Opposite paracrine effects of 5-HT and dopamine on Na(+)-Pi cotransport in opossum kidney cells

The effect of insulin on protein kinase activity and plasma membrane translocation of the glucose transporter GLUT 4 has been studied in adipocytes permeabilized by Streptolysin-O. Insulin increased protein kinase activity, and this was completely inhibited by the PKC pseudosubstrate inhibitor peptide (PKC19-36). Insulin-mediated translocation of GLUT 4 was also inhibited by the PKC inhibitor peptide. Both these insulin effects were blocked by a PKCbeta neutralizing antibody. Our results are consistent with the hypothesis that insulin activates PKCbeta activity in adipocytes in situ, and that this PKC activation is a component of the system whereby insulin regulates translocation of GLUT 4 to the plasma membrane.