Selective Induction of Liver Parenchymal Cell Heme Oxygenase-1 in Selenium-Deficient Rats
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V. Mostert
Abstract
Liver heme oxygenase (HO) activity is higher in selenium-deficient rats than in control animals under basal conditions and is further increased in them, but not in controls, by phenobarbital treatment. In the present study we characterized liver HO induction by selenium deficiency using molecular methods. Severe selenium deficiency in rats caused a doubling of liver HO activity without affecting spleen, kidney, brain, or testis HO activities. HO-1 protein and mRNA were increased to accompany the increased HO activity, but HO-2 protein and mRNA were not increased. Fractionation of the liver into hepatocyte and Kupffer cell/endothelial cell fractions revealed that the increased HO activity resides in the hepatocyte fraction. Immunohistochemical localization of HO-1 protein confirms the induction of HO-1 taking place solely in hepatocytes and throughout the liver lobule. Phenobarbital treatment sharply increased HO-1 mRNA and protein expression in selenium-deficient liver and HO activity in hepatocytes, but had no effect in control liver or in the Kupffer cell/endothelial cell fraction of selenium-deficient liver. Electrophoretic mobility shift assays showed increased AP-1 binding activity, suggesting an involvement of this redoxsensitive transcription factor in the induction by phenobarbital of HO-1 in selenium deficiency. We speculate that selenium deficiency affects hepatic antioxidant selenoproteins, resulting in an upregulation of HO-1.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- Biosynthesis of Trypanothione in Trypanosoma brucei brucei
- Transcriptional Regulation of Cytosol and Membrane Alanyl-Aminopeptidase in Human T Cell Subsets
- Regulation of Gene Transcription by a Constitutively Active Mutant of Activating Transcription Factor 2 (ATF2)
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- Selective Induction of Liver Parenchymal Cell Heme Oxygenase-1 in Selenium-Deficient Rats
Articles in the same Issue
- Glutathione, Related Enzymology, and Leopold Flohé
- 'Lest I Forget Thee, Glutathione...'
- Glutathione Pathways in the Brain
- The Role of Glutathione Peroxidases in Trypanosomatids
- Cytoprotection against Oxidative Stress and the Regulation of Glutathione Synthesis
- The Parasite-Specific Trypanothione Metabolism of Trypanosoma and Leishmania
- Glutathione – Functions and Metabolism in the Malarial Parasite Plasmodium falciparum
- Oxidative Stress Caused by Inactivation of Glutathione Peroxidase and Adaptive Responses
- Versatility of Selenium Catalysis in PHGPx Unraveled by LC/ESI-MS/MS
- Modulation of the Chymotrypsin-Like Activity of the 20S Proteasome by Intracellular Redox Status: Effects of Glutathione Peroxidase-1 Overexpression and Antioxidant Drugs
- Microflora Trigger Colitis in Mice Deficient in Selenium-Dependent Glutathione Peroxidase and Induce Gpx2 Gene Expression
- Recruitment of the Interleukin-1 Receptor (IL-1RI)-Associated Kinase IRAK to the IL-1RI Is Redox Regulated
- Kinetics and Redox-Sensitive Oligomerisation Reveal Negative Subunit Cooperativity in Tryparedoxin Peroxidase of Trypanosoma brucei brucei
- Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx)
- Selective Recognition of Peptide Sequences by Glutathione Transferases: A Possible Mechanism for Modulation of Cellular Stress-Induced Signaling Pathways
- Biosynthesis of Trypanothione in Trypanosoma brucei brucei
- Transcriptional Regulation of Cytosol and Membrane Alanyl-Aminopeptidase in Human T Cell Subsets
- Regulation of Gene Transcription by a Constitutively Active Mutant of Activating Transcription Factor 2 (ATF2)
- Solvent Isotope Effect on the Reaction Catalysed by the Pyruvate Dehydrogenase Complex from Escherichia coli
- Selective Induction of Liver Parenchymal Cell Heme Oxygenase-1 in Selenium-Deficient Rats
