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Copper, zinc-superoxide
dismutase (SOD1) and selenium-dependent cellular glutathione
peroxidase-1 (GPX1) are two primary intracellular antioxidant enzymes.
SOD1 converts superoxide anions into hydrogen peroxide that is in turn
reduced to water by GPX1. Our lab has demonstrated the protection of
GPX1 against reactive oxygen species (ROS)-related oxidative stress both
in vitro and in vivo. However, GPX1 and SOD1 might have different
functions against reactive nitrogen species (RNS)-related oxidative
stress. Using GPX1 and SOD1 knockout mouse model, we have found that
knockout of SOD1 and double-knockout of SOD1 and GPX1 enhanced mouse
resistance to acetaminophen-induced toxicity. Currently we are studying the
impact of GPX1 and SOD1 on nitric oxide production and the formation of
protein nitration.
Another main interest of
our group is to study the function of GPX1
and SOD1 in the insulin-related pathways. Antioxidant enzymes impart
vital roles in regulating homeostasis of ROS and mediating mitochondrial
potential and insulin secretion. Our lab has shown the development of
insulin resistance and obesity in GPX1 overexpressing mice. To further
investigate this issue, we also apply SOD1 and GPX1 knockout mouse models
to study the impact of these two antioxidant enzymes on insulin
secretion and its function.
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The physiological importance and
biochemical mechanism of GPX1 in protecting Se-deficient
or Se-adequate mice against severe vs. moderate
oxidative stress by Lei & Cheng. Cover page of the
Journal of Nutrition: Oct., 2005 |
Comparison of GPX1 Overpressing
Mice (Obese) vs. Wild Type Mice |
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