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Superoxide Dismutase is an important enzyme that plays a crucial role in protecting cells from oxidative stress.
Superoxide Dismutase catalyzes the dismutation (or partitioning) of the superoxide (O₂⁻) radical into ordinary molecular oxygen (O₂) and hydrogen peroxide (H₂O₂).
Superoxide Dismutase is a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms.
CAS Number: 9054-89-1
EINECS Number: 232-943-0
Synonyms: zidovudine, Azidothymidine, 30516-87-1, 3'-Azido-3'-deoxythymidine, Retrovir, AZT, Thymidine, 3'-azido-3'-deoxy-, Zidovudinum, Compound S, Zidovudina, ZIDOVUDINE [AZT], zidovudin, Trizivir, BW A509U, Zidovudinum [Latin], 3'-Deoxy-3'-azidothymidine, BWA509U, BW-A509U, ZDV, BW-A-509U, DRG-0004, Azidothymidine (AZT), Aztec, CCRIS 105, 3'-azt, HSDB 6515, 3'-Azidothymidine, UNII-4B9XT59T7S, MFCD00006536, NSC 602670, 1-[(2R,4S,5S)-4-azido-5-(hydroxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione, 4B9XT59T7S, DTXSID8020127, CHEBI:10110, BW-A 509U, 1-((2R,4S,5S)-4-AZIDO-5-(HYDROXYMETHYL)TETRAHYDROFURAN-2-YL)-5-METHYLPYRIMIDINE-2,4(1H,3H)-DIONE, 1-[(2R,4S,5S)-4-azido-5-(hydroxymethyl)oxolan-2-yl]-5-methyl-1,2,3,4-tetrahydropyrimidine-2,4-dione, CHEMBL129, NSC-602670, Azitidin, DTXCID60127, MLS000028548, AZT Antiviral, COMBIVIR COMPONENT ZIDOVUDINE, TRIZIVIR COMPONENT ZIDOVUDINE, AZT, Antiviral, Zidovudinum (Latin), 1-(3-Azido-2,3-dideoxy-beta-D-ribofuranosyl)-5-methylpyrimidine-2,4-(1H,3H)-dione, AZT (Antiviral), Zidovudine [USAN:USP:INN:BAN:JAN], NCGC00023945-05, SMR000058351, Zidovudina [Spanish], ZIDOVUDINE (IARC), ZIDOVUDINE [IARC], Antiviral AZT, ZIDOVUDINE (MART.), ZIDOVUDINE [MART.], ZIDOVUDINE (USP-RS), ZIDOVUDINE [USP-RS], Timazid, 399024-19-2, ZIDOVUDINE (EP IMPURITY), ZIDOVUDINE [EP IMPURITY], ZIDOVUDINE (EP MONOGRAPH), ZIDOVUDINE [EP MONOGRAPH], ZIDOVUDINE (USP MONOGRAPH), ZIDOVUDINE [USP MONOGRAPH], Propolis+AZT, 3'-Azido-2',3'-Dideoxythymidine, Zidovudine (USAN:USP:INN:BAN:JAN), Retrovir(TM), AZT & Li & EPO, Retrovir (TN), 3' Azido 3' deoxythymidine, Cpd S, Intron A & AZT, Racemic Liposomal AZT, Liposomal AZT-SN-1, Liposomal AZT-SN-3, Zidovudine+PRO 140, PC-SOD+AZT, 3' Azido 2',3' Dideoxythymidine, AZT & srCD4, AZT & rIFN.alpha.2, AZT & rsT4, rIFN-beta seron & AZT, 3'-Azido-3'-deoxythymidine (AIDS), AZT & EPO, AZT & GM-CSF, AZT & HPA, AZT & sCD4, AZT & SST, zudovidine, Aziodothymidine, AZT & Li & GM-CSF, AZT+PRO 140, Met-SDF-1.beta. & AZT, AZT & Li & IL-1, AZT & Li & IL-6, AZT & IL-1, AZT & IL-2, AZT & IL-6, AZT & Interferon-.alpha.