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Query: EC:6.4.1.2 (
acetyl-CoA carboxylase
)
2,876
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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.
...
PMID:Inactivation of hepatic acetyl-CoA carboxylase by catecholamine and its agonists through the alpha-adrenergic receptors. 611 54