Inhibition of acetyl-CoA carboxylase activity in isolated rat adipocytes incubated with glucagon. Interactions with the effects of insulin, adrenaline and adenosine deaminase

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Abstract
Adipocytes isolated from epididymal fat-pads of fed rats were incubated with different concentarations of glucagon, insulin, adrenaline [epinephrine] and adenosine deaminase, and the effects of these agents on the initial activity of acetyl-CoA carboxylase in the cells were studied. Glucagon (at concentrations between 0.1 and 10 nM) inhibited acetyl-CoA carboxylase activity. Maximal inhibition was approximately 70% of the control activity in the absence of added hormone, and the concentration of hormone required for half-maximal inhibition was 0.3-0.5 nM glucagon. Incubation of cells with adenosine deaminase resulted in a similar inhibition of acetyl-CoA carboxylase activity. Preincubation of adipocytes with adenosine deaminase did not alter either the sensitivity of carboxylase activity to increasing concentrations of glucagon or the maximal extent of inhibition. Adrenaline inhibited acetyl-CoA carboxylase to the same extent as glucagon. Preincubation of the cells with glucagon did not alter the sensitivity of enzyme activity to adrenaline or the degree of maximal inhibition. Insulin activated the enzyme by 70-80% of control activity. Preincubation of the cells with glucagon did not alter the concentration of insulin required to produce half the maximal stimulatory effect (about 12 .mu.U of insulin/ml). The effects of insulin and glucagon appeared to be mediated completely independently and were approximately quantitatively similar but opposite. These characteristics resulted in the mutual cancellation of the effects of the 2 hormones when they were both present at equally effective concentrations. The implications of these findings with regard to current concepts about the mechanism of regulation of acetyl-CoA carboxylase and to the regulation of the enzyme in vivo are discussed.

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