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Am J Physiol Endocrinol Metab 281: E375-E383, 2001;
0193-1849/01 $5.00
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Vol. 281, Issue 2, E375-E383, August 2001

Lack of hepatic "interregulation" during inhibition of glycogenolysis in a canine model

K. Fosgerau1, S. D. Mittelman2, A. Sunehag3, M. K. Dea2, K. Lundgren1, and R. N. Bergman2

1 Department of Diabetes Biochemistry and Metabolism, Novo Nordisk, DK-2760 Maaloev, Denmark; 2 Department of Physiology and Biophysics, University of Southern California, Los Angeles, California 90033; and 3 Children's Nutrition Research Center, Houston, Texas 77030

It has been proposed that the glycogenolytic and gluconeogenic pathways contributing to endogenous glucose production are interrelated. Thus a change in one source of glucose 6-phosphate might be compensated for by an inverse change in the other pathway. We therefore investigated the effects of 1,4-dideoxy-1,4-imino-D-arabinitol (DAB), a potent glycogen phosphorylase inhibitor, on glucose production in fasted conscious dogs. When dogs were treated acutely with high glucagon, glucose production rose from 1.93 ± 0.14 to 3.07 ± 0.37 mg · kg-1 · min-1 (P < 0.01). When dogs were treated acutely with DAB in addition to high glucagon infusion, the stimulation of the glycogenolytic rate was completely suppressed. Glucose production rose from 1.85 ± 0.20 to 2.41 ± 0.17 mg · kg-1 · min-1 (P < 0.05), which was due to the increase in gluconeogenesis from 0.93 ± 0.09 to 1.54 ± 0.08 mg · kg-1 · min-1 (P < 0.001). In conclusion, infusion of DAB inhibited glycogenolysis; however, the absolute contribution of gluconeogenesis to glucose production was not affected. These results suggest that inhibition of glycogenolysis could be an effective antidiabetic treatment.

type 2 diabetes; glycogen phosphorylase; 1,4-dideoxy-1,4-imino-D-arabinitol


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