scholarly journals Effect of catalase inactivation on levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies (Musca domestica)

1983 ◽  
Vol 216 (2) ◽  
pp. 503-506 ◽  
Author(s):  
R G Allen ◽  
K J Farmer ◽  
R S Sohal

The effects of total inhibition of catalase, induced by 3-amino-1,2,4-triazole, on the adult housefly (Musca domestica) were examined. The lack of catalase activity had no effect on the longevity of the houseflies. Inorganic-peroxide concentration was elevated at younger ages, but declined in older flies. The rate of oxygen consumption by the flies was greatly decreased and the levels of oxidized as well as reduced glutathione were augmented. Superoxide dismutase activity showed a slight increase. This study suggests that loss of catalase activity does not affect survival of houseflies due to adaptive responses.

Author(s):  
N. Harasym ◽  
◽  
H. Baran ◽  
N. Bodnarchuk ◽  
V. Otchych ◽  
...  

The effect of histamine and quercetin, as well as their combined effect on the activity of superoxide dismutase, catalase and the content of reduced glutathione in the blood plasma of rats was studied. It was found that the addition to the blood of quercetin at a concentration of 0.1; 0.3; 0.5; 1.0; 5.0 mM causes an increase in superoxide dismutase activity. It was found that histamine at concentrations of .01 and 0.1 μm leads to a decrease in superoxide dismutase activity by 31 and 17 %, respectively. Whereas the biogenic amine in the lowest and highest concentrations does not change the activity of superoxide dismutase in plasma. At simultaneous introduction into blood of histamine in the maximum concentration (10.0 μm) and quercetin in concentration of 0,1; 0.5; 3.0 mM normalizes the activity of superoxide dismutase. And only the combined action of histamine of this concentration and quercetin at a concentration of 5.0 mM reduces the activity of the enzyme by 21 %. Histamine at a concentration of 0.01 μm and the simultaneous action of quercetin at a concentration of 0.1; 0.5; 3.0; 5.0 mM increases the activity of superoxide dismutase, which indicates the generation of reactive oxygen species, in particular the superoxide anion radical. It was found that the addition of whole concentrations of quercetin to whole blood causes a decrease in plasma catalase activity. The combined action of quercetin and histamine causes a decrease in catalase activity. It was found that the addition to the blood of quercetin at a concentration of 0.1; 0.3; 0.5; 1.0 mM causes a decrease in the content of reduced glutathione. Quercetin at a concentration of 3.0 and 5.0 mM causes an increase in reduced glutathione by 27 and 14 %, respectively, compared to the reference plasma. Histamine at concentrations of 10.0, 1.0 and 0.01 μm leads to an increase in the amount of reduced glutathione by 24, 26 and 19 %, respectively. And at a concentration of 0.1 μm, the biogenic amine reduces the GSH content by 39 %. With simultaneous introduction into the blood of histamine at a concentration of 10.0 μm and quercetin at a concentration of 0.1; 0.5; 3.0 mM there is an increase in the content of reduced glutathione. And only at a concentration of 5.0 mM quercetin on the background of the action of histamine (10.0 μm), the content of reduced glutathione is slightly reduced. However, with the combined action of histamine at a minimum concentration (0.01 μM) and quercetin at a concentration of 0.1; 0.5; 3.0 and 5.0 mM there is a decrease in the content of reduced glutathione. After performing a dispersion analysis, it was found that the state of the antioxidant system, both enzymatic and non-enzymatic, is significantly affected by histamine. The smallest, but significant share of the effect is on the action of quercetin in the blood plasma of rats. The indirect and significant effect of the simultaneous action of histamine and quercetin on the antioxidant system of rat plasma was revealed.


2015 ◽  
Vol 117 (suppl_1) ◽  
Author(s):  
Sumitra Miriyala ◽  
Mini Chandra ◽  
Benjamin Maxey ◽  
Daret K St. Clair ◽  
Manikandan Panchatcharam

Manganese Superoxide Dismutase (MnSOD), an antioxidant enzyme that catalyzes the conversion of superoxide radicals (O 2 •-) in mitochondria. Constitutive activation mitochondrial reactive oxygen species (ROS) has been implicated in both the pathogenesis and the progression of cardiovascular disease. Absence of SOD2 (gene that encodes MnSOD) is found to be embryonic lethal in animal models due to impairment of mitochondrial function, most noticeably in the heart. In our earlier investigation, we have shown that the MnSOD mimetic, MnTnBuOE-2-PyP 5+ distributes 3-fold more in mitochondria than in cytosol. The exceptional ability of MnTnBuOE-2-PyP 5+ to dismute O 2 •- parallels its ability to reduce ONOO– and CO3–. Based on our earlier reports, we have generated mice that specifically lack MnSOD in cardiomyocytes (Mhy6-SOD2 Δ ). These mice showed early mortality ~4 months due to cardiac mitochondrial dysfunction. Oxidative phosphorylation (OXPHOS) in mitochondria is the predominant mode for O 2 consumption in cells, and the mitochondria are the primary source of ROS in cells due to leaked electrons. FACS analyses using Mito-Tracker Green indicated that the mass of mitochondria per cell was slightly decreased in the Mhy6-SOD2 Δ to the wild type. We then examined OXPHOS levels in Mhy6-SOD2 Δ v.s. wild type using a Seahorse XF analyzer. The rate of oxygen consumption per cells was signi[[Unable to Display Character: fi]]cantly lower in Mhy6-SOD2 Δ cardiomyocytes than that in wild type. The most noticeable difference in the O 2 consumption was found in the presence of FCCP (H+ ionophore / uncoupler). FCCP is an inner membrane pore opener which resets the proton gradient between the mitochondrial matrix and the interspace, resulting in continuous transport of protons and consuming O 2 at the maximum potential. Remarkably, while the FCCP treatment increased O 2 consumption in wild type, the treatment showed no effect on the O 2 consumption in the Mhy6-SOD2 Δ cardiomyocytes. The result indicated that the low basal OXPHOS activity in Mhy6-SOD2 Δ was due to unusually low OXPHOS potential. We examined glycolysis in these cells by measuring extracellular acidi[[Unable to Display Character: fi]]cation (ECAR) and the pattern exactly opposite to that of oxygen consumption rate (OCR) was observed for glycolysis rates between Mhy6-SOD2 Δ and wild type.


2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
De-Lu Ma ◽  
Mai Chen ◽  
Chen X. Su ◽  
Brett J. West

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.


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