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Expression profiling reveals novel hypoxic biomarkers in peripheral blood of adult mice exposed to chronic hypoxia.
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Hypoxia induces a myriad of changes including an increase in hematocrit due to erythropoietin (EPO) mediated erythropoiesis. While hypoxia is of importance physiologically and clinically, lacunae exist in our knowledge of the systemic and temporal changes in gene expression occurring in blood during
Generation of free radicals in Langendorff and working hearts during normoxia, hypoxia, and reoxygenation.
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The release of .OH and alkyl free radicals into the coronary flow were compared in Langendorff perfused and working rat hearts during normoxia (30 min), hypoxia (30 min) and reoxygenation (60 min) by means of spin-trapping techniques using 5,5-dimethyl-1-pyrroline-1-oxide (DMPO). In Langendorff
Oxygen radical generation and enzymatic properties of mitochondria in hypoxia/reoxygenation.
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The time-dependence of oxygen radical formation and development of enzymatic dysfunction after hypoxia/reoxygenation was investigated in isolated rat liver mitochondria. Generation of oxygen radicals was studied by electron paramagnetic resonance (EPR) spectroscopy using the spin trap DMPO
Injury to cultured liver endothelial cells after cold preservation: mediation by reactive oxygen species that are released independently of the known trigger hypoxia/reoxygenation.
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When cultured liver endothelial cells were incubated in cold University of Wisconsin (UW) solution under hypoxic conditions, 3 +/- 2% of cells had lost viability after 25 h. Simulating reperfusion by returning the cells to normal cell culture conditions increased the injury to 30 +/- 11% after 3 h
Determination of the mechanism of free radical generation in human aortic endothelial cells exposed to anoxia and reoxygenation.
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Endothelial cell-derived oxygen free radicals are important mediators of postischemic injury; however, the mechanisms that trigger this radical generation are not known, and it is not known if this process can occur in human cells and tissues. The enzyme xanthine oxidase can be an important source
Manganese superoxide dismutase modulates hypoxia-inducible factor-1 alpha induction via superoxide.
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Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that plays an important role in O(2) homeostasis. Numerous observations suggest that changes in reactive oxygen species affect HIF-1 alpha stabilization and HIF-1 alpha transcriptional activation in many cell types. The antioxidant enzyme
Regulation of proline metabolism in mycobacteria and its role in carbon metabolism under hypoxia.
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Genes with a role in proline metabolism are strongly expressed when mycobacterial cells are exposed to nutrient starvation and hypoxia. Here we show that proline metabolism in mycobacteria is mediated by the monofunctional enzymes Δ(1) -pyrroline-5-carboxylate dehydrogenase (PruA) and proline
Free radical generation coupled with arachidonate lipoxygenase reaction relates to reoxygenation induced myocardial cell injury.
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OBJECTIVE
The role of arachidonate lipoxygenase activity in reoxygenation induced cell injury in adult canine cardiac myocytes was investigated.
METHODS
The production of hydroxyeicosatetraenoic acids (HETEs), which are lipoxygenase metabolites, was measured with high pressure liquid chromatography
Oxygen-free radical-mediated injury to cultured rat hepatocytes during cold incubation in preservation solutions.
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We have previously shown that the injury to cultured liver endothelial cells during cold incubation in University of Wisconsin (UW) solution is energy-dependent and is mediated by reactive oxygen species. Here we demonstrate that this reactive oxygen-mediated injury is specific neither to
Leptin's activity on the hydroxyl radical: a possible link to the oxidative stress-related endothelial vasodilation in patients with obstructive sleep apnea.
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OBJECTIVE
Obstructive sleep apnea (OSA) is associated with increased cardiovascular morbidity, whereas the underlying mechanism is still eluding, the thought participants are chronic intermittent hypoxia with consequent increase in the reactive oxygen species, leading to endothelial cell damage and
Radical Chemistry and Cytotoxicity of Bioreductive 3-Substituted Quinoxaline Di-N-Oxides.
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The radical chemistry and cytotoxicity of a series of quinoxaline di-N-oxide (QDO) compounds has been investigated to explore the mechanism of action of this class of bioreductive drugs. A series of water-soluble 3-trifluoromethyl (4-10), 3-phenyl (11-19), and 3-methyl (20-21) substituted QDO
Protection against SR 4233 (Tirapazamine) aerobic cytotoxicity by the metal chelators desferrioxamine and tiron.
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OBJECTIVE
Metal chelating agents and antioxidants were evaluated as potential protectors against aerobic SR 4233 cytotoxicity in Chinese hamster V79 cells. The differential protection of aerobic and hypoxic cells by two metal chelators, desferrioxamine and Tiron, is discussed in the context of their
Electron spin resonance investigation of the cyanyl and azidyl radical formation by cytochrome c oxidase.
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Cyanide (CN(-)) is a frequently used inhibitor of mitochondrial respiration due to its binding to the ferric heme a(3) of cytochrome c oxidase (CcO). As-isolated CcO oxidized cyanide to the cyanyl radical ((.)CN) that was detected, using the ESR spin-trapping technique, as the
Role of leptin as antioxidant in obstructive sleep apnea: an in vitro study using electron paramagnetic resonance method.
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BACKGROUND
As in obstructive sleep apnea (OSA), the chronic cycles of hypoxia and reoxygenation are thought to be conducive of oxidative stress (OS) with generation of reactive oxygen species, identifying effective mechanisms of protection against oxidant-mediated tissue damage becomes of outmost
Synthesis of prostaglandin H synthase-2 by human alveolar macrophages in response to lipopolysaccharide is inhibited by decreased cell oxidant tone.
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We previously demonstrated that lipopolysaccharide (LPS) increases expression of the prostaglandin H synthase-2 (PGHS-2) gene (Hempel, S.L., Monick, M.M., and Hunninghake, G.W. (1994) J. Clin. Invest. 93, 391-396). In this study, the expression of the PGHS-2 gene in response to changes in cell
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