Biomimetic Superoxide Dismutase Stabilized by Photopolymerization for Superoxide Anions Biosensing and Cell Monitoring

2014 ◽  
Vol 86 (10) ◽  
pp. 4783-4790 ◽  
Author(s):  
Ling Yuan ◽  
Suli Liu ◽  
Wenwen Tu ◽  
Zengsong Zhang ◽  
Jianchun Bao ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Anions ◽  
Cell Monitoring

Scavenging of superoxide anions by lecithinized superoxide dismutase in HL-60 cells

2016 ◽  
Vol 12 (1) ◽  
pp. 274-282
Author(s):  
Tsutomu Ishihara ◽  
Misaki Shibui ◽  
Takaya Hoshi ◽  
Tohru Mizushima
Keyword(s):  
Superoxide Dismutase ◽  
Plasma Membrane ◽  
Therapeutic Effects ◽  
Superoxide Anions ◽  
Covalently Bound

Superoxide dismutase covalently bound to four lecithin molecules (PC-SOD) on plasma membrane has been found to have beneficial therapeutic effects.

scholarly journals Involvement of the superoxide anion in sulphoxidation (Short Communication)

1974 ◽  
Vol 137 (1) ◽  
pp. 119-121 ◽  
Author(s):  
K. Prema ◽  
K. P. Gopinathan
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Anion ◽  
Short Communication ◽  
Model System ◽  
Complete Inhibition ◽  
Superoxide Anions ◽  
Phenazine Methosulphate

Sulphoxidation of compounds capable of undergoing biological sulphoxidation has been demonstrated in a model system (NADH–phenazine methosulphate–O2), known to generate superoxide anions (O2-). Addition of superoxide dismutase to this system results in complete inhibition, suggesting the involvement of O2- in sulphoxidation.

Kinetic Investigations of the Autoxidation of Adrenalin

1978 ◽  
Vol 33 (11-12) ◽  
pp. 891-896 ◽  
Author(s):  
W. Bors ◽  
C. Michel ◽  
M. Saran ◽  
E. Lengfelder
Keyword(s):  
Superoxide Dismutase ◽  
Rate Constants ◽  
Alkaline Solutions ◽  
Superoxide Anions ◽  
Kinetic Investigations

Generation rates of superoxide anions (O2-) by autoxidizing adrenalin at pH 9.5 were deter­mined in solutions containing either superoxide dismutase (0.85 м-1 s-1) or hydroxylamine (0.0185 м-1 s-1) as competitive scavengers. The rate constants of O2- with adrenalin and hydroxyl­amine were calculated for neutral and alkaline solutions. The respective values were for adrenalin: 5.6 ×104 м-1 s-1, pH 7.8; 7.0 × 103 м-1 s-1, pH 9.5 - and for hydroxylamine 5.9 × 104 м-1 s-1, pH 7.8; 3.4 ×104 м-1 s-1, pH 9.5. The effects of various competitors and O2--sources on the rate constants were compared.

scholarly journals Development of intrinsic tone in isolated pulmonary arterioles

1999 ◽  
Vol 276 (5) ◽  
pp. L805-L813 ◽  
Author(s):  
Qiang Liu ◽  
J. T. Sylvester
Keyword(s):  
Nitric Oxide ◽  
Superoxide Dismutase ◽  
Smooth Muscle ◽  
Methyl Ester ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Transmural Pressure ◽  
Time Dependent ◽  
Superoxide Anions ◽  
Calcium Dependent

In isolated porcine pulmonary arterioles with endothelium, intraluminal diameter measured at a transmural pressure of 20 mmHg decreased spontaneously from 233 ± 11 to 171 ± 12 μm in 135 min. This intrinsic constriction was not prevented by indomethacin, tetraethylammonium, or superoxide dismutase. Indomethacin plus N G-nitro-l-arginine methyl ester caused initial constriction and BQ-123 or BQ-123 plus BQ-788 caused initial dilation, but these treatments did not prevent subsequent progressive constriction. In pulmonary arterioles with endothelium exposed to calcium-free conditions and pulmonary arterioles without endothelium, the intraluminal diameter measured at a transmural pressure of 20 mmHg was constant at 239 ± 16 and 174 ± 7 μm, respectively. Thus the spontaneous development of tone in isolated pulmonary arterioles required extracellular calcium and resulted from 1) time-independent smooth muscle contraction caused by mechanisms intrinsic to smooth muscle and 2) time-dependent contraction caused by decreasing activity of endothelium-derived relaxing factors other than nitric oxide, vasodilator prostaglandins, and hyperpolarizing factors acting on calcium-dependent potassium channels or increasing activity of endothelium-derived contracting factors other than endothelin-1, vasoconstrictor prostaglandins, and superoxide anions. Further investigation is indicated to identify these unknown mechanisms and determine their role in pulmonary vasoreactivity.

scholarly journals Superoxide dismutase enhances the formation of hydroxyl radicals in the reaction of 3-hydroxyanthranilic acid with molecular oxygen

1988 ◽  
Vol 251 (3) ◽  
pp. 893-899 ◽  
Author(s):  
H Iwahashi ◽  
T Ishii ◽  
R Sugata ◽  
R Kido
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Hydroxyl Radical ◽  
Molecular Oxygen ◽  
Hydroxyl Radicals ◽  
Fenton Reaction ◽  
Potassium Phosphate ◽  
Radical Formation ◽  
Superoxide Anions ◽  
Hydroxyanthranilic Acid

