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Am J Physiol Endocrinol Metab 279: E947-E955, 2000;
0193-1849/00 $5.00
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Vol. 279, Issue 5, E947-E955, November 2000

Muscle glycogen content affects insulin-stimulated glucose transport and protein kinase B activity

W. Derave1, B. F. Hansen2, S. Lund3, S. Kristiansen1, and E. A. Richter1

1 Copenhagen Muscle Research Centre, Human Physiology, University of Copenhagen, 2100 Copenhagen; 2 Diabetes Biology, Novo Nordisk, 2880 Bagsværd; and 3 Medical Research Laboratory, Aarhus Kommunehospital, 8000 Aarhus C, Denmark

We investigated the possible regulatory role of glycogen in insulin-stimulated glucose transport and insulin signaling in skeletal muscle. Rats were preconditioned to obtain low (LG), normal, or high (HG) muscle glycogen content, and perfused isolated hindlimbs were exposed to 0, 100, or 10,000 µU/ml insulin. In the fast-twitch white gastrocnemius, insulin-stimulated glucose transport was significantly higher in LG compared with HG. This difference was less pronounced in the mixed-fiber red gastrocnemius and was absent in the slow-twitch soleus. In the white gastrocnemius, insulin activation of insulin receptor tyrosine kinase and phosphoinositide 3-kinase was unaffected by glycogen levels, whereas protein kinase B activity was significantly higher in LG compared with HG. In additional incubation experiments on fast-twitch epitrochlearis muscles, insulin-stimulated cell surface GLUT-4 content was significantly higher in LG compared with HG. The data indicate that, in fast-twitch muscle, the effect of insulin on glucose transport and cell surface GLUT-4 content is modulated by glycogen content, which does not involve initial but possibly more downstream signaling events.

GLUT-4; skeletal muscle; fiber type; phosphoinositide 3-kinase


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