Inverse relationship of skeletal muscle glycogen from wild-type and genetically modified mice to their phosphorylase a activity

Biochem Biophys Res Commun. 2002 Jan 18;290(2):874-7. doi: 10.1006/bbrc.2001.6292.

Abstract

Leg muscle was biopsied and frozen for storage at -70 degrees C. from 5 wild-type mice, two knocked out acid alpha-glucosidase (GAA) gene mice, and seven glycogen synthase plus glucose muscle transporter transgenic mice. All of the wild-type mice had very little muscle glycogen (3.58 +/- 1.67 micromols glucosyl subunits per g muscle), and 52% or more of its glycogen phosphorylase activity without AMP (69% +/- 17% glycogen phosphorylase a). In contrast the GAA knockout and transgenic mice had glycogen ranging from 63 to 297 micromols glucosyl subunits per g muscle, and very little or no glycogen phosphorylase activity without 1.00 mM AMP (4.8% and less glycogen phosphorylase a). This suggests that there is an inverse relationship between mouse muscle phosphorylase a and the muscle's glycogen content.

MeSH terms

  • Animals
  • Enzyme Activation / physiology
  • Fructose-Bisphosphate Aldolase / metabolism
  • Glucan 1,4-alpha-Glucosidase / deficiency
  • Glucan 1,4-alpha-Glucosidase / genetics
  • Glucan 1,4-alpha-Glucosidase / metabolism
  • Glucose Transporter Type 1
  • Glycogen / analysis
  • Glycogen / metabolism*
  • Glycogen Debranching Enzyme System / metabolism
  • Glycogen Synthase / genetics
  • Glycogen Synthase / metabolism
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Monosaccharide Transport Proteins / genetics
  • Monosaccharide Transport Proteins / metabolism
  • Muscle, Skeletal / chemistry
  • Muscle, Skeletal / metabolism*
  • Phosphofructokinases / metabolism
  • Phosphorylase a / metabolism*

Substances

  • Glucose Transporter Type 1
  • Glycogen Debranching Enzyme System
  • Monosaccharide Transport Proteins
  • Glycogen
  • Phosphorylase a
  • Glycogen Synthase
  • Phosphofructokinases
  • Glucan 1,4-alpha-Glucosidase
  • Fructose-Bisphosphate Aldolase