Endotoxin increases lung Cu,Zn superoxide dismutase mRNA: O2 raises enzyme synthesis

Administration of endotoxin to adult rats increases lung Cu,Zn superoxide activity after 72 h of exposure to greater than 95% O2. The increased activity is brought about mainly by a faster rate of Cu,Zn superoxide dismutase synthesis; rats treated with endotoxin but not exposed to hyperoxia do not exhibit these findings (Hass, Frank, and Massaro, J. Biol. Chem. 257: 9379-9383, 1982). We now report that 48 h after treatment of adult rats with endotoxin there was a decreased rate of Cu,Zn superoxide dismutase synthesis by lung slices from air- and O2- exposed rats, although, in both groups, the lung concentration of Cu,Zn superoxide dismutase mRNA was increased approximately 45%. Exposure of endotoxin-treated rats to greater than 95% O2 or air for an additional 24 h (72 h all told) resulted in continued elevation of Cu,Zn superoxide dismutase mRNA only in lungs of O2- exposed rats. In vitro exposure of lung slices from air-breathing saline- or endotoxin-treated rats to 95% O2 for 6 h led to an increased rate of Cu,Zn superoxide dismutase synthesis only in slices from endotoxin-treated rats. We conclude that endotoxin treatment leads to an increased concentration of Cu,Zn superoxide dismutase mRNA in rat lungs, but a sustained elevation of the mRNA, and its translation into an increased rate of Cu,Zn superoxide dismutase synthesis requires exposure of the lung to hyperoxia.

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Developmental regulation of rat lung Cu,Zn-superoxide dismutase

Biochemical Journal ◽

10.1042/bj2460697 ◽

1987 ◽

Vol 246 (3) ◽

pp. 697-703 ◽

Cited By ~ 24

Author(s):

M A Hass ◽

D Massaro

Keyword(s):

Superoxide Dismutase ◽

Half Life ◽

Specific Activity ◽

Developmental Regulation ◽

Progressive Increase ◽

Enzyme Synthesis ◽

Enzyme Activation ◽

Sod Activity ◽

Adult Rats ◽

Copper Chelation

In the present investigation we found that lung Cu, Zn-superoxide dismutase (SOD) activity (units/mg of DNA) increases steadily in the rat from birth to adulthood. The specific activity (units/micrograms of enzyme) of Cu, Zn-SOD was unchanged from birth to adulthood, excluding enzyme activation as a mechanism responsible for the increase in enzyme activity. Lung synthesis of Cu, Zn-SOD peaked at 1 day before birth and decreased thereafter to adult values. Calculations, based on rates of Cu, Zn-SOD synthesis and the tissue content of the enzyme, indicated that lung Cu, Zn-SOD activity increased during development owing to the rate of enzyme synthesis exceeding its rate of degradation by 5-10%. These calculations were supported by measurements of enzyme degradation in the neonatal (half-life, t1/2, = 12 h) and adult lung (t1/2 = greater than 100 h); the difference in half-life did not reflect the rates of overall protein degradation in the lung, since these rates were not different in lungs from neonatal and adult rats. We did not detect differences in the Mr or pI of Cu, Zn-SOD during development, but the susceptibility of the enzyme to inactivation by heat or copper chelation decreased with increasing age of the rats. We conclude that the progressive increase in activity of Cu, Zn-SOD is due to a rate of synthesis that exceeds degradation of the enzyme. The data also suggest that increased stabilization of enzyme conformation accounts for the greater half-life of the enzyme in lungs of adult compared with neonatal rats.

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Differences in CuZn superoxide dismutase induction in lungs of neonatal and adult rats

AJP Cell Physiology ◽

10.1152/ajpcell.1987.253.1.c66 ◽

1987 ◽

Vol 253 (1) ◽

pp. C66-C70 ◽

Cited By ~ 26

Author(s):

M. A. Hass ◽

D. Massaro

Keyword(s):

Superoxide Dismutase ◽

Antioxidant Enzyme ◽

Prolonged Exposure ◽

Synthesis Rate ◽

Adult Rats ◽

Adult Lung ◽

Neonatal Lung ◽

Cuzn Superoxide Dismutase

The failure of adult rats to survive prolonged exposure to greater than 95% O2 is generally ascribed to the inability of their lungs to increase antioxidant enzyme synthesis in response to the oxidant challenge. We studied the synthesis rate of the antioxidant enzyme CuZn superoxide dismutase (CuZn SOD) in lungs of adult and neonatal rats exposed to conditions that alter the lung's oxidant-to-antioxidant balance. Lung CuZn SOD synthesis in the adult was significantly increased after 24 h of hyperoxia but fell to control levels after further exposure, whereas in neonatal lungs an increased rate of synthesis of CuZn SOD was found only after 72 h of hyperoxia. The adult lung responded to two in vitro oxidant stresses, [diethyldithiocarbamate exposure and heat (42 degrees C)] with increases in CuZn SOD synthesis twice the magnitude of those in the neonatal lung. These data indicate that the adult lung is at least as capable as the neonatal lung of increasing its synthesis of CuZn SOD in response to an oxidative stress. However, the inability of the adult lung to maintain an increased rate of CuZn SOD synthesis during in vivo hyperoxia may contribute to the poor tolerance of the adult lung to greater than 95% O2.

