Inhibition of glycogen synthase kinase-3 by insulin in cultured human skeletal muscle myoblasts

Biochem Biophys Res Commun. 1995 May 25;210(3):738-45. doi: 10.1006/bbrc.1995.1721.

Abstract

The acute effects of insulin on the activity of glycogen synthase kinase 3 (GSK-3) have been investigated both in the rat L6 muscle cell line and in cultured human myoblasts. The alpha and beta isoforms of GSK-3 are present in both cell types, with the beta isoform being predominant in the human cells. Insulin causes a rapid inactivation of both isoforms in both cell lines, with 50% inactivation being observed in the human myoblasts.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors*
  • Calcium-Calmodulin-Dependent Protein Kinases / isolation & purification
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Cells, Cultured
  • Chromatography, Gel
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Glycogen Synthase Kinase 3
  • Glycogen Synthase Kinases
  • Humans
  • Immunoblotting
  • Insulin / pharmacology*
  • Isoenzymes / antagonists & inhibitors*
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Kinetics
  • Molecular Sequence Data
  • Muscle, Skeletal / enzymology*
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Phosphorylation
  • Rats
  • Substrate Specificity

Substances

  • Insulin
  • Isoenzymes
  • Peptides
  • Glycogen Synthase Kinases
  • Cyclic AMP-Dependent Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Glycogen Synthase Kinase 3