Dataset Information

Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats.

ABSTRACT:

Background

The alterations of the glutathione peroxidase enzyme complex system occur in physiological conditions such as aging and oxidative stress consequent to strenuous exercise.

Methods

Authors optimize the spectrophotometric method to measure glutathione peroxidase activity in rat red blood cell membranes.

Results

The optimization, when applied to age paired rats, both nulligravid and pregnant, shows that pregnancy induces, at seventeen d of pregnancy, an increase of both reactive oxygen substance concentration in red blood cells and membrane glutathione peroxidase activity.

Conclusion

The glutathione peroxidase increase in erythrocyte membranes is induced by systemic oxidative stress long lasting rat pregnancy.

SUBMITTER: Gallo G

PROVIDER: S-EPMC2657797 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

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Publications

Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats.

Gallo Giuseppe G Martino Guglielmo G

Reproductive biology and endocrinology : RB&E 20090126

<h4>Background</h4>The alterations of the glutathione peroxidase enzyme complex system occur in physiological conditions such as aging and oxidative stress consequent to strenuous exercise.<h4>Methods</h4>Authors optimize the spectrophotometric method to measure glutathione peroxidase activity in rat red blood cell membranes.<h4>Results</h4>The optimization, when applied to age paired rats, both nulligravid and pregnant, shows that pregnancy induces, at seventeen d of pregnancy, an increase of b ...[more]

PMID: 19171040

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Project description:Huntington's disease (HD) is an autosomal dominantly inherited neurodegenerative disease characterized by symptoms attributable to the death of striatal and cortical neurons. The molecular mechanisms mediating neuronal death in HD involve oxidative stress and mitochondrial dysfunction. Administration of 3-nitropropionic acid (3-NP), an irreversible inhibitor of the mitochondrial enzyme succinate dehydrogenase, in rodents has been proposed as a useful experimental model of HD. This study evaluated the effects of probucol, a lipid-lowering agent with anti-inflammatory and antioxidant properties, on the biochemical parameters related to oxidative stress, as well as on the behavioral parameters related to motor function in an in vivo HD model based on 3-NP intoxication in rats. Animals were treated with 3.5 mg/kg of probucol in drinking water daily for 2 months and, subsequently, received 3-NP (25 mg/kg i.p.) once a day for 6 days. At the end of the treatments, 3-NP-treated animals showed a significant decrease in body weight, which corresponded with impairment on motor ability, inhibition of mitochondrial complex II activity and oxidative stress in the striatum. Probucol, which did not rescue complex II inhibition, protected against behavioral and striatal biochemical changes induced by 3-NP, attenuating 3-NP-induced motor impairments and striatal oxidative stress. Importantly, probucol was able to increase activity of glutathione peroxidase (GPx), an enzyme important in mediating the detoxification of peroxides in the central nervous system. The major finding of this study was that probucol protected against 3-NP-induced behavioral and striatal biochemical changes without affecting 3-NP-induced mitochondrial complex II inhibition, indicating that long-term probucol treatment resulted in an increased resistance against neurotoxic events (i.e., increased oxidative damage) secondary to mitochondrial dysfunction. These data appeared to be of great relevance when extrapolated to human neurodegenerative processes involving mitochondrial dysfunction and indicates that GPx is an important molecular target involved in the beneficial effects of probucol.

Dataset Information

Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats.

Background

Methods

Results

Conclusion

Publications

Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats.

Similar Datasets

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