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Effects of in vitro exposure to ozone and/or hyperoxia on superoxide dismutase, catalase, glutathione and lipid peroxidation in red blood cells and plasma of rainbow trout, Oncorhynchus mykiss (Walbaum)

Aquaculture Research ◽

10.1046/j.1365-2109.2002.00649.x ◽

2002 ◽

Vol 33 (3) ◽

pp. 165-175 ◽

Cited By ~ 21

Author(s):

O Ritola ◽

L D Peters ◽

D R Livingstone ◽

P Lindström-Seppä

Keyword(s):

Lipid Peroxidation ◽

Superoxide Dismutase ◽

Rainbow Trout ◽

Oncorhynchus Mykiss ◽

Red Blood Cells ◽

Blood Cells ◽

Rainbow Trout Oncorhynchus Mykiss ◽

In Vitro Exposure

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Rat lung antioxidant enzyme induction by ozone

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.1991.260.6.l412 ◽

1991 ◽

Vol 260 (6) ◽

pp. L412-L418 ◽

Cited By ~ 4

Author(s):

I. Rahman ◽

L. B. Clerch ◽

D. Massaro

Keyword(s):

Superoxide Dismutase ◽

Enzyme Activity ◽

Antioxidant Enzymes ◽

Glutathione Peroxidase ◽

Antioxidant Enzyme ◽

Enzyme Induction ◽

Rat Lung ◽

Adult Rats ◽

Air Breathing ◽

Different Ages

We exposed rats of different ages (weights approximately 45-300 g) to 0.7 ppm O3 for 1-5 days. At 5 days lungs of O3-exposed rats had higher activity of Cu,Zn superoxide dismutase (SOD), Mn SOD, catalase, and glutathione peroxidase than air-breathing rats; this greater activity was not due to blood-associated enzyme activity. The greater enzyme activity occurred with a higher concentration of the mRNA for each enzyme (Mn SOD not measured) without altered stability of these mRNAs. In adult rats the concentrations of these mRNAs were measured after 1, 3, and 5 days exposure to O3 and were elevated by day 3. The intergroup differences (air vs. O3) among antioxidant enzymes (AOEs) were unequal, and the intergroup differences in concentration of the specific AOE mRNA were greater than the differences in activity of their AOE. We conclude exposure to O3 led to greater expression of AOE genes; the increased expression was mediated pretranslationally probably at the level of transcription.

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Superoxide, Xanthine Oxidase and Platelet Reactions: Further Studies on Mechanisms by which Oxidants Influence Platelets

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650190 ◽

1981 ◽

Vol 45 (03) ◽

pp. 290-293 ◽

Cited By ~ 9

Author(s):

Peter H Levine ◽

Danielle G Sladdin ◽

Norman I Krinsky

Keyword(s):

Superoxide Dismutase ◽

Cytochrome C ◽

Xanthine Oxidase ◽

Direct Effect ◽

Platelet Function ◽

Experimental Conditions ◽

Release Reaction

SummaryIn the course of studying the effects on platelets of the oxidant species superoxide (O- 2), Of was generated by the interaction of xanthine oxidase plus xanthine. Surprisingly, gel-filtered platelets, when exposed to xanthine oxidase in the absence of xanthine substrate, were found to generate superoxide (O- 2), as determined by the reduction of added cytochrome c and by the inhibition of this reduction in the presence of superoxide dismutase.In addition to generating Of, the xanthine oxidase-treated platelets display both aggregation and evidence of the release reaction. This xanthine oxidase induced aggreagtion is not inhibited by the addition of either superoxide dismutase or cytochrome c, suggesting that it is due to either a further metabolite of O- 2, or that O- 2 itself exerts no important direct effect on platelet function under these experimental conditions. The ability of Of to modulate platelet reactions in vivo or in vitro remains in doubt, and xanthine oxidase is an unsuitable source of O- 2 in platelet studies because of its own effects on platelets.

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Faculty Opinions recommendation of Effects of in vitro exposure to dibutyl phthalate, mono-butyl phthalate, and acetyl tributyl citrate on ovarian antral follicle growth and viability.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.727593855.793536980 ◽

2017 ◽

Author(s):

Virendra Mahesh

Keyword(s):

Dibutyl Phthalate ◽

Antral Follicle ◽

Follicle Growth ◽

In Vitro Exposure ◽

Acetyl Tributyl Citrate ◽

Butyl Phthalate

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Synthesis and antioxidant activity of new selenium-containing quinolines

Medicinal Chemistry ◽

10.2174/1573406416666200403081831 ◽

2020 ◽

Vol 16 ◽

Cited By ~ 1

Author(s):

Benedetta Bocchini ◽

Bruna Goldani ◽

Fernanda S.S. Sousa ◽

Paloma T. Birmann ◽

Cesar A. Brüning ◽

...

