Insulin-like and non-insulin-like selenium actions in 3T3-L1 adipocytes
| Autor: | Emma Heart, Chin K. Sung |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
inorganic chemicals
medicine.medical_specialty Time Factors Monosaccharide Transport Proteins Lipolysis medicine.medical_treatment Deoxyglucose Biochemistry Insulin Antagonists Mice Phosphatidylinositol 3-Kinases Selenium chemistry.chemical_compound Insulin receptor substrate Internal medicine Adipocytes medicine Animals Insulin Enzyme Inhibitors Phosphorylation Molecular Biology Protein kinase B Phosphoinositide-3 Kinase Inhibitors Glucose Transporter Type 1 Dose-Response Relationship Drug biology Cell Membrane Glucose transporter food and beverages Tyrosine phosphorylation 3T3 Cells Cell Biology IRS1 Androstadienes Enzyme Activation Insulin receptor Glucose Endocrinology chemistry biology.protein Wortmannin Signal Transduction |
| Zdroj: | Journal of Cellular Biochemistry. 88:719-731 |
| ISSN: | 1097-4644 0730-2312 |
| DOI: | 10.1002/jcb.10395 |
| Popis: | In insulin-sensitive 3T3-L1 adipocytes, selenium stimulates glucose transport and antilipolysis and these actions of selenium, like insulin actions, are sensitive to wortmanin, an inhibitor of phosphatidylinositol-3-kinase (PI3K). Selenium stimulates PI3K activity that is sustained up to 24 h. Selenium after 5-10 min increases tyrosine phosphorylation of selective cellular proteins, but after 24 h overall tyrosine phosphorylation is increased. Tyrosine phosphorylation of insulin receptor substrate 1 is detected when enriched by immunoprecipitation with anti-PI3K antibody. Selenium, however, does not stimulate insulin receptor tyrosine kinase activity. Selenium also increases phosphorylation of other insulin signaling proteins, including Akt and extracellular signal regulated kinases. Selenium-stimulated glucose transport is accompanied by increases in glucose transporter-1 content in the plasma membrane. These data are consistent with similar selenium action in glucose transport in 3T3-L1 fibroblasts expressing mainly GLUT1. In chronic insulin-induced insulin resistant cells, selenium unlike insulin fully stimulates glucose transport. In summary, selenium stimulates glucose transport and antilipolysis in a PI3K-dependent manner, but independent of insulin receptor activation. Selenium exerts both insulin-like and non-insulin-like actions in cells. |
| Databáze: | OpenAIRE |
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