetic therapy and industrial use
Academia Letters, 2021
Humans have a strong natural instinct to know every cause, consequences and mechanism of natural processes. By gathering the knowledge and information about these natural processes, they have developed a big pile of molecular libraries which can mimic or imitate these delicate, highly environmental/biological/chemical specific reactions. One of these reactions is dismutation reaction that includes conversion of superoxide radical anion (O 2˙− ) to peroxide catalysed by the enzyme called as superoxide dismutase (SOD) and the reaction is also called as SOD biocatalytic process. In the reaction, the chemical entity O 2˙− gets oxidized and reduced at the same time and hence the name dismutation is offered for the reaction .
Superoxide Dismutases and Superoxide Reductases
Chemical Reviews, 2014
| Chem. Rev. XXXX, XXX, XXX−XXX D a Eukaryotic NiSOD is found in the cytosol of some green algae. b FeSOD is found in protist Tetrahymena pyriformis. c Cytosolic MnSOD is found in C. albicans and many crustaceans, which also express a mitochondrial MnSOD. d The gene of CuZnSOD has been identified in two Methanobacteria, Methanosarcina acetivorans (Gene Access Number: NP_617328.1) and Methanocella arvoryzae (Gene Access Number: YP_684494.1). e Extracellular CuZnSOD is found in mammals and many plants. f The proposed cytosolic location of prokaryotic SORs comes from the absence of detectable translocation signal peptides in the translated amino acid sequences; there are, however (see section 7), a few sequences with putative twin-arginine signatures. g 1Fe-SORs with a single catalytic domain are tetramers; SORs with an extra desulforedoxin-like domain, with or without the FeCys 4 metal center, are homodimers.
Superoxide Dismutase; structure, function and possible role in cancer prevention in living cells
The enzyme superoxide dismutase (an antioxidant) is an enzyme which catalyses the dismutation reaction of superoxide to ground state oxygen and hydrogen peroxide. This enzyme was found by Irwin Fridovich and Joe McCord. The are three types of superoxide with superoxide dismutase-1 and superoxide dismutase-3 having copper and zinc and superoxide dismutase-2 being a manganese superoxide, however, superoxide dismutase-3 differs from superoxide dismutase-1.With the help of enzymes involved, such as Catalase and Glutathione reductase, complete reaction can be carried out leaving all products which are not harmful to the body. However no clear studies have been done on whether the role of superoxide dismutase radicals have any role in aging or life span but it have been clearly shown that these radicals play an important role in carcinogenesis as they mutate cancer-related genes. Superoxide dismutase however follows a very complicated mechanism due to more enzymes being involved. Superoxide Dismutase plays a role in cancer treatment even though this is not clearly out-stated, however, the enzyme increase the rate of the dismutation reaction as dismutation reaction can occur out of the enzyme but the reaction will be relatively slow which can increase possible activation of cancer cells.
Regulation and Role of Superoxide Dismutase
Biochemical Society Transactions, 1978
Although microorganisms are capable of using a wide range of terminal electron acceptors for respiration (e.g. 02, nitrate, nitrite, sulphate, fumarate etc.), O2 is the most commonly used of these and is of course the sole electron acceptor for many obligate aerobes. Since microorganisms , unlike higher plants or animals, are subjected t o wide19 fluctuating 0, partial pressures in their natural environments, their respiratory systems are capable of adapting t o these extremes in a variety of ways that provide maximum benefit (or at least minimum damage) to the cell. Several respiratory-chain adaptations have been documented for selected microorganisms, particularly bacteria, in response t o either very low or very high O2 partial pressures. The former is a very common environmental condition that poses potentially serious problems for both obligate aerobes and facultative anaerobes growing on non