Differential Contribution of Superoxide Dismutase Activity by Prion Protein in Vivo

2000 ◽  
Vol 273 (1) ◽  
pp. 136-139 ◽  
Author(s):  
Boon-Seng Wong ◽  
Tao Pan ◽  
Tong Liu ◽  
Ruliang Li ◽  
Pierluigi Gambetti ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Prion Protein ◽  
Superoxide Dismutase Activity ◽  
Differential Contribution

scholarly journals In VivoAntioxidant Activity of Deacetylasperulosidic Acid in Noni

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
De-Lu Ma ◽  
Mai Chen ◽  
Chen X. Su ◽  
Brett J. West
Keyword(s):  
Antioxidant Activity ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Catalase Activity ◽  
Antioxidant Properties ◽  
Superoxide Dismutase Activity ◽  
Morinda Citrifolia ◽  
Control Group ◽  
Dose Dependent

Deacetylasperulosidic acid (DAA) is a major phytochemical constituent ofMorinda citrifolia(noni) fruit. Noni juice has demonstrated antioxidant activityin vivoand in human trials. To evaluate the role of DAA in this antioxidant activity, Wistar rats were fed 0 (control group), 15, 30, or 60 mg/kg body weight per day for 7 days. Afterwards, serum malondialdehyde concentration and superoxide dismutase and glutathione peroxidase activities were measured and compared among groups. A dose-dependent reduction in malondialdehyde was evident as well as a dose-dependent increase in superoxide dismutase activity. DAA ingestion did not influence serum glutathione peroxidase activity. These results suggest that DAA contributes to the antioxidant activity of noni juice by increasing superoxide dismutase activity. The fact that malondialdehyde concentrations declined with increased DAA dose, despite the lack of glutathione peroxidase-inducing activity, suggests that DAA may also increase catalase activity. It has been previously reported that noni juice increases catalase activityin vivobut additional research is required to confirm the effect of DAA on catalase. Even so, the current findings do explain a possible mechanism of action for the antioxidant properties of noni juice that have been observed in human clinical trials.

Effect of nickel chloride on streptozotocin-induced diabetes in rats

1988 ◽  
Vol 66 (5) ◽  
pp. 663-665 ◽  
Author(s):  
Ethel L. B. Novelli ◽  
Ney L. Rodrigues ◽  
Bartolomé O. Ribas
Keyword(s):  
Superoxide Dismutase ◽  
Body Weight ◽  
Single Dose ◽  
Protective Effect ◽  
Plasma Insulin ◽  
Nickel Chloride ◽  
Superoxide Dismutase Activity ◽  
Streptozotocin Induced Diabetes

The potential of nickel chloride to prevent streptozotocin-induced hyperglycemia was tested in rats in vivo. To induce diabetes, streptozotocin (100 mg/kg body weight) was injected as a single dose. Streptozotocin treatment resulted in a significant decrease in plasma insulin and ceruloplasmin, and pancreatic Cu, protein, and Cu–Zn superoxide dismutase activity. In rats treated with nickel chloride (10 mg/kg body weight) and streptozotocin, these values were comparable with those observed in control rats. The results indicate that nickel chloride injected before streptozotocin prevented streptozotocin-induced hyperglycemia, and suggest that the protective effect was related to Cu–Zn superoxide dismutase activity, mediated by copper.

Chronic UVB irradiation induces superoxide dismutase activity in human epidermis in vivo

1995 ◽  
Vol 30 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Kari Punnonen ◽  
Kirsi Lehtola ◽  
Pekka Autio ◽  
Urpo Kiistala ◽  
Markku Ahotupa
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Dismutase Activity ◽  
Human Epidermis ◽  
Uvb Irradiation

Intracellular superoxide dismutase activity defines invasiveness of the murine T-lymphoma cell line L5187Y-ML25 in vitro and in vivo

2013 ◽  
Vol 37 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Maki Tanaka ◽  
Kageaki Kuribayashi ◽  
Kastuhisa Kogawa ◽  
Kiminori Nakamura ◽  
Naoki Watanabe
Keyword(s):  
Superoxide Dismutase ◽  
Cell Line ◽  
Lymphoma Cell ◽  
Superoxide Dismutase Activity ◽  
Lymphoma Cell Line ◽  
T Lymphoma

Streptonigrin toxicity in Escherichia coli: oxygen dependence and the role of the intracellular oxidation–reduction state

1982 ◽  
Vol 28 (5) ◽  
pp. 545-552 ◽  
Author(s):  
John B. Harley ◽  
Caroline J. Fetterolf ◽  
Cesar A. Bello ◽  
Joel G. Flaks
Keyword(s):  
Escherichia Coli ◽  
Superoxide Dismutase ◽  
Superoxide Dismutase Activity ◽  
Lethal Concentration ◽  
Bacterial Physiology ◽  
E Coli ◽  
Escherichia Coli K12 ◽  
Oxidation Reduction

The bacterial physiology of streptonigrin toxicity was further investigated. An optimal oxygen concentration for toxicity was inferred from data showing that steptonigrin at 5 µg/mL was rapidly lethal to aerobic cultures of Escherichia coli K12 JF361, but was without effect on anaerobic cultures and was bacteriostatic to cultures incubated in 5 atm of oxygen plus 1 atm of air (5 atm O2 plus air) (1 atm = 101.325 kPa). Escherichia coli were protected from a potentially lethal concentration of streptonigrin during anaerobic incubation, whether previously grown anaerobically, aerobically, or in 5 atm O2 plus air. Superoxide dismutase activity increased with increasing oxygen tension in the medium, but was not significantly changed by a lethal concentration of streptonigrin. Although the superoxide dismutase activity was four times greater in E. coli grown in 5 atm O2 plus air than those grown in air alone, the aerobic survival in 5 µg/mL streptonigrin was identical, which suggested that superoxide dismutase was not rate limiting for toxicity. Escherichia coli K12 strains deficient in glutathione (KMBL54-129, AB1157-821, and AB1157-830) were protected from streptonigrin poisoning. Dithiothreotol (5.0 mM), diamide (1 mM), methyl viologen (1 mM), and cyanide (10 mM) protected aerobic E. coli from 5 µg/mL streptonigrin.These data are also consistent with a model of in vivo streptonigrin toxicity that requires a favorable intracellular oxidation–reduction state and an optimal concentration of molecular oxygen.

scholarly journals Melatonin and tryptophan counteract lipid peroxidation and modulate superoxide dismutase activity in ringdove heterophils in vivo. Effect of antigen-induced activation and age

AGE ◽  
2009 ◽  
Vol 31 (3) ◽  
pp. 179-188 ◽  
Author(s):  
Sergio D. Paredes ◽  
Ignacio Bejarano ◽  
María Pilar Terrón ◽  
Carmen Barriga ◽  
Russel J. Reiter ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Superoxide Dismutase Activity
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