Distinct type-2A protein phosphatases activate HMGCoA reductase and acetyl-CoA carboxylase in liver

FEBS Lett. 1997 Aug 11;413(1):115-8. doi: 10.1016/s0014-5793(97)00890-9.

Abstract

Acetyl-CoA carboxylase and HMGCoA reductase are inactivated by the same AMP-activated protein kinase and are activated by type-2A protein phosphatase. To determine whether the same species of protein phosphatase-2A were involved, we studied the interconversion of acetyl-CoA carboxylase and HMGCoA reductase in isolated rat hepatocytes. We show that (i) these enzymes are differently regulated in hepatocytes and (ii) the species of type-2A protein phosphatase involved in their activation are different and can be separated by anion-exchange chromatography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Acetyl-CoA Carboxylase / metabolism*
  • Animals
  • Cell Hypoxia
  • Chromatography
  • Enzyme Activation
  • Glutamine / pharmacology*
  • Hydroxymethylglutaryl CoA Reductases / metabolism*
  • Liver / drug effects
  • Liver / enzymology*
  • Male
  • Multienzyme Complexes / metabolism
  • Phosphoprotein Phosphatases / metabolism*
  • Protein Kinases / metabolism
  • Protein Phosphatase 2
  • Protein Serine-Threonine Kinases*
  • Rats
  • Rats, Wistar
  • Time Factors

Substances

  • Multienzyme Complexes
  • Glutamine
  • Hydroxymethylglutaryl CoA Reductases
  • Protein Kinases
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 2
  • Acetyl-CoA Carboxylase