A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

FEBS Letters

Volumn 223, Issue 2, 1987, Pages 217-222

  Carling, David ^a   Zammit, Victor A ^a,b   Hardie, D Grahame ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b HANNAH RESEARCH INSTITUTE   (United Kingdom)

Author keywords

Acetyl CoA carboxylase; Cholesterol synthesis; Fatty acid synthesis; Fatty acyl CoA ester; Hydroxymethylglutaryl CoA reductase; Protein kinase

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ADENOSINE PHOSPHATE; CHOLESTEROL; FATTY ACID; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LIGASE; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE;

ANIMAL; ARTICLE; BIOSYNTHESIS; ENZYMOLOGY; LIVER; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; RAT;

ACETYL-COA CARBOXYLASE; ADENOSINE MONOPHOSPHATE; ANIMAL; CHOLESTEROL; FATTY ACIDS; HYDROXYMETHYLGLUTARYL COA REDUCTASES; LIGASES; LIVER; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN KINASES; RATS; SUPPORT, NON-U.S. GOV'T;

EID: 0023642627     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(87)80292-2     Document Type: Article

References (25)

1. The in vivo regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. Phosphorylation of the enzyme as an early regulatory response following cholesterol feeding.