Insulin and glucose modulate protein kinase C activity in rat adipocytes.
In the presence of 1 mM glucose, insulin (10 ng/ml) increases both catalytic and receptor-binding properties of adipocyte cytosolic protein kinase C (PKC). Preincubation of adipocytes with 10 mM glucose raises basal PKC catalytic activity and prevents further stimulation of this enzyme by insulin. The effect of hyperglycemia is likely to be mediated by direct conversion of glucose into diacylglycerol. Thus, an incorporation of 14C-glucose into diacylglycerol is enhanced 10-fold in the presence of 10 mM glucose. These observations indicate that, in normal adipocytes, both insulin and glucose activate PKC; hyperglycemia eliminates the ability of insulin to stimulate this enzyme, thereby interfering with insulin action.
D000273:Adipose Tissue / Q000187:drug effects / Q000201:enzymology*; D000818:Animals; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology; D005947:Glucose / Q000494:pharmacology*; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D012016:Reference Values
D007328:Insulin; D011493:Protein Kinase C; D005947:Glucose