Superoxide dismutase (SOD) enhanced the formation of hydroxyl radicals, which were detected by using the e.s.r. spin-trapping technique, in a reaction mixture containing 3-hydroxyanthranilic acid (or p-aminophenol), Fe3+ ions, EDTA and potassium phosphate buffer, pH 7.4. The hydroxyl-radical formation enhanced by SOD was inhibited by catalase and desferrioxamine, and stimulated by EDTA and diethylenetriaminepenta-acetic acid, suggesting that both hydrogen peroxide and iron ions participate in the reaction. The hydroxyl-radical formation enhanced by SOD may be considered to proceed via the following steps. First, 3-hydroxyanthranilic acid is spontaneously auto-oxidized in a process that requires molecular oxygen and yields superoxide anions and anthranilyl radicals. This reaction seems to be reversible. Secondly, the superoxide anions formed in the first step are dismuted by SOD to generate hydrogen peroxide and molecular oxygen, and hence the equilibrium in the first step is displaced in favour of the formation of superoxide anions. Thirdly, hydroxyl radicals are generated from hydrogen peroxide through the Fenton reaction. In this Fenton reaction Fe2+ ions are available since Fe3+ ions are readily reduced by 3-hydroxyanthranilic acid. The superoxide anions do not seem to participate in the reduction of Fe3+ ions, since superoxide anions are rapidly dismuted by SOD present in the reaction mixture.

Lecithinized superoxide dismutase induces vasodilation; evidence of direct contribution of superoxide anions to modulating vascular tone

Life Sciences ◽  
1998 ◽  
Vol 64 (4) ◽  
pp. 65-70 ◽  
Author(s):  
Tetsuya Nakamura ◽  
Rie Igarashi ◽  
Toshiaki Kurashina ◽  
Yuichiro Saito ◽  
Jin Hoshino ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Vascular Tone ◽  
Superoxide Anions ◽  
Direct Contribution

scholarly journals SUPEROKSIDA DISMUTASE (SOD) DAN RADIKAL BEBAS

2020 ◽  
Vol 2 (2) ◽  
pp. 124-129
Author(s):  
Evirosa Juliartha Simanjuntak ◽  
Zulham Zulham
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Free Radicals ◽  
Cellular Tissue ◽  
The Body ◽  
Enzymatic Antioxidants ◽  
Superoxide Anions ◽  
Cell Components ◽  
Endogenous Antioxidant

Superoxide dismutase (SOD) is an endogenous antioxidant that works by regulating ROS levels. This group of enzymes functions to catalyze the efficient disposal of superoxide anions. Superoxide anions are produced enzymatically and non-enzymatically. In mammals there are 3 types of SOD, namely SOD1 (CuZnSOD), SOD2 (MnSOD), SOD3 (ECSOD). Oxidative stress caused by free radicals has been reported to be involved in several diseases. Various stressors trigger ROS production, also triggering the production of enzymatic antioxidants such as catalase (CAT), hydroperoxidase (HPx) and superoxide dismutase (SOD). Free radicals cause oxidative stress when the amount in the body is excessive, this situation will cause oxidative damage at the cellular, tissue to organ levels that will accelerate the aging process and the onset of disease. Free radicals are molecules that have one or more unpaired electrons and are therefore relatively unstable. Free radicals try to stabilize themselves by taking electrons from other molecules and will produce reactive oxygen species (ROS). If there is a disturbance in the balance of ROS products with antioxidants, oxidative stress will occur which results in damage to cell components. The higher levels of oxidative stress will increase the lipid peroxidation marker which is presented as malondialdehyde (MDA) and decrease the SOD enzyme activity. Thus the role of molecules that have antioxidant activity is very necessary to ward off oxidative stress.

Inhibition of Phagocytosis-Associated Chemiluminescence by Superoxide Dismutase

1974 ◽  
Vol 9 (6) ◽  
pp. 1051-1056
Author(s):  
Lawrence S. Webb ◽  
Bernard B. Keele ◽  
Richard B. Johnston
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Hydroxyl Radical ◽  
Bactericidal Activity ◽  
Liquid Scintillation ◽  
Superoxide Anions ◽  
Liquid Scintillation Spectrometer ◽  
Human Leukocytes ◽  
Enzyme Superoxide Dismutase ◽  
The Relationship

During the process of phagocytosis, human leukocytes emit a burst of luminescence which can be measured in a liquid scintillation spectrometer. The enzyme superoxide dismutase, which removes superoxide anions (O · ), inhibited this chemiluminescence by 70% at a concentration of 100 μg/ml. The enzyme did not inhibit phagocytosis. These results support other studies indicating that O · is elaborated by phagocytizing leukocytes. They also indicate that O · plays a major role in phagocytosis-associated chemiluminescence, though not necessarily as the luminescing agent. Catalase and benzoate inhibited the chemiluminescence of phagocytosis to a slight extent, suggesting that hydrogen peroxide and hydroxyl radical, respectively, might also be involved in this phenomenon. The relationship between the mediators of chemiluminescence and those responsible for phagocytic bactericidal activity remains to be defined.

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