-2, AZT & Concanavalin A (ConA), AZT & Lymphoblastoid Interferon, AZT & PM-19, Met-SDF-1.beta. & Zidovudine, 4lhm, 1-(4-Azido-5-hydroxymethyl-tetrahydro-furan-2-yl)-5-methyl-1H-pyrimidine-2,4-dione (AZT), 1-(4-Azido-5-hydroxymethyl-tetrahydro-furan-2-yl)-5-methyl-1H-pyrimidine-2,4-dione [AZT], AZT & rsCD4 & rIFN.alpha.A, 3'-azido-3'-deoxythymidine, AZT, DS-4152 & AZT, 1-((2R,4R,5S)-4-azido-5-(hydroxymethyl)tetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione, 1-[(2R,4S,5S)-4-azido-5-(hydroxymethyl)tetrahydrofuran-2-yl]-5-methyl-pyrimidine-2,4-dione, 5-methyl-1-[rac-(2R,4S,5S)-4-azido-5-(hydroxymethyl)tetrahydrofuran-2-yl]pyrimidine-2,4-dione, AZT & Colony-stimulating factor 2, AZT & NP (from PHCA or HSA), Zidovudine; 1-(3-Azido-2,3-dideoxy-ss-d-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione; Zidovudine (GR 63367X); BP Zidovudine and Lamivudine Impurity Standard, 1-(3-Azido-2,3-dideoxy-beta-D-ribofuranosyl)thymine, 3''-azido-thymidine, K7 [P Ti2 W10 O40], Zidovudine & IFNL1, Zidovudine & IFNL2, Zidovudine & IFNL3, Zidovudine (Retrovir), Zidovudine (Standard), COMPOUND-S, Spectrum_001348, AZT & CD4(178)-PE 40, AZT & IFN.alpha., Zidovudine & IL-29, ZIDOVUDINE [MI], Zidovudine & IL-28A, Zidovudine & IL-28B, AZT, ZDV, ZIDOVUDINE [INN], ZIDOVUDINE [JAN], AZT & Interleukin 29, Opera_ID_1602, Prestwick3_000333, Spectrum2_000927, Spectrum3_001507, Spectrum4_000332, Spectrum5_001101, 3'azido-3'deoxythymidine, ZIDOVUDINE [HSDB], ZIDOVUDINE [USAN], 3'-Azido-3'-deoxythymidine & Erythropoietin, 3'-Azido-3'-deoxythymidine & Sho-Saiko-To, Azidothymidine; Zidovudine, Interferon AD + 3'-azido-3'-deoxythymidine, AZT & Interleukin 28A, AZT & Interleukin 28B, 3'-Azido-3'-deoxythymidine & Concanavalin A, 3'-Azido-3'-deoxythymidine & Interleukin-1, 3'-Azido-3'-deoxythymidine & Interleukin-2, 3'-Azido-3'-deoxythymidine & Interleukin-6, ZIDOVUDINE [VANDF], 3'-azido-3-deoxythimydine, 3'-azido3'-deoxythymidine, AZT & IFNL1, AZT & IFNL2, AZT & IFNL3, AZT & Interferon lambda-1, AZT & Interferon lambda-2, AZT & Interferon lambda-3, AZT (PHARMACEUTICAL), ZIDOVUDINE [WHO-DD], ZIDOVUDINE [WHO-IP], 3''-Deoxy-3-azidothymidine, BSPBio_000365, BSPBio_003153, KBioGR_000703, KBioSS_001828, MLS001055351, MLS001076358, MLS002153202, MLS002222249, Zidovudine & Interleukin 29, DivK1c_000524, SPECTRUM1502109, ZIDOVUDINE [EMA EPAR], 3'-deoxy-3'-azido-thymidine, SPBio_000834, Zidovudine & Interleukin 28A, Zidovudine & Interleukin 28B, AZT & IL-28A, AZT & IL-28B, BPBio1_000403, GTPL4825, Zidovudine (JP18/USP/INN), 3'-Azido-3'-deoxythymidine & Lithium & Erythropoietin, 3'-Azido-3'-deoxythymidine & Lithium & Interleukin-1, 3'-Azido-3'-deoxythymidine & Lithium & Interleukin-6, 3'-Azido-3'-deoxythymidine & Lymphoblastoid Interferon, SCHEMBL14615088, SN-1-dipalmitoylglycerophospho-AZT (in a lipid vesicle), SN-3-dipalmitoylglycerophospho-AZT (in a lipid vesicle), ZIDOVUDINE [ORANGE BOOK], AZT & IL-29, HMS501K06, KBio1_000524, KBio2_001828, KBio2_004396, KBio2_006964, KBio3_002653, J05AF, Dismutase,superoxide;SOD Superoxide Dismuyase;rh-SOD1;Superoxide Dismutase from pig blood;Recombinant Human Superoxide Dismutase(rhSOD);SUPEROXIDE DISMUTASE, 20000u/mg;superoxide dismutase from bovine*erythrocytes;superoxide dismutase microbial sources*from esche.
Superoxide Dismutase is widely present in the human body, including the skin and its appendages.
Any of a type of antioxidant metalloenzymes that occur in aerobic and facultatitive bacteria and in eukarotes.
They catalyze a reaction in which two molecules of the highly toxic, highly reactive, superoxide anion is converted into one molecule each of hydrogen peroxide and molecular oxygen.
Based on the metal cofactors present in the active sites, Superoxide Dismutase can be classified into four distinct groups: Copper-Zinc-SOD (Cu, Zn-SOD), Iron SOD (Fe-SOD), Manganese SOD (Mn-SOD), and Nickel SOD.
The enzyme can serve as an anti-inflammatory agent and can also prevent precancerous cell changes.
Superoxide Dismutase is used in cosmetics and personal care products as an anti-aging ingredient and antioxidant due to its ability to reduce free radical damage to the skin, therefore preventing wrinkles, fine lines, and age spots, and it also helps with wound healing, softens scar tissue, protects against UV rays, and reduces other signs of aging.
Superoxide Dismutase has been reported that SOD has an important link in several human health problems including RBC-related disorders, cystic fibrosis (CF), postcholecystectomy pain syndrome, malignant breast disease, steroid-sensitive nephrotic syndrome, amyotrophic lateral sclerosis, neuronal apoptosis, AIDS, and cancer.
In many animal models having myocardial ischemia-reperfusion injury, inflammation, cerebral ischemia-reperfusion injury, etc., SOD enzymes are found to be very effective.
Furthermore, a strong association between the activity of SOD and Alzheimer's disease has been suggested by some researchers.
This process is essential because superoxide radicals are reactive oxygen species (ROS) that can cause significant damage to cellular components such as DNA, proteins, and lipids.
They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide.
Superoxide Dismutase is the only antioxidant enzyme that scavenges the superoxide anion by converting this free radical to oxygen and hydrogen peroxide, thus preventing peroxynitrite production and further damage.
Superoxide Dismutase is extensively researched and used in anti-inflammatory, antitumor, radiation protection, and antisenility applications.
Superoxide Dismutase is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O−2) anion radical into normal molecular oxygen (O2) and hydrogen peroxide (H2O2).
Superoxide Dismutase as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage.
Hydrogen peroxide is also damaging and is degraded by other enzymes such as catalase.
Thus, Superoxide Dismutase is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use intracellular manganese to prevent damage from reactive O−
Superoxide Dismutase helps to neutralize superoxide radicals, which are by-products of normal cellular metabolism, especially in mitochondria.
By converting these radicals into less harmful molecules (oxygen and hydrogen peroxide), Superoxide Dismutase protects cells from oxidative damage.
Superoxide Dismutase is critical for maintaining cellular health and preventing oxidative stress-related diseases.
Imbalances or deficiencies in SOD activity are associated with various conditions, including neurodegenerative diseases (like ALS and Parkinson's disease), cancer, and inflammatory diseases.
Due to its protective role against oxidative stress, Superoxide Dismutase has been studied for potential therapeutic applications, including treatments for inflammatory diseases, ischemia-reperfusion injuries, and as a supplement to mitigate oxidative damage in various conditions.
In higher plants, Superoxide Dismutase isozymes have been localized in different cell compartments.
Superoxide Dismutase is present in mitochondria and peroxisomes.
Fe-Superoxide Dismutase has been found mainly in chloroplasts but has also been detected in peroxisomes, and CuZn-SOD has been localized in cytosol, chloroplasts, peroxisomes, and apoplast.
In higher plants, Superoxide Dismutase act as antioxidants and protect cellular components from being oxidized by reactive oxygen species (ROS).
ROS can form as a result of drought, injury, herbicides and pesticides, ozone, plant metabolic activity, nutrient deficiencies, photoinhibition, temperature above and below ground, toxic metals, and UV or gamma rays.
To be specific, molecular O2 is reduced to O−2 (a ROS called superoxide) when it absorbs an excited electron released from compounds of the electron transport chain.
Superoxide is known to denature enzymes, oxidize lipids, and fragment DNA.
Superoxide Dismutases catalyze the production of O2 and H2O2 from superoxide (O−2), which results in less harmful reactants.
When acclimating to increased levels of oxidative stress, Superoxide Dismutase concentrations typically increase with the degree of stress conditions.
The compartmentalization of different forms of SOD throughout the plant makes them counteract stress very effectively.
There are three well-known and -studied classes of SOD metallic coenzymes that exist in plants.
First, Fe Superoxide Dismutases consist of two species, one homodimer (containing 1–2 g Fe) and one tetramer (containing 2–4 g Fe).
They are thought to be the most ancient Superoxide Dismutase metalloenzymes and are found within both prokaryotes and eukaryotes.
Fe Superoxide Dismutases are most abundantly localized inside plant chloroplasts, where they are indigenous.
Second, Mn Superoxide Dismutases consist of a homodimer and homotetramer species each containing a single Mn(III) atom per subunit.
They are found predominantly in mitochondrion and peroxisomes.
Third, Cu-Zn Superoxide Dismutases have electrical properties very different from those of the other two classes.
These are concentrated in the chloroplast, cytosol, and in some cases the extracellular space.
Note that Cu-Zn Superoxide Dismutases provide less protection than Fe Superoxide Dismutases when localized in the chloroplast.
Superoxide Dismutase is one of the main reactive oxygen species in the cell.
As a consequence, Superoxide Dismutase serves a key antioxidant role.
The physiological importance of Superoxide Dismutases is illustrated by the severe pathologies evident in mice genetically engineered to lack these enzymes.
Mice lacking Superoxide Dismutase2 die several days after birth, amid massive oxidative stress.
Mice lacking Superoxide Dismutase1 develop a wide range of pathologies, including hepatocellular carcinoma, an acceleration of age-related muscle mass loss, an earlier incidence of cataracts, and a reduced lifespan.
Mice lacking Superoxide Dismutase3 do not show any obvious defects and exhibit a normal lifespan, though they are more sensitive to hyperoxic injury.
Knockout mice of any Superoxide Dismutase enzyme are more sensitive to the lethal effects of superoxide-generating compounds, such as paraquat and diquat (herbicides).
Drosophila lacking SOD1 have a dramatically shortened lifespan, whereas flies lacking SOD2 die before birth.
Depletion of Superoxide Dismutase1 and Superoxide Dismutase2 in the nervous system and muscles of Drosophila is associated with reduced lifespan.
The accumulation of neuronal and muscular ROS appears to contribute to age-associated impairments.
When overexpression of mitochondrial Superoxide Dismutase2 is induced, the lifespan of adult Drosophila is extended.
Among black garden ants (Lasius niger), the lifespan of queens is an order of magnitude greater than of workers despite no systematic nucleotide sequence difference between them.
The Superoxide Dismutase3 gene was found to be the most differentially over-expressed in the brains of queen vs worker ants.
This finding raises the possibility of an important role of antioxidant function in modulating lifespan.
Superoxide Dismutase knockdowns in the worm C. elegans do not cause major physiological disruptions.
However, the lifespan of C. elegans can be extended by superoxide/catalase mimetics suggesting that oxidative stress is a major determinant of the rate of aging.
Knockout or null mutations in SOD1 are highly detrimental to aerobic growth in the budding yeast Saccharomyces cerevisiae and result in a dramatic reduction in post-diauxic lifespan.
In wild-type S. cerevisiae, DNA damage rates increased 3-fold with age, but more than 5-fold in mutants deleted for either the SOD1 or SOD2 genes.
Reactive oxygen species levels increase with age in these mutant strains and show a similar pattern to the pattern of DNA damage increase with age.
Thus it appears that superoxide dismutase plays a substantial role in preserving genome integrity during aging in S. cerevisiae.
SOD2 knockout or null mutations cause growth inhibition on respiratory carbon sources in addition to decreased post-diauxic lifespan.
Superoxide Dismutase is commercially obtained from marine phytoplankton, bovine liver, horseradish, cantaloupe, and certain bacteria.
For therapeutic purpose, Superoxide Dismutase is usually injected locally.
There is no evidence that ingestion of unprotected Superoxide Dismutase or SOD-rich foods can have any physiological effects, as all ingested SOD is broken down into amino acids before being absorbed.
However, ingestion of Superoxide Dismutase bound to wheat proteins could improve its therapeutic activity, at least in theory.
Superoxide Dismutase is a class of enzymes that restrict the biological oxidant cluster enzyme system in the body, which can effectively respond to cellular oxidative stress, lipid metabolism, inflammation, and oxidation.
Published studies have shown that Superoxide Dismutase enzymes (SODs) could maintain a dynamic balance between the production and scavenging of biological oxidants in the body and prevent the toxic effects of free radicals, and have been shown to be effective in anti-tumor, anti-radiation, and anti-aging studies.
Nickel superoxide dismutase (Ni-SOD) is a metalloenzyme that, like the other superoxide dismutases, protects cells from oxidative damage by catalyzing the disproportionation of the cytotoxic superoxide radical (O−2) to hydrogen peroxide and molecular oxygen.
Superoxide Dismutase is a reactive oxygen species that is produced in large amounts during photosynthesis and aerobic cellular respiration.
There is interest in using gene therapy to increase SOD expression in diseases where oxidative stress plays a critical role.
Superoxide Dismutase levels are sometimes used as a biomarker to assess oxidative stress levels in various diseases, helping in both diagnosis and monitoring of treatment efficacy.
storage temp.: -20°C
solubility: Dissolves readily at 5 mg/mL in 0.05 M potassium phosphate buffer, pH 7.8, containing 0.1 mM EDTA.
form: powder
color: blue-gray
Superoxide Dismutase is widely studied and used for anti-inflammatory, anti-tumor, radiation protection and anti-aging applications.
Superoxide Dismutase enzymes have metal ions at their active sites that are essential for their catalytic activity.
The type of metal ion present (copper, zinc, manganese, or iron) defines the specific Superoxide Dismutase isoform.
Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen.
Plays a critical role in the defense of cells against the toxic effects of oxygen radicals.
Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO.
Superoxide Dismutase has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
Irwin Fridovich and Joe McCord at Duke University discovered the enzymatic activity of superoxide dismutase in 1968.
Superoxide Dismutases were previously known as a group of metalloproteins with unknown function; for example, CuZnSOD was known as erythrocuprein (or hemocuprein, or cytocuprein) or as the veterinary anti-inflammatory drug "Orgotein".
Likewise, Brewer (1967) identified a protein that later became known as Superoxide Dismutase as an indophenol oxidase by protein analysis of starch gels using the phenazine-tetrazolium technique.
There are three major families of superoxide dismutase, depending on the protein fold and the metal cofactor: the Cu/Zn type (which binds both copper and zinc), Fe and Mn types (which bind either iron or manganese), and the Ni type (which binds nickel).
Copper and zinc – most commonly used by eukaryotes, including humans.
The cytosols of virtually all eukaryotic cells contain a Superoxide Dismutase enzyme with copper and zinc (Cu-Zn-SOD).
For example, Cu-Zn-SOD available commercially is normally purified from bovine red blood cells.
The bovine Cu-Zn enzyme is a homodimer of molecular weight 32,500.
It was the first Superoxide Dismutase whose atomic-detail crystal structure was solved, in 1975.
Superoxide Dismutase is an 8-stranded "Greek key" beta-barrel, with the active site held between the barrel and two surface loops.
The two subunits are tightly joined back-to-back, mostly by hydrophobic and some electrostatic interactions.
The ligands of the copper and zinc are six histidine and one aspartate side-chains; one histidine is bound between the two metals.
Iron – Many bacteria contain a form of the enzyme with iron (Fe-SOD); some bacteria contain Fe-SOD, others Mn-SOD, and some (such as E. coli) contain both.
Fe-Superoxide Dismutase can also be found in the chloroplasts of plants.
The 3D structures of the homologous Mn and Fe superoxide dismutases have the same arrangement of alpha-helices, and their active sites contain the same type and arrangement of amino acid side-chains.
They are usually dimers, but occasionally tetramers.
Manganese – Nearly all mitochondria, and many bacteria, contain a form with manganese (Mn-SOD): For example, the Mn-SOD found in human mitochondria.
The ligands of the manganese ions are 3 histidine side-chains, an aspartate side-chain and a water molecule or hydroxy ligand, depending on the Mn oxidation state (respectively II and III).
This has a hexameric (6-copy) structure built from right-handed 4-helix bundles, each containing N-terminal hooks that chelate a Ni ion.
The Ni-hook contains the motif His-Cys-X-X-Pro-Cys-Gly-X-Tyr; it provides most of the interactions critical for metal binding and catalysis and is, therefore, a likely diagnostic of NiSODs.
