The hormonal control of glycogen metabolism. Phosphorylation of protein phosphatase inhibitor-1 in vivo in response to adrenaline

Eur J Biochem. 1979 Jun;97(1):251-6. doi: 10.1111/j.1432-1033.1979.tb13109.x.

Abstract

Inhibitor-1 has been shown to be phosphorylated in skeletal muscle in vivo. In normal fed animals the degree of phosphorylation was 31 +/- 7% and this value increases to 70 +/- 12% following an intravenous injection of adrenaline. The results imply that the phosphorylation of inhibitor-1 may be equally as important as the phosphorylation of phosphorylase kinase in elevating the levels of phosphorylase a. The role of inhibitor-1 in metabolism is discussed.

MeSH terms

  • Animals
  • Epinephrine / pharmacology*
  • Glycogen / metabolism*
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / physiology*
  • Muscles / drug effects
  • Muscles / enzymology*
  • Phosphoprotein Phosphatases / metabolism*
  • Phosphorylase Kinase / metabolism
  • Phosphorylase a / metabolism
  • Phosphorylase b / metabolism
  • Phosphorylation
  • Rabbits

Substances

  • Intracellular Signaling Peptides and Proteins
  • Muscle Proteins
  • protein phosphatase inhibitor-1
  • Glycogen
  • Phosphorylase a
  • Phosphorylase b
  • Phosphorylase Kinase
  • Phosphoprotein Phosphatases
  • Epinephrine