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Vol. 273, Issue 1, 228-234, January 2, 1998
From the Diabetes Research and Training Center, Albert Einstein
College of Medicine, Bronx, New York 10461 and the § Center
for Human Genetics, University of Pennsylvania School of Medicine,
Philadelphia, Pennsylvania 19104
Hepatic gene expression of P-enolpyruvate
carboxykinase (PEPCK) and glucose-6-phosphatase (Glc-6-Pase) is
regulated in response to changes in the availability of substrates, in
particular glucose (Glc; