Discovery - University of Dundee - Online Publications

Library & Learning Centre

Effect of acute exercise on glycogen synthase in muscle from obese and diabetic subjects

Effect of acute exercise on glycogen synthase in muscle from obese and diabetic subjects

Research output: Contribution to journalArticle

View graph of relations


  • Jorgen Jensen
  • Puntip Tantiwong
  • Jorid T. Stuenaes
  • Marjorie Molina-Carrion
  • Ralph A. DeFronzo
  • Kei Sakamoto
  • Nicolas Musi

Research units


Original languageEnglish
Pages (from-to)E82-E89
Number of pages8
JournalAmerican Journal of Physiology, Endocrinology and Metabolism
Issue number1
StatePublished - Jul 2012


Jensen J, Tantiwong P, Stuenaes JT, Molina-Carrion M, DeFronzo RA, Sakamoto K, Musi N. Effect of acute exercise on glycogen synthase in muscle from obese and diabetic subjects. Am J Physiol Endocrinol Metab 303: E82-E89, 2012. First published April 17, 2012; doi: 10.1152/ajpendo.00658.2011.-Insulin stimulates glycogen synthase (GS) through dephosphorylation of serine residues, and this effect is impaired in skeletal muscle from insulin-resistant [obese and type 2 diabetic (T2DM)] subjects. Exercise also increases GS activity, yet it is not known whether the ability of exercise to affect GS is impaired in insulin-resistant subjects. The objective of this study was to examine the effect of acute exercise on GS phosphorylation and enzyme kinetic properties in muscle from insulin-resistant individuals. Lean normal glucose-tolerant (NGT), obese NGT, and obese T2DM subjects performed 40 min of moderate-intensity cycle exercise (70% of Vo(2max)). GS kinetic properties and phosphorylation were measured in vastus lateralis muscle before exercise, immediately after exercise, and 3.5 h postexercise. In lean subjects, GS fractional activity increased twofold after 40 min of exercise, and it remained elevated after the 3.5-h rest period. Importantly, exercise also decreased GS K-m for UDP-glucose from approximate to 0.5 to approximate to 0.2 mM. In lean subjects, exercise caused significant dephosphorylation of GS by 50-70% (Ser(641), Ser(645), and Ser(645,649,653,657)), and phosphorylation of these sites remained decreased after 3.5 h; Ser(7) phosphorylation was not regulated by exercise. In obese NGT and T2DM subjects, exercise increased GS fractional activity, decreased K-m for UDP-glucose, and decreased GS phosphorylation as effectively as in lean NGT subjects. We conclude that the molecular regulatory process by which exercise promotes glycogen synthesis in muscle is preserved in insulin-resistant subjects.



Library & Learning Centre

Contact | Accessibility | Policy