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J Biol Chem, Vol. 274, Issue 39, 27497-27504, September 24, 1999
,§
From the The role of increased glucose transport in the
hormonal regulation of glycogen synthase by insulin was investigated in
3T3-L1 adipocytes. Insulin treatment stimulated glycogen synthase
activity 4-5-fold in these cells. Cytosolic glycogen synthase levels
decreased by 75% in response to insulin, whereas, conversely, the
glycogenolytic agent isoproterenol increased cytosolic enzyme levels by
200%. Removal of extracellular glucose reduced glycogen synthase
activation by 40% and completely blocked enzymatic translocation.
Addition of 5 mM 2-deoxyglucose did not restore
glycogen synthase translocation but did augment dephosphorylation of
the protein by insulin. The translocation event could be reconstituted
in vitro only by the addition of UDP-glucose to basal cell
lysates. Amylase pretreatment of the extracts suppressed glycogen
synthase translocation, indicating that the enzyme was binding to
glycogen. Incubation of 3T3-L1 adipocytes with 10 mM
glucosamine induced a state of insulin resistance, blocked the
translocation of glycogen synthase, and inhibited insulin-stimulated
glycogen synthesis by 50%. Surprisingly, glycogen synthase activation
by insulin was enhanced 4-fold, in part due to allosteric activation by
a glucosamine metabolite. In vitro, glucosamine 6-phosphate
and glucose 6-phosphate stimulated glycogen synthase activity with
similar concentration curves. These results indicate that glucose
metabolites have an impact on the regulation of glycogen synthase
activation and localization by insulin.
Department of Cell Biology, Parke-Davis
Pharmaceutical Research Division, Ann Arbor, Michigan 48105 and the
§ Department of Physiology, University of Michigan School of
Medicine, Ann Arbor, Michigan 48109
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