Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress (Q28372953)

GOA release 2020-03-11

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Y Fu

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W H Cheng

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J M Porres

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D A Ross

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X G Lei

Free Radical Biology and Medicine

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language of work or name

English

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publication date

September 1999

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published in

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volume

27

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issue

5-6

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page(s)

605-11

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cites work

Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides

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Liver necrosis and lipid peroxidation in the rat as the result of paraquat and diquat administration. Effect of selenium deficiency

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Effect of BCNU pretreatment on diquat-induced oxidant stress and hepatotoxicity.

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Glutathione peroxidase: a selenoenzyme

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Selenium: Biochemical Role as a Component of Glutathione Peroxidase

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Cellular glutathione peroxidase knockout mice express normal levels of selenium-dependent plasma and phospholipid hydroperoxide glutathione peroxidases in various tissues

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7 January 2021

Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia

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7 January 2021

Cellular glutathione peroxidase is the mediator of body selenium to protect against paraquat lethality in transgenic mice

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7 January 2021

Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide.

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A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism.

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Mass spectrometry of prostanoids: F2-isoprostanes produced by non-cyclooxygenase free radical-catalyzed mechanism

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Determination of carbonyl content in oxidatively modified proteins

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Oxidative damage to proteins: spectrophotometric method for carbonyl assay

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Glutathione peroxidase activity in rat lens and other tissues in relation to dietary selenium intake

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Phospholipid hydroperoxide glutathione peroxidase

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Thioredoxin and thioredoxin reductase

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Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3'--1--(phenylamino)-carbonyl--3, 4-tetrazolium]-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase

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Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats.

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Tissue specificity of selenoprotein gene expression in rats

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Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme

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Rat skeletal muscle selenoprotein W: cDNA clone and mRNA modulation by dietary selenium

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The selenium requirement for glutathione peroxidase mRNA level is half of the selenium requirement for glutathione peroxidase activity in female rats

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7 January 2021

Dietary selenium intake controls rat plasma selenoprotein P concentration

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Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay

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Deterioration of membrane morphology, phospholipids, and cytoskeletal protein in rat erythrocytes exposed to tert-butyl hydroperoxide: protection by exogenous glutathione fails in selenium deficiency

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Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation

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Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide.

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7 January 2021