Rat testis mitochondrial phospholipid hydroperoxide glutathione peroxidase does not protect endogenous vitamin E against Fe2+-induced (lipo)peroxidation
Autor: | Enrico Panfili, Federica Tramer, Gabriella Sandri, Cristiana Godeas |
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Rok vydání: | 1996 |
Předmět: |
Vitamin
Male medicine.medical_treatment Iron Iodoacetates Mitochondrion GPX4 Biochemistry Lipid peroxidation chemistry.chemical_compound Membrane Lipids Testis medicine Animals Vitamin E Phospholipid-hydroperoxide glutathione peroxidase Chromatography High Pressure Liquid Phospholipids Mercaptoethanol chemistry.chemical_classification Glutathione Peroxidase biology Cell Membrane Age Factors Rats Inbred Strains Phospholipid Hydroperoxide Glutathione Peroxidase Glutathione Enzyme assay Iodoacetic Acid Mitochondria Rats Enzyme chemistry biology.protein Lipid Peroxidation |
Zdroj: | Biochemical and molecular medicine. 58(2) |
ISSN: | 1077-3150 |
Popis: | Rat testis mitochondria contain large amounts of both seleno-enzyme phospholipid hydroperoxide glutathione peroxidase (EC 1.11.1.12, PHGPx) and α-tocopherol. The scavenger role of vitamin E consists of transforming the lipoperoxyl radicals into lipid hydroperoxides, thus interrupting the peroxidative cascade. These hydroperoxides are in turn substrates of the PHGPx, which is considered one of the most important specific enzymes capable of protecting, in situ, the membranes from lipid peroxidation. A connection or synergism could, therefore, be envisaged between vitamin and enzyme opposing lipid damage in the mitochondria. Here we present data concerning the HPLC evaluation of vitamin E consumption in rat testis mitochondria and mitochondrial membranes, under different conditions of PHGPx activity, after Fe 2+ -induced lipid peroxidation. We have found that the enzyme activity, under the conditions tested, does not spare vitamin E from its peroxidation, therefore indicating that the postulated synergism between PHGPx and α-tocopherol can be excluded in rat testis mitochondria. |
Databáze: | OpenAIRE |
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