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peroxidase/hypoxie
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Increased expression of mitochondrial peroxiredoxin-3 (thioredoxin peroxidase-2) protects cancer cells against hypoxia and drug-induced hydrogen peroxide-dependent apoptosis.
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Peroxiredoxin-3 (Prdx3) is a mitochondrial member of the antioxidant family of thioredoxin peroxidases that uses mitochondrial thioredoxin-2 (Trx2) as a source of reducing equivalents to scavenge hydrogen peroxide (H(2)O(2)). Low levels of H(2)O(2) produced by the mitochondria regulate physiological
Impairment of synaptic transmission by transient hypoxia in hippocampal slices: improved recovery in glutathione peroxidase transgenic mice.
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There is increasing evidence that oxygen free radicals contribute to ischemic brain injury. It is unclear, however, to what extent specific antioxidant enzymes can prevent or reverse the impairment of synaptic function caused by transient hypoxia. In this study, we investigated in transgenic (Tg)
Alteration in Downstream Hypoxia Gene Signaling in Neonatal Glutathione Peroxidase Overexpressing Mouse Brain after Hypoxia-Ischemia.
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We have previously shown that glutathione peroxidase (GPx) overexpressing mice (hGPx-tg) have reduced brain injury after neonatal hypoxia-ischemia (HI) as a consequence of reduced hydrogen peroxide accumulation. However, this protection is reversed with hypoxia preconditioning, raising the question
[Lipid peroxidation, peroxidase activity and glutathione antiperoxide systems in rat tissues under conditions of high altitude hypoxia].
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The content of lipid peroxides in rat tissues does not vary essentially under conditions of high altitude hypoxia. The peroxidase activity undergoes fluctuating changes with a significant increase in brain tissues. Among the enzymes of the glutathione antiperoxide system only the glutathione
[The peroxidase activity of rat cerebral hemisphere neurons during hypoxia training].
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Peroxidase activity (PA) was studied in the rat's brain cortex during a 2 months training to hypoxia according to the Barbashova method. PA was investigated histochemically by an ammonium--molibdate--benzidine method on blocks of surviving brain tissue, thereafter they were studied by the contact
Selenoprotein M gene expression, peroxidases activity and hydrogen peroxide concentration are differentially regulated in gill and hepatopancreas of the white shrimp Litopenaeus vannamei during hypoxia and reoxygenation.
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In many organisms, episodes of low O2 concentration (hypoxia) and the subsequent rise of O2 concentration (reoxygenation) result in the accumulation of reactive oxygen species and oxidative stress. Selenoprotein M (SelM), is a selenocysteine containing protein with redox activity involved in the
Glutathione peroxidase 3 (GPX3) suppresses the growth of melanoma cells through reactive oxygen species (ROS)-dependent stabilization of hypoxia-inducible factor 1-α and 2-α.
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In this study, we aimed to explore the mechanism of glutathione peroxidase 3 (GPX3) in the growth of malignant melanoma (MM) cells by hypoxia-inducible factor-1α (HIF1-α) and HIF2-α regulating the metabolism through reactive oxygen species (ROS). The messenger RNA and protein expression of GPX3,
Glutathione peroxidase and glutathione S-transferase in blood and liver from a hypoxia-tolerant fish under oxygen deprivation.
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Liver enzyme activities can be employed as biomarkers, but liver can only be obtained with death of the specimen. On the other hand, blood withdrawal is a non-lethal procedure. Accordingly, the hypothesis of this study is to verify if glutathione peroxidase (GPX) and glutathione S-transferase (GST)
Hypoxic preconditioning reverses protection after neonatal hypoxia-ischemia in glutathione peroxidase transgenic murine brain.
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The effect of hypoxic preconditioning (PC) on hypoxic-ischemic (HI) injury was explored in glutathione peroxidase (GPx)-overexpressing mice (human GPx-transgenic [hGPx-tg]) mice. Six-day-old hGPx-tg mice and wild-type (Wt) littermates were pre-conditioned with hypoxia for 30 min and subjected to the
Roles of catalase and glutathione peroxidase in the tolerance of a pulmonate gastropod to anoxia and reoxygenation.
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Humans and most mammals suffer severe damage when exposed to ischemia and reperfusion episodes due to an overproduction of reactive oxygen species (ROS). In contrast, several hypoxia/anoxia-tolerant animals survive very similar situations. We evaluated herein the redox metabolism in the
Enhanced expression of glutathione peroxidase protects islet beta cells from hypoxia-reoxygenation.
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The survival of pancreatic islet beta-cell xenografts and allografts may be affected by damaging reactive oxygen and nitrogen species generated during hypoxia-reoxygenation. Peroxynitrite, which is formed from superoxide and nitric oxide, appears to be an important mediator of beta-cell destruction.
Coordination between NADPH oxidase and vascular peroxidase 1 promotes dysfunctions of endothelial progenitor cells in hypoxia-induced pulmonary hypertensive rats.
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Previous studies have demonstrated that NADPH oxidase (NOX)/vascular peroxidase (VPO1) pathway - mediated oxidative stress plays an important role in the pathogenesis of multiple cardiovascular diseases. This study aims to evaluate the correlation between NOX/VPO1 pathway and endothelial progenitor
Assessment of reactive oxygen species production in cultured equine skeletal myoblasts in response to conditions of anoxia followed by reoxygenation with or without exposure to peroxidases.
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OBJECTIVE
To culture equine myoblasts from muscle microbiopsy specimens, examine myoblast production of reactive oxygen species (ROS) in conditions of anoxia followed by reoxygenation, and assess the effects of horseradish peroxidase (HRP) and myeloperoxidase (MPO) on ROS production.
METHODS
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Glutathione peroxidase 1 protects mitochondria against hypoxia/reoxygenation damage in mouse hearts.
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Glutathione peroxidase 1 (GPx1) plays an important role in preventing cardiac dysfunction following ischemia-reperfusion injury. However, its role in protecting cardiac mitochondria against reoxygenation-induced reactive oxygen species (ROS) generation in vivo is unclear. We examined the role of
Anoxia pretreatment protects soybean cells against H(2)O(2)-induced cell death: possible involvement of peroxidases and of alternative oxidase.
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Anoxia followed by reoxygenation causes extensive damage to cellular components through generation of reactive oxygen intermediates. We examined cellular responses to oxidative stress after anoxia in cultured soybean or human fibroblast cells. Anoxia pretreatment protected soybean but not
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