Oxidative Stress Caused by Inactivation of Glutathione Peroxidase and Adaptive Responses
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Y. Miyamoto
Abstract
Reactive oxygen species (ROS) are generated as by-products of cellular metabolism, primarily in the mitochondria. When the cellular production of ROS exceeds the cell's antioxidant capacity, cellular macromolecules such as lipids, proteins and DNA can be damaged. Because of this, 'oxidative stress' is thought to contribute to aging and pathogenesis of a variety of human diseases. However, in the last 10-15 years, a considerable body of evidence has accumulated that ROS serve as subcellular messengers, and play a role in gene regulation and signal transduction pathways, which may be involved in defensive mechanisms against oxidative stress. This review focuses on oxidative stress caused by the inactivation of glutathione peroxidase (GPx), a major peroxide scavenging enzyme. GPx is inactivated by a variety of physiological substances, including nitric oxide and carbonyl compounds in vitro and in cell culture. Decreased GPx activity has also been reported in tissues where oxidative stress occurs in several pathological animal models. The accumulation of increased levels of peroxide resulting from inactivation of GPx may act as a second messenger and regulate expression of antiapoptotic genes and the GPx itself to protect against cell damage. These findings suggest that GPx undergoes inactivation under various conditions such as nitroxidative stress and glycoxidative stress, and that these changes are a common feature of various types of oxidative stress which may be associated with the modification of redox regulation and cellular function.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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
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
