Journal of Biological Chemistry · 1990 · 207 citations · 34 references
Life SciencesBiochemistryMolecular BiologyCell SignalingMetabolic RegulationMetabolismDiabetes MellitusInsulin Signaling In MetabolismReceptor Tyrosine Kinase SignalingSelenium MetabolismSelenium NutritionTrace Element MetabolismAdipocyte Insulin SignalingGlucose TransportGlucose Transport RegulationInsulin ActionInsulin Receptor SignalingInsulin Signaling PathwayPhosphorylation EffectsSelenium Biochemistry
Selenate was found to have several insulin-like effects in rat adipocytes: stimulation of glucose transport activity by translocation of two types of glucose transporters from intracellular sites to the plasma membrane, stimulation of cAMP phosphodiesterase activity, and stimulation of ribosomal S6 protein phosphorylation. Furthermore, in intact cells addition of 1 mM selenate stimulated tyrosyl phosphorylation of 210-, 170-, 120-, 95-, 70-, and 60-kDa proteins but failed to stimulate insulin receptor kinase activity, suggesting that selenate stimulated other tyrosine kinase. In the presence of insulin, selenate enhances insulin receptor kinase activity and phosphorylations of insulin-stimulated tyrosyl phosphoproteins. These results may provide clues for the elucidation of the role of selenium in animals and the mechanism of insulin action.
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