Mutations in the first Superoxide Dismutase enzyme (SOD1) can cause familial amyotrophic lateral sclerosis (ALS, a form of motor neuron disease).
Inactivation of SOD1 causes hepatocellular carcinoma.
Superoxide Dismutase activity has been linked to lung diseases such as acute respiratory distress syndrome (ARDS) or chronic obstructive pulmonary disease (COPD).
Superoxide Dismutase is not expressed in neural crest cells in the developing fetus.
Hence, high levels of free radicals can cause damage to them and induce dysraphic anomalies (neural tube defects).
Mutations in SOD1 can cause familial ALS (several pieces of evidence also show that wild-type SOD1, under conditions of cellular stress, is implicated in a significant fraction of sporadic ALS cases, which represent 90% of ALS patients.), by a mechanism that is presently not understood, but not due to loss of enzymatic activity or a decrease in the conformational stability of the SOD1 protein.
Overexpression of Superoxide Dismutase has been linked to the neural disorders seen in Down syndrome.
In patients with thalassemia, Superoxide Dismutase will increase as a form of compensation mechanism.
However, in the chronic stage, Superoxide Dismutase does not seem to be sufficient and tends to decrease due to the destruction of proteins from the massive reaction of oxidant-antioxidant.
Mitochondria are the primary source of superoxide radicals during cellular respiration, making Mn-SOD crucial for protecting mitochondrial integrity.
Superoxide Dismutase is a frontline defense against oxidative stress, a major factor in aging and the pathogenesis of age-related diseases.
By mitigating oxidative damage, SOD helps maintain cellular function and integrity.
Deficient Superoxide Dismutase activity can lead to the accumulation of superoxide radicals, contributing to neurodegeneration in diseases like ALS, Parkinson’s, and Alzheimer’s.
Oxidative stress is implicated in cancer progression.
Superoxide Dismutase helps reduce this stress, thereby potentially lowering cancer risk.
By reducing oxidative stress, Superoxide Dismutase may protect against cardiovascular conditions such as atherosclerosis and hypertension.
Superoxide Dismutase mimetics (synthetic compounds that mimic SOD activity) are being explored for treating diseases associated with oxidative stress.
Superoxide Dismutase is also available as a dietary supplement, often derived from natural sources like melons or bacteria, and is marketed for its potential anti-aging and anti-inflammatory benefits.
Research is ongoing to evaluate the effectiveness of Superoxide Dismutase and its mimetics in clinical settings for conditions like stroke, heart attack, and inflammatory diseases.
Uses:
Superoxide Dismutase is used as an excellent therapeutic agent to combat reactive oxygen species-mediated diseases such as cancer, inflammatory diseases, cystic fibrosis, ischemia, aging, rheumatoid arthritis, neurodegenerative diseases, and diabetes.
However, the enzyme has some limitations in clinical applications.
Therefore, Superoxide Dismutase conjugates and mimetics have been developed to improve its therapeutic efficiency.
Superoxide Dismutase from bovine erythrocytes has been used in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions.
It also catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen.
Plays a critical role in the defense of cells against the toxic effects of oxygen radicals.
Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby Superoxide Dismutase promotes the activity of NO.
Superoxide Dismutase has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
Superoxide Dismutase (polyoxyalkylene-modified) is used in cosmetic preparations to prevent drying and aging of the skin without causing irritation.
Supplementary Superoxide Dismutase has been suggested as a treatment to prevent bronchopulmonary dysplasia in infants who are born preterm, however the effectiveness of his treatment is not clear.
Superoxide Dismutase has been used in experimental treatment of chronic inflammation in inflammatory bowel conditions.
Superoxide Dismutase may ameliorate cis-platinum-induced nephrotoxicity (rodent studies).
As "Orgotein" or "ontosein", a pharmacologically-active purified bovine liver Superoxide Dismutase, it is also effective in the treatment of urinary tract inflammatory disease in man.
For a time, bovine liver SOD even had regulatory approval in several European countries for such use.
This was cut short by concerns about prion disease.
An Superoxide Dismutase-mimetic agent, TEMPOL, is currently in clinical trials for radioprotection and to prevent radiation-induced dermatitis.
TEMPOL and similar Superoxide Dismutase-mimetic nitroxides exhibit a multiplicity of actions in diseases involving oxidative stress.
