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      Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation.

      The Journal of Biological Chemistry

      3T3 Cells, Adipose Tissue, enzymology, Animals, Cell Differentiation, Cell Membrane, Enzyme Activation, Fibroblasts, Glucose, metabolism, Glucose Transporter Type 1, Glucose Transporter Type 4, Glycogen, biosynthesis, Kinetics, Lipids, Mice, Monosaccharide Transport Proteins, Muscle Proteins, Myristic Acid, Myristic Acids, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, genetics, Proto-Oncogene Proteins c-akt

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          Akt is a serine/threonine kinase that requires a functional phosphatidylinositol 3-kinase to be stimulated by insulin and other growth factors. When directed to membranes by the addition of a src myristoylation sequence, Akt becomes constitutively active. In the present studies, the constitutively active Akt and a nonmyristoylated control mutant were expressed in 3T3-L1 cells that can be induced to differentiate into adipocytes. The constitutively active Akt induced glucose uptake into adipocytes in the absence of insulin by stimulating translocation of the insulin-responsive glucose transporter 4 to the plasma membrane. The constitutively active Akt also increased the synthesis of the ubiquitously expressed glucose transporter 1. The increased glucose influx in the 3T3-L1 adipocytes directed lipid but not glycogen synthesis. These results indicate that Akt can regulate glucose uptake and metabolism.

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