Selenoprotein P protects cells from lipid hydroperoxides generated by 15-LOX-1 |
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| Affiliation: | 1. Institute of Chemistry, Saint Petersburg State University, RU–198504 Saint Petersburg, Russia;2. Department of Analytical Chemistry, University of P.J. Šafárik, SK-04154 Košice, Slovakia;1. Department of Child and Adolescent Mental Health, National Institute of Mental Health, National Center of Neurology and Psychiatry, Japan;2. Department of Neuropsychiatry, University of Fukui, Japan;3. Research Center for Child Mental Development, University of Fukui, Japan;4. Hiratani Child Development Clinic, Fukui, Japan;5. Department of Pediatrics, University of Fukui, Japan;1. Department of Clinical Research London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK;2. MRC International Nutrition Group, MRC Keneba, The Gambia;1. Planning and Technology, Sasol Polymers, Johannesburg, South Africa;2. Department of Chemistry and Polymer Science, University of Stellenbosch, South Africa;3. Sasol Technology, Sasolburg, South Africa;1. Centro/Departamento de Física da Universidade do Minho, Campus de Gualtar, 4710-057 Braga, Portugal;2. Departament de Química, Centro de Química, Universidade do Minho, Campus de Gualtar, 4710-057 Braga, Portugal |
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| Abstract: | Reactive lipid hydroperoxides formed by lipoxygenases and cyclooxygenases can contribute to disease through cellular oxidative damage. Several selenoproteins have lipid hydroperoxidase activity, including glutathione peroxidase 4, thioredoxin reductase, and selenoprotein P (SelP). SelP is an extracellular glycoprotein that functions both in selenium distribution and has an antioxidant activity. The major objective of this study was to determine if an SelP, at physiological concentrations and in selenium replete media, possessed hydroperoxidase activity directed at lipid hydroperoxides generated from the metabolism of arachidonic acid by 15-lipoxygenase-1 (15-LOX-1). An SelP displayed in vitro lipid hydroperoxidase activity of 15-hydroperoxyeicosatetraenoic acid (15-HpETE), attenuated 15-HpETE oxidation in cellular assays, and in transcellular assay when 15-LOX-1 is metabolically active. These results suggest that an SelP can function as an antioxidant enzyme against reactive lipid intermediates formed during inflammation, but an SelP has modest activity. Nevertheless, this effect may help protect cells against the oxidative damage induced by these lipid metabolites. |
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