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Am J Physiol Endocrinol Metab 282: E1214-E1221, 2002. First published February 5, 2002; doi:10.1152/ajpendo.00254.2001
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Vol. 282, Issue 6, E1214-E1221, June 2002

Glucose transport rate and glycogen synthase activity both limit skeletal muscle glycogen accumulation

Jonathan S. Fisher, Lorraine A. Nolte, Kentaro Kawanaka, Dong-Ho Han, Terry E. Jones, and John O. Holloszy

Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

We varied rates of glucose transport and glycogen synthase I (GS-I) activity (%GS-I) in isolated rat epitrochlearis muscle to examine the role of each process in determining the rate of glycogen accumulation. %GS-I was maintained at or above the fasting basal range during 3 h of incubation with 36 mM glucose and 60 µU/ml insulin. Lithium (2 mM LiCl) added to insulin increased glucose transport rate and muscle glycogen content compared with insulin alone. The glycogen synthase kinase-3beta inhibitor GF-109203x (GF; 10 µM) maintained %GS-I about twofold higher than insulin with or without lithium but did not increase glycogen accumulation. When %GS-I was lowered below the fasting range by prolonged incubation with 36 mM glucose and 2 mU/ml insulin, raising rates of glucose transport with bpV(phen) or of %GS-I with GF produced additive increases in glycogen concentration. Phosphorylase activity was unaffected by GF or bpV(phen). In muscles of fed animals, %GS-I was ~30% lower than in those of fasted rats, and insulin-stimulated glycogen accumulation did not occur unless %GS-I was raised with GF. We conclude that the rate of glucose transport is rate limiting for glycogen accumulation unless %GS-I is below the fasting range, in which case both glucose transport rate and GS activity can limit glycogen accumulation.

glycogen synthase kinase-3beta ; lithium; insulin; fasting state; fed state


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