Bromosulfophthalein abolishes glutathione-dependent protection against lipid peroxidation in rat liver mitochondria |
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| Authors: | M Yonaha Y Tampo |
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| Affiliation: | 1. Biomarkers in Cancer Unit, Biocruces-Bizkaia Health Research Institute, 48903 Barakaldo, Bizkaia, Spain;2. Department of Pathology, Cruces University Hospital, University of the Basque Country (UPV/EHU), 48903 Barakaldo, Bizkaia, Spain;3. Quantitative Biomedicine Unit, Biocruces-Bizkaia Health Research Institute, 48903 Barakaldo, Bizkaia, Spain;4. Pediatric Oncology and Hematology, Cruces University Hospital, 48903 Barakaldo, Bizkaia, Spain;5. IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Bizkaia, Spain;6. Department of Tumor Biology, Institute for Cancer Research, Oslo University Hospital Radiumhospitalet, N-0424 Oslo, Norway;7. Department of Cell Biology and Histology, University of the Basque Country (UPV/EHU), 48940 Leioa, Bizkaia, Spain;1. Department of Pathological Biochemistry, Otto-von-Guericke University, D-39120 Magdeburg, Germany;2. Institute of Medical Biochemistry and Molecular Biology, Ernst-Moritz-Arndt-University, D-17475 Greifswald, Germany;3. Institute of Molecular and Clinical Immunology, Otto-von-Guericke University, D-39120 Magdeburg, Germany |
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| Abstract: | The effect of bromosulfophthalein (BSP) on GSH-dependent protection against lipid peroxidation in rat liver mitochondria was examined. Mitochondrial lipid peroxidation induced by ascorbate-Fe2+ was prevented by GSH, and addition of BSP abolished the protective effect of GSH. The effect of BSP was apparently not due to causing disappearance of GSH from the reaction mixture by interacting directly with GSH. BSP strongly inhibited the mitochondrial GSH S-transferase activity rather than the GSH peroxidase activity. Ascorbate-Fe2+-induced lipid peroxidation in mitochondria without addition of GSH was also stimulated to some extent by BSP, and the stimulation seems likely to be due to abolition of the inhibitory effect of endogenous GSH. GSH could not be replaced as an inhibitor of lipid peroxidation by cysteine, beta-mercaptoethanol, or dithiothreitol. The inhibitory effect of GSH on lipid peroxidation was not observed in vitamin E-deficient mitochondria. No inhibitory effect of exogenous vitamin E was demonstrated either in vitamin E-deficient mitochondria or in vitamin E-sufficient mitochondria in the presence of BSP, whether GSH was added or not. These results indicate that a mitochondrial GSH-dependent factor which inhibits lipid peroxidation requires vitamin E to exert its function. It is suggested that mitochondrial GSH S-transferase(s) may be responsible for GSH-dependent inhibition of lipid peroxidation in mitochondria, probably by scavenging lipid radicals. |
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