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  • Title: Inactivation of hepatic acetyl-CoA carboxylase by catecholamine and its agonists through the alpha-adrenergic receptors.
    Author: Ly S, Kim KH.
    Journal: J Biol Chem; 1981 Nov 25; 256(22):11585-90. PubMed ID: 6117554.
    Abstract:
    The effects of adrenergic agonists on acetyl-CoA carboxylase and fatty acid synthesis were studied in isolated rat hepatocytes from mature rats (300 to 350 g). Norepinephrine and phenylephrine inactivate acetyl-CoA carboxylase activity and inhibit fatty acid synthesis. The effects of both norepinephrine and phenylephrine were blocked by the alpha-adrenergic receptor blockers, phentolamine and phenoxybenzamine, and unaffected by the beta-receptor blocker propranolol. This inactivation was not mimicked by the beta-agonist isoproterenol. The measurable increase in cyclic AMP levels caused by norepinephrine and phenylephrine was abolished by the alpha-antagonist phentolamine and diminished by the beta-antagonist propranolol. Calcium depletion potentiated the increase in cyclic AMP levels by phenylephrine but abolished the phenylephrine inactivation of the carboxylase. The inactivation of acetyl-CoA carboxylase by phenylephrine was correlated with an increase in the incorporation of [32P]phosphate into the enzyme. Thus, catecholamines and their agonists promote phosphorylation and inactivation of acetyl-CoA carboxylase through the alpha-adrenergic receptor, and the inactivation requires calcium.
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