Activation of glycogen phosphorylase and glycogenolysis in rat skeletal muscle by AICAR--an activator of AMP-activated protein kinase

FEBS Lett. 1996 Mar 11;382(1-2):43-7. doi: 10.1016/0014-5793(96)00129-9.

Abstract

We determined whether the cell permeable molecule AICAR, whose metabolite activates AMP-activated protein kinase (AMPK) in cells, affected glycogen metabolism in rat soleus muscle preparations in vitro. The basal and insulin-stimulated rates of radiochemical lactate formation, net lactate release and glycogen synthesis were determined. AICAR stimulated net lactate release (but not radiochemical lactate formation) only at a basal concentration of insulin. An increased rate of glycogenolysis was the likely cause of increased net lactate release as glycogen phosphorylase activity was significantly increased by AICAR. AICAR-stimulated net lactate release and phosphorylase activity were potently inhibited by insulin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Adenosine Monophosphate / pharmacology
  • Aminoimidazole Carboxamide / analogs & derivatives*
  • Aminoimidazole Carboxamide / pharmacology
  • Animals
  • Enzyme Activation / drug effects
  • Glycogen / biosynthesis
  • Glycogen / metabolism*
  • Glycolysis
  • Insulin / pharmacology
  • Lactates / metabolism
  • Lactic Acid
  • Male
  • Multienzyme Complexes / metabolism*
  • Muscle, Skeletal / enzymology
  • Muscle, Skeletal / metabolism*
  • Phosphorylases / metabolism*
  • Protein Kinases / metabolism*
  • Protein-Serine-Threonine Kinases*
  • Rats
  • Rats, Wistar
  • Ribonucleotides / pharmacology*

Substances

  • Insulin
  • Lactates
  • Multienzyme Complexes
  • Ribonucleotides
  • Lactic Acid
  • Aminoimidazole Carboxamide
  • Adenosine Monophosphate
  • Glycogen
  • Phosphorylases
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • AICA ribonucleotide