Keyword(s):

Antioxidant Activity ◽

Superoxide Dismutase ◽

Radical Scavenging ◽

Building Blocks ◽

Antioxidant Potential ◽

In Vitro Assays ◽

Pharmacological Activities ◽

Antioxidant Power ◽

Antioxidant Agents

Background: Quinoline derivatives have been attracted much attention in drug discovery and synthetic derivatives of these scaffolds present a range of pharmacological activities. Therefore, organoselenium compounds are valuable scaffolds in organic synthesis because their pharmacological activities and their use as versatile building blocks for regio-, chemio-and stereoselective reactions. Thus, the synthesis of selenium-containing quinolines has great significance, and their applicability range from simple antioxidant agents, to selective DNA-binding and photocleaving agents. Objective: In the present study we describe the synthesis and antioxidant activity in vitro of new 7-chloroN(arylselanyl)quinolin-4-amines 5 by the reaction of 4,7-dichloroquinoline 4 with (arylselanyl)-amines 3. Methods: For the synthesis of 7-chloro-N(arylselanyl)quinolin-4-amines 5, we performed the reaction of (arylselanyl)- amines 3 with 4,7-dichloroquinoline 4 in the presence of Et3N at 120 °C in a sealed tube. The antioxidant activities of the compounds 5 were evaluated by the following in vitro assays: 2,2- diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2,2-azinobis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS), ferric ion reducing antioxidant power (FRAP), nitric oxide (NO) scavenging and superoxide dismutase-like activity (SOD-Like). Results: 7-Chloro-N(arylselanyl)quinolin-4-amines 5a-d has been synthesized in yields ranging from 68% to 82% by the reaction of 4,7-dichloroquinoline 4 with arylselanyl-amines 3a-d using Et3N as base, at 120 °C, in a sealed tube for 24 hours and tolerates different substituents, such as -OMe and -Cl, in the arylselanyl moiety. The obtained compounds 5a-d presented significant results with respect to the antioxidant potential, which had effect in the tests of inhibition of radical’s DPPH, ABTS+ and NO, as well as in the test that evaluates the capacity (FRAP) and in the superoxide dismutase-like activity assay (SOD-Like). It is worth mentioning that 7-chloro-N(arylselanyl)quinolin-4-amine 5b presented excellent results, demonstrating a better antioxidant capacity when compared to the others. Conclusion: According to the obtained results 7-chloro-N(arylselanyl)quinolin-4-amines 5 were synthesized in good yields by the reaction of 4,7-dichloroquinoline with arylselanyl-amines and tolerates different substituents in the arylselanyl moiety. The tested compounds presented significant antioxidant potential in the tests of inhibition of DPPH, ABTS+ and NO radicals, as well as in the FRAP and superoxide dismutase-like activity assays (SOD-Like).

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10-gingerol induces oxidative stress through HTR1A in cumulus cells: in-vitro and in-silico studies

Journal of Complementary and Integrative Medicine ◽

10.1515/jcim-2019-0042 ◽

2020 ◽

Vol 0 (0) ◽

Author(s):

Kiptiyah Kiptiyah ◽

Widodo Widodo ◽

Gatot Ciptadi ◽

Aulanni’am Aulanni’Am ◽

Mohammad A. Widodo ◽

...

Keyword(s):

Oxidative Stress ◽

Cell Culture ◽

Superoxide Dismutase ◽

In Silico ◽

Cumulus Cell ◽

Cumulus Cells ◽

Sod Activity ◽

In Silico Studies ◽

Incubation Periods

AbstractBackgroundWe investigated whether 10-gingerol is able to induce oxidative stress in cumulus cells.MethodsFor the in-vitro research, we used a cumulus cell culture in M199, containing 10-gingerol in various concentrations (0, 12, 16, and 20 µM), and detected oxidative stress through superoxide dismutase (SOD) activity and malondialdehyde (MDA) concentrations, with incubation periods of 24, 48, 72, and 96 h. The obtained results were confirmed by in-silico studies.ResultsThe in-vitro data revealed that SOD activity and MDA concentration increased with increasing incubation periods: SOD activity at 0 µM (1.39 ± 0.24i), 12 µM (16.42 ± 0.35ab), 16 µM (17.28 ± 0.55ab), 20 µM (17.81 ± 0.12a), with a contribution of 71.1%. MDA concentration at 0 µM (17.82 ± 1.39 l), 12 µM (72.99 ± 0.31c), 16 µM (79.77 ± 4.19b), 20 µM (85.07 ± 2.57a), with a contribution of 73.1%. Based on this, the in-silico data uncovered that 10˗gingerol induces oxidative stress in cumulus cells by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.Conclusions10-gingerol induces oxidative stress in cumulus cells through enhancing SOD activity and MDA concentration by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.

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