1. Response of rat alveolar type II cells and human lung tumor cells towards oxidative stress induced by hydrogen peroxide and paraquat.
- Author
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Weidauer E, Lehmann T, Rämisch A, Röhrdanz E, and Foth H
- Subjects
- ATP Binding Cassette Transporter, Subfamily B genetics, Animals, Catalase metabolism, Cell Line, Tumor, Humans, Hydrogen Peroxide toxicity, Lung Neoplasms pathology, Male, Malondialdehyde metabolism, Microscopy, Electron, Oxidative Stress physiology, Paraquat toxicity, Pulmonary Alveoli pathology, RNA genetics, Rats, Rats, Wistar, Reverse Transcriptase Polymerase Chain Reaction, Superoxide Dismutase metabolism, ATP-Binding Cassette Sub-Family B Member 4, ATP Binding Cassette Transporter, Subfamily B metabolism, Hydrogen Peroxide pharmacology, Lung Neoplasms drug therapy, Lung Neoplasms metabolism, Paraquat pharmacology, Pulmonary Alveoli drug effects, Pulmonary Alveoli metabolism
- Abstract
The expression of MDR1b coding mRNA is increased in alveolar type II cells from juvenile rat lung in culture. Hydrogen peroxide and paraquat-induced further upregulation supporting that oxidative stress mediated mechanisms are involved in the regulation of MDR1b in rat lung. The expression rates of mRNA for catalase, Cu/Zn-superoxide dismutase (Cu/Zn-SOD) and Mn-superoxide dismutase (Mn-SOD) remains constant during culture and were not modulated by hydrogen peroxide or paraquat. Thus, antioxidative enzymes in primary A II cells from rat lung are not regulated by reactive oxygen species dependent mechanisms. Primary A II cells were substantially more sensitive towards paraquat-induced cytotoxicity and lipid peroxidation than the permanent human lung tumor cell lines H322 and H358. A 100 microM hydrogen peroxide for 2h induces substantial DNA damage which is not paralleled by an increased rate of lipid peroxidation. The expression rate of mRNA coding for catalase and Mn-SOD was not changed and almost the same is true for the activity of catalase and Cu/Zn-SOD. Only 50 microM paraquat induced a significant decrease in catalase activity and an increase in Cu/Zn-SOD activity.
- Published
- 2004
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