The overexpression of NADPH-producing enzymes counters the oxidative stress evoked by gallium, an iron mimetic
Autor: | Vasu D. Appanna, R. Hamel, H. Joly, Ryan J. Mailloux, Daniel Chenier, Robin Beriault |
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Rok vydání: | 2006 |
Předmět: |
Iron
Gallium Pseudomonas fluorescens Oxidative phosphorylation Glucosephosphate Dehydrogenase medicine.disease_cause Thiobarbituric Acid Reactive Substances General Biochemistry Genetics and Molecular Biology Biomaterials Superoxide dismutase chemistry.chemical_compound medicine Homeostasis Glucose-6-phosphate dehydrogenase chemistry.chemical_classification Reactive oxygen species biology Superoxide Dismutase Metals and Alloys Hydrogen Peroxide Metabolism Catalase Oxidants biology.organism_classification Isocitrate Dehydrogenase Enzyme Activation Isoenzymes Oxidative Stress chemistry Biochemistry Enzyme Induction biology.protein Reactive Oxygen Species General Agricultural and Biological Sciences Oxidation-Reduction NADP Oxidative stress |
Zdroj: | BioMetals. 20:165-176 |
ISSN: | 1572-8773 0966-0844 |
DOI: | 10.1007/s10534-006-9024-0 |
Popis: | Gallium (Ga), an iron (Fe) mimetic promoted an oxidative environment and elicited an antioxidative response in Pseudomonas fluorescens. Ga-stressed P. fluorescens was characterized by higher amounts of oxidized lipids and proteins compared to control cells. The oxidative environment provoked by Ga was nullified by increased synthesis of NADPH. The activity and expression glucose 6-phosphate dehydrogenase (G6PDH) and isocitrate dehydrogenase-NADP (ICDH) were stimulated in Ga-cultures. The induction of isoenzymes of these dehydrogenases was also evident in the Ga-stressed cells. Although superoxide dismutase (SOD) activity was significantly enhanced in Ga-stressed cultures, catalase activity experienced a marked diminution. Fe metabolism appeared to be severely impeded by Ga toxicity. This is the first demonstration of the oxidative stress evoked by Ga to be neutralized by a reductive environment generated via the overexpression of NADPH-producing enzymes. |
Databáze: | OpenAIRE |
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