The low activity of acetyl‐CoA car☐ylase in basal and glucagon‐stimulated hepatocytes is due to phosphorylation by the AMP‐activated protein kinase and not cyclic AMP‐dependent protein kinase

FEBS Letters

Hardie, D.G.¹  Sim, Alastair T.R.¹ 

[1] MRC Protein Phosphorylation Group, Department of Biochemistry, The University, Dundee DD1 4HN, Scotland

关键词: Acetyl-CoA car☐ylase;    Hepatocyte;    Glucagon;    AMP-activated protein kinase;    cyclic AMP-dependent protein kinase;    (Rat);    HMG-CoA;    3-hydroxy-3-methylglutaryl coenzyme A;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(88)80445-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Acetyl-CoA car☐ylase purified from isolated hepatocytes is activated dramatically by protein phosphatase treatment, concomitant with a reduction of the phosphate content from 3.7 to 1.1 mol/subunit. Glucagon treatment of the cells produces a further inactivation of the enzyme that is totally reversed by phosphatase treatment, and is associated with an increase in phosphate content of 0.8 mol/subunit, distributed in two peptides which contain the sites phosphorylated in vitro by the cyclic AMP-dependent and AMP-activated protein kinases. Sequencing of these peptides shows that the low activity of acetyl-CoA car☐ylase is due to phosphorylation by the AMP-activated protein kinase, and not cyclic AMP-dependent protein kinase, even after glucagon treatment.

【 授权许可】

Unknown