Additive effect of contraction and insulin on glucose uptake and glycogen synthase in muscle with different glycogen contents

Research output: Contribution to journalArticlepeer-review

Authors

Colleges, School and Institutes

External organisations

  • National Institute of Occupational Health
  • University of Dundee

Abstract

Insulin and contraction regulate glucose uptake and glycogen synthase (GS) via distinct mechanisms in skeletal muscles, and an additive effect has been reported. Glycogen content is known to influence both contraction- and insulin-stimulated glucose uptake and GS activity. Our study reports that contraction and insulin additively stimulate glucose uptake in rat epitrochlearis muscles with normal (NG) and high (HG) glycogen contents, but the additive effect was only partial. In muscles with low glycogen (LG) content no additive effect was seen, but glucose uptake was higher in LG than in NG and HG during contraction, insulin stimulation, and when the two stimuli were combined. In LG, contraction-stimulated AMP-activated protein kinase (AMPK) activity and insulin-stimulated PKB phosphorylation were higher than in NG and HG, but phosphorylation of Akt substrate of 160 kDa was not elevated correspondingly. GLUT4 content was 50% increased in LG (rats fasted 24 h), which may explain the increased glucose uptake. Contraction and insulin also additively increased GS fractional activity in NG and HG but not in LG. GS fractional activity correlated most strongly with GS Ser641 phosphorylation (R -0.94, P < 0.001). GS fractional activity also correlated with GS Ser7,10 phosphorylation, but insulin did not reduce GS Ser7,10 phosphorylation. In conclusion, an additive effect of contraction and insulin on glucose uptake and GS activity occurs in muscles with normal and high glycogen content but not in muscles with low glycogen content. Furthermore, contraction, insulin, and glycogen content all regulate GS Ser641 phosphorylation and GS fractional activity in concert.

Details

Original languageEnglish
Pages (from-to)1106-1115
Number of pages10
JournalJournal of Applied Physiology
Volume108
Issue number5
Publication statusPublished - 1 May 2010

Keywords

  • Akt substrate of 160 kDa, AMP-activated protein kinase, Protein kinase B, TBC1D1

ASJC Scopus subject areas