INACTIVATION OF HEPATIC ACETYL-COA CARBOXYLASE BY CATECHOLAMINE AND ITS AGONISTS THROUGH THE ALPHA-ADRENERGIC RECEPTORS

被引：0

作者：

LY, S ^{[1
]}

KIM, KH ^{[1
]}

机构：

[1] PURDUE UNIV, DEPT BIOCHEM, W LAFAYETTE, IN 47907 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1981年 / 256卷 / 22期

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中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The effects of adrenergic agonists on acetyl-CoA carboxylase and fatty acid synthesis were studied in isolated rat hepatocytes from mature rats (300-350 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 cAMP levels caused by norepinephrine and phenylephrine was abolished by the .alpha.-antagonist phentolamine and diminished by the .beta.-antagonist propranolol. Ca depletion potentiated the increase in cAMP 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. Catecholamines and their agonists promote phosphorylation and inactivation of acetyl-CoA carboxylase through the .alpha.-adrenergic receptor, and the inactivation requires Ca.

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页码：1585 / 1590

页数：6

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