Comparative effects of insulin and isoproterenol on lipoprotein lipase in rat adipose cells

The effects of insulin and isoproterenol on lipoprotein lipase mass and enzyme activity were investigated in rat adipocytes. Cells were pulse labeled for 1 h with [S-35]methionine to measure immunoprecipitable lipoprotein lipase. The results showed that 80% of the newly synthesized enzyme was membrane associated and 20% was secreted into the cell incubation medium. Enzyme activity was mainly associated with lipoprotein lipase secreted into the medium. A 10-min incubation with 10(-7) M insulin stimulated the secretion of lipoprotein lipase activity and the activity associated with adipocyte membranes. Conversely, 10(-6) M isoproterenol decreased the activity in all fractions. In addition, insulin increased lipoprotein lipase mass associated with cell membranes and decreased that in the incubation medium, whereas isoproterenol induced a decrease in both cell membranes and medium. Insulin and isoproterenol stimulated phosphorylation of lipoprotein lipase. These findings suggest that insulin stimulates the secretion of active lipoprotein lipase and a reuptake of inactive secreted enzyme, and isoproterenol decreases the activity by enzyme degradation. Moreover, because both agents stimulate phosphorylation of lipoprotein lipase, phosphorylation may play a role in the effect of insulin increasing enzyme activity, in secretion or reuptake, and in the effect of isoproterenol inducing degradation of lipoprotein lipase.