scholarly journals Superoxide dismutase nanozyme: an emerging star for anti-oxidation

2021 ◽  
Author(s):  
Hanqing Zhao ◽  
Ruofei zhang ◽  
Xiyun Yan ◽  
Kelong Fan
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Superoxide Radicals ◽  
Superoxide Dismutases ◽  
First Line

Superoxide dismutases (SODs) are a group of metalloenzymes that catalyze the dismutation of superoxide radicals (O2•−) into hydrogen peroxide (H2O2) and oxygen (O2). As the first line of defense against...

Superoxide dismutase fromAscaris suum

Parasitology ◽  
1988 ◽  
Vol 97 (2) ◽  
pp. 345-353 ◽  
Author(s):  
M. Sanchez-Moreno ◽  
M. Monteoliva ◽  
A. Fatou ◽  
M. A. García-Ruiz
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Mitochondrial Fraction ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Superoxide Dismutases ◽  
Cytoplasmic Fraction ◽  
Sephadex Column ◽  
Ammonium Sulphate Precipitation ◽  
Electrophoretic Patterns

SummaryThree superoxide dismutases (SOD) (EC 1.15.1.1) were detected in homogenates ofAscaris suum. Each of the three forms of SOD was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange chromatography and G-75 Sephadex column chromatography. The three forms of SOD were present in different cellular locations; one in the cytoplasmic fraction, sensitive to cyanide and hydrogen peroxide, and two in the mitochondrial fraction, one of which was cyanide sensitive. The SOD forms presented clear differences in their electrophoretic patterns. The sexual organs of females showed the highest SOD activities of all the tissues examined. The finding of such high levels of superoxide dismutase inA. suumreflects the importance of this enzyme in the metabolism of this helminth parasite.

Superoxide dismutase mimetic drug tempol aggravates anti-GBM antibody-induced glomerulonephritis in mice

2010 ◽  
Vol 299 (2) ◽  
pp. F445-F452 ◽  
Author(s):  
Hua Lu ◽  
Junhui Zhen ◽  
Tianfu Wu ◽  
Ai Peng ◽  
Ting Ye ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Immunohistochemical Staining ◽  
Treated Group ◽  
First Line ◽  
Sod Activity ◽  
Leukocyte Influx

Oxidative stress plays an important role in the pathogenesis of anti-glomerular basement membrane antibody-induced glomerulonephritis (anti-GBM-GN). Superoxide dismutase (SOD) is the first line of defense against oxidative stress by converting superoxide to hydrogen peroxide (H2O2). We investigated the effect of the SOD mimetic drug tempol on anti-GBM-GN in mice. 129/svJ mice were challenged with rabbit anti-mouse-GBM sera to induce GN and subsequently divided into tempol (200 mg·kg−1·day−1, orally) and vehicle-treated groups. Routine histology, SOD and catalase activities, malondialdehyde (MDA), H2O2, and immunohistochemical staining for neutrophils, lymphocytes, macrophages, p65-NF-κB, and osteopontin were performed. Mice with anti-GBM-GN had significantly reduced renal SOD and catalase activities and increased H2O2 and MDA levels. Unexpectedly, tempol administration exacerbated anti-GBM-GN as evidenced by intensification of proteinuria, the presence of severe crescentic GN with leukocyte influx, and accelerated mortality in the treated group. Tempol treatment raised SOD activity and H2O2 level in urine, upregulated p65-NF-κB and osteopontin in the kidney, but had no effect on renal catalase activity. Thus tempol aggravates anti-GBM-GN by increasing production of H2O2 which is a potent NF-κB activator and as such can intensify inflammation and renal injury. This supposition is supported by increases seen in p65-NF-κB, osteopontin, and leukocyte influx in the kidneys of the tempol-treated group.

scholarly journals Properties of extracellular superoxide dismutase from human lung

1984 ◽  
Vol 220 (1) ◽  
pp. 269-272 ◽  
Author(s):  
S L Marklund
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Human Lung ◽  
Sodium Dodecyl ◽  
Superoxide Dismutases ◽  
Extracellular Superoxide Dismutase ◽  
Order Of Magnitude ◽  
Cuzn Superoxide Dismutase ◽  
Very High

A further characterization of human extracellular superoxide dismutase is reported. The study was especially aimed at the interaction with substances known to interfere with CuZn superoxide dismutase and other superoxide dismutases. Extracellular superoxide dismutase is efficiently inhibited by cyanide and is about 3 times more sensitive than is human CuZn superoxide dismutase. The sensitivity to azide is much lower, but still about 3 times higher than that of human CuZn superoxide dismutase. Extracellular superoxide dismutase is about as rapidly inactivated by hydrogen peroxide as is CuZn superoxide dismutase. The sensitivity to diethyldithiocarbamate is very high and more than an order of magnitude larger than that of CuZn superoxide dismutase. Sodium dodecyl sulphate, under conditions suggested as being suitable for distinguishing between the insensitive CuZn superoxide dismutase and the sensitive Mn superoxide dismutase, efficiently inactivated extracellular superoxide dismutase. No antigenic similarities between extracellular superoxide dismutase and CuZn superoxide dismutase could be demonstrated. Anti-(extracellular superoxide dismutase) did not bind CuZn superoxide dismutase, and anti-(CuZn superoxide dismutase) did not bind extracellular superoxide dismutase.

Effect of Val 73 → Trp Mutation on the Reaction of “Cambialistic” Superoxide Dismutase fromPropionibacterium shermaniiwith Hydrogen Peroxide

1997 ◽  
Vol 345 (1) ◽  
pp. 156-159 ◽  
Author(s):  
R. Gabbianelli ◽  
A. Battistoni ◽  
C. Capo ◽  
F. Polticelli ◽  
G. Rotilio ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase

scholarly journals Cromoglycate and nedocromil enhanced the reactive oxygen species-dependent suppressions with, but not without, dexamethasone in ischaemic and histamine paw oedema of mice

1997 ◽  
Vol 6 (5-6) ◽  
pp. 369-374
Author(s):  
Y. Oyanagui
Keyword(s):  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Glucocorticoid Receptor ◽  
Low Dose ◽  
Natural Antioxidant ◽  
Target Cells ◽  
Oxygen Species ◽  
Paw Oedema ◽  
Β Carotene

Anti-inflammatory actions of two anti-allergic drugs, alone or with dexamethasone (Dex) were examined in two models, because inflammation is claimed to be important for allergic events, especially for asthma. Cromoglycate and nedocromil were tested in ischaemic- and histamineinduced paw oedema models of mice. These antiallergic drugs (1–100 mg/kg, i.p.) failed to suppress these oedemata, but enhanced the suppressions by a low dose of dexamethasone (0.1 mg/kg, s.c.) at 3–8 h after Dex injection. The mode of effects by anti-allergic drugs resembled that of a natural antioxidant (α-tocopherol, β-carotene etc.), and was different from that of an immunosuppressant like FK506. The enhancing potencies of the two anti-allergic drugs were similar at 6 h after Dex in both oedemata, and were diminished by superoxide dismutase (SOD) or catalase (i.p.). Cycloheximide completely abolished suppressions. Nedocromil, but not cromoglycate, inhibits inflammatory events. Therefore, there are common unknown actions by which the two anti-allergics enhance suppression by Dex. A possible mechanism of this action was supposed to enhance the superoxide and/or hydrogen peroxide-dependent glucocorticoid receptor (GR) signalling in the target cells.

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