Post-transcriptional control of increased hepatic catalase gene expression in response to oxidative stress
- 1 August 1996
- journal article
- other
- Published by Taylor & Francis in Redox Report
- Vol. 2 (4) , 273-278
- https://doi.org/10.1080/13510002.1996.11747061
Abstract
Summary Catalase is an important member of the antioxidant network that protects the cell against reactive oxygen species (ROS). We studied catalase gene expression in the liver of rats exposed to oxidative stress induced by the ROS-generating drug nitrofurantoin (NF). Catalase enzymatic activity and content are enhanced by NF treatment. The corresponding increase in the steady state level of the messenger ribonucleic acid (mRNA) occurs without significant changes in transcription and seems therefore controlled post-transcriptionally. Indeed, RNA band-shift assays demonstrated a reduced binding of redox-sensitive cytoplasmic protein(s) to the 3′ region of catalase mRNA in NF-treated rats, thus suggesting that the redox state of protein that binds to an antioxidant enzyme mRNA may play a role in the hepatic response to oxidative stress.Keywords
This publication has 33 references indexed in Scilit:
- Nitric‐Oxide‐Mediated Activation of Iron‐Regulatory Protein Controls Hepatic Iron Metabolism During Acute InflammationEuropean Journal of Biochemistry, 1995
- Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selectionCell, 1994
- Complete cDNA and 5′ Genomic Sequences and Multilevel Regulation of the Mouse Catalase GeneGenomics, 1994
- Free Radicals in ToxicologyToxicology and Applied Pharmacology, 1993
- Redox redux: The control of oxidative stress responsesCell, 1991
- Transcriptional Regulator of Oxidative Stress-Inducible Genes: Direct Activation by OxidationScience, 1990
- Changes in the expression of superoxide dismutase and catalase as a function of age and dietary restrictionBiochemical and Biophysical Research Communications, 1989
- The measurement of free radical reactions in humansFEBS Letters, 1987
- Antioxidant Defenses in the LungAnnual Review of Physiology, 1986
- Nucleoside and nucleotide inactivation of R17 coat protein: evidence for a transient covalent RNA-protein bondBiochemistry, 1985