[HTML][HTML] The activation of glycogen synthase by insulin switches from kinase inhibition to phosphatase activation during adipogenesis in 3T3-L1 cells
MJ Brady, FJ Bourbonais, AR Saltiel - Journal of Biological Chemistry, 1998 - ASBMB
The effects of insulin and platelet-derived growth factor (PDGF) on glycogen synthase
activation were compared in 3T3-L1 fibroblasts and adipocytes. In the fibroblasts, PDGF
elicited a stronger phosphorylation of mitogen-activated protein kinase (MAPK) and AKT
than did insulin. Both agents caused a comparable stimulation of receptor
autophosphorylation, MAPK, and phosphatidylinositol 3-kinase (PI3-K) activation in the
adipocytes. However, adipogenesis resulted in the uncoupling of PI3-K activation by PDGF …
activation were compared in 3T3-L1 fibroblasts and adipocytes. In the fibroblasts, PDGF
elicited a stronger phosphorylation of mitogen-activated protein kinase (MAPK) and AKT
than did insulin. Both agents caused a comparable stimulation of receptor
autophosphorylation, MAPK, and phosphatidylinositol 3-kinase (PI3-K) activation in the
adipocytes. However, adipogenesis resulted in the uncoupling of PI3-K activation by PDGF …