Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

Acetyl-CoA carboxylase activity was measured in digitonin-permeabilized rat hepatocytes by coupling the carboxylase reaction to the fatty acid synthase reaction. Using this assay the activity of acetyl-CoA carboxylase was covariant with the rate of fatty acid synthesis. Insulin and the tumor promotor phorbol myristate acetate were found to stimulate, and glucagon and noradrenaline to inhibit both cellular parameters. The stimulation of acetyl-CoA carboxylase by insulin developed slowly (15 to 30 min) whereas the phorbol myristate acetate effect developed faster (within 15 min). The inhibition of the enzyme caused by glucagon was already apparent within 1 min after hormone addition. Inhibition by noradrenaline, in the presence of propranolol, was also quite rapid and occurred within 2 min after addition of the agonist.
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PMID:Time course of hormonal effects on acetyl-CoA carboxylase as measured in digitonin-permeabilized rat hepatocytes. 257 37

The rate of fatty acid synthesis in interscapular brown adipose tissue of female cold-adapted rats, as measured by the incorporation of 3H from 3H2O into tissue lipid, was decreased by about 70% after injection of noradrenaline. There was a similar decrease in the activity of acetyl-CoA carboxylase. In contrast, the proportion of pyruvate dehydrogenase in its active non-phosphorylated form was greatly increased after injection of noradrenaline. This finding suggests that the oxidation of glucose may be important in noradrenaline-induced thermogenesis in rat brown adipose tissue.
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PMID:Evidence that noradrenaline increases pyruvate dehydrogenase activity and decreases acetyl-CoA carboxylase activity in rat interscapular brown adipose tissue in vivo. 286 61

Insulin stimulates lipogenesis by 100% for 5 h by a covalent modulation of acetyl-CoA carboxylase, and by 200% for 24 h by increasing malic enzyme and fatty acid synthase enzymic activities in brown-adipocyte primary cultures. At short times, noradrenaline and isoprenaline decrease lipogenesis. However, phenylephrine and glucagon have no effect. At long times, dexamethasone inhibits lipogenesis. This effect is precluded in the presence of insulin. Progesterone and tri-iodothyronine, alone or in the presence of insulin, produce a stimulation of the rates of lipogenesis.
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PMID:Hormonal regulation of rat foetal lipogenesis in brown-adipocyte primary cultures. 304 67

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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PMID:Inactivation of hepatic acetyl-CoA carboxylase by catecholamine and its agonists through the alpha-adrenergic receptors. 611 54