Differential protein expression due to Se deficiency and Se toxicity in rat liver |
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| Institution: | 1. Department of Nutrition, Dietetics and Food, Monash University, VIC, Australia;2. The Florey Institute of Neuroscience and Mental Health, CRC for Mental Health, University of Melbourne, Australia;3. Center for Natural Sciences and Humanities, Universidade Federal do ABC, Santo André, Brazil;4. Department of Nutritional Sciences, University of Wisconsin, Madison, Wisconsin, USA;5. Department of Biochemistry, Emory School of Medicine, Atlanta, Georgia, USA;6. Department of Neurology, Emory School of Medicine, Atlanta, Georgia, USA;1. Department of Chemistry, The University of Adelaide, South Australia 5005, Australia,;2. The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Victoria 3000, Australia,;1. Nutrition Research Institute, University of North Carolina at Chapel Hill, Kannapolis, North Carolina,;2. Department of Biochemistry & Molecular Biology, Hollings Cancer center, Medical University of South Carolina, 173 Ashley Avenue, Charleston, South Carolina,;3. Department of Nutrition, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina,;1. Linus Pauling Institute, Oregon State University, Corvallis, Oregon;2. Integrative Biology Program, Oregon State University, Corvallis, Oregon;3. Molecular and Cell Biology Program;4. Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, Oregon;5. School of Biological and Population Health Sciences, Oregon State University, Corvallis, Oregon;1. Department of Nutrition, Texas A&M University, College Station, Texas, USA;2. Department of VIP Medical Service Center, the Third Affiliated Hospital of Sun Yat-sen University, Guangzhou, Guangdong, China;3. Department of Veterinary Integrative Biosciences, Texas A&M University, College Station, Texas, USA;4. Medical Physiology, Texas A&M University College of Medicine, Bryan, Texas, USA;5. Hepatology and Gastroenterology, Medicine, Indiana University, Indianapolis, Indiana, USA;6. Richard L. Roudebush VA Medical Center, Indianapolis, Indiana, USA |
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| Abstract: | There is a U-shaped dose-response between selenium (Se) status and health outcomes, but underlying metabolic processes are unclear. This study aims to identify candidate proteins in liver regulated by dietary Se, ranging from deficiency to toxic. Male rats (n=4) were fed graded Se concentrations as selenite for 28 days. Bulk Se analysis was performed by ICP-MS on both soluble and insoluble fractions. Soluble fraction samples were chromatographically separated for identification of selenocompounds by SEC-ICP-MS and protein quantification by LC-MS/MS. Bioinformatics analysis compared low-Se (0 and 0.08 µg Se g−1) and high-Se (0.8, 2 and 5 µg Se g−1) with adequate-Se (0.24 µg Se g−1) diets. Major breakpoints for Se were seen at 0.8 and 2 µg Se g−1 in the insoluble and soluble fractions, respectively. Glutathione peroxidase 1 protein abundance reached a plateau at ≥0.08 µg Se g−1diet; Se bound to selenium binding protein 2 was observed with 2 and 5 µg Se g−1 Se. The extreme diets presented the highest number of differentially expressed (P value <0.05, FC ≥1.2) proteins in comparison to the adequate-Se diet (0 µg Se g−1: 45 proteins; 5 µg Se g−1: 59 proteins); 13 proteins were commonly affected in 0 and 5 µg Se g−1 treatments. Network analysis revealed that the metabolism of glutathione, xenobiotics and amino acids were enriched in both 0 and 5 µg Se g−1 diets, indicating a U-shape effect of Se. This similarity is likely due to down-stream effects of lack of essential selenoproteins in Se deficiency and due to toxic effects of Se that exceeds the capacity to cope with excess Se. |
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