The synthesis of enzymes such as superoxide dismutase, L-ascorbate oxidase, and Delta 1 DNA polymerase is initiated in plants with the activation of genes associated with stress conditions for plants.
The most common stress conditions can be injury, drought or soil salinity.
Limiting this process initiated by the conditions of strong soil salinity can be achieved by administering exogenous glutamine to plants.
The decrease in the level of expression of genes responsible for the synthesis of superoxide dismutase increases with the increase in glutamine concentration.
Superoxide Dismutase is used in research for diseases like ALS, Parkinson’s, and Alzheimer’s to mitigate oxidative damage.
Helps in protecting the heart and blood vessels from oxidative damage, potentially reducing the risk of atherosclerosis and hypertension.
Explored as an adjunct therapy to reduce oxidative stress in cancer patients, potentially improving outcomes and reducing side effects of treatments.
Superoxide Dismutase has anti-inflammatory properties and is used in conditions like rheumatoid arthritis and inflammatory bowel diseases.
Superoxide Dismutase is included in skincare formulations for its ability to reduce oxidative stress, which can lead to signs of aging such as wrinkles, fine lines, and sagging skin.
Superoxide Dismutase helps mitigate damage from UV radiation, reducing the risk of sunburn and long-term skin damage.
Promotes skin healing and repair by reducing oxidative damage and inflammation, making it beneficial for treating conditions like eczema, psoriasis, and acne.
Superoxide Dismutase supplements are marketed for their ability to boost the body’s antioxidant defenses, supporting overall health and wellness.
By reducing oxidative stress, SOD may help bolster the immune system, improving resistance to infections and diseases.
Athletes may use Superoxide Dismutase supplements to enhance performance, reduce exercise-induced oxidative stress, and accelerate recovery.
Superoxide Dismutase is widely used in research to study oxidative stress and its impact on various biological processes and diseases.
It serves as a target in the development of drugs aimed at reducing oxidative damage in various conditions, including neurodegenerative and cardiovascular diseases.
Superoxide Dismutase is used in agriculture to protect plants from oxidative damage caused by environmental stresses like drought, high salinity, and pathogen attacks.
In veterinary medicine, Superoxide Dismutase is used to improve the health and well-being of animals, particularly in managing stress-related conditions and enhancing immune responses.
Superoxide Dismutase has been used in topical formulations to accelerate wound healing by reducing oxidative stress at the wound site, promoting faster recovery and reducing the risk of infection.
Research is exploring the use of Superoxide Dismutase gene therapy to increase the enzyme’s levels in diseases where oxidative stress is a significant factor, potentially offering a new avenue for treatment.
Superoxide Dismutase is used in the food industry to extend the shelf life of products by reducing oxidative damage, thus preserving flavor, color, and nutritional value.
Superoxide Dismutase may reduce free radical damage to skin—for example, to reduce fibrosis following radiation for breast cancer.
Studies of this kind must be regarded as tentative, however, as there were not adequate controls in the study including a lack of randomization, double-blinding, or placebo.
Superoxide Dismutase is known to reverse fibrosis, possibly through de-differentiation of myofibroblasts back to fibroblasts.
Safety Profile:
When used in topical formulations (like in cosmetics or skincare products), some individuals may develop allergic reactions, including redness, itching, or rashes.
In rare cases, inhaling powdered forms of SOD, especially in industrial or laboratory settings, can lead to respiratory irritation or hypersensitivity reactions.
While antioxidants like Superoxide Dismutase are beneficial in normal amounts, excessive antioxidant levels can sometimes interfere with the body's natural processes.
Excessive use could potentially hinder the body's ability to fight off infections or lead to imbalances in cellular functions.
High doses of Superoxide Dismutase, especially in supplement form, may lead to digestive issues, such as nausea, bloating, or diarrhea.
There is also the potential for toxicity if taken with other antioxidant supplements that could cause an over-saturation of antioxidant activity in the body.
Superoxide Dismutase may interfere with medications that suppress the immune system, such as corticosteroids.
This could lead to reduced effectiveness of these drugs or unwanted side effects.
Since Superoxide Dismutase has antioxidant properties, it might interfere with certain cancer treatments, such as chemotherapy and radiation, which rely on oxidative stress to kill cancer cells.
The potential for Superoxide Dismutase to reduce the effectiveness of these treatments is still a subject of ongoing research.
There is some concern that high levels of Superoxide Dismutase might interfere with blood-thinning medications, although this risk is not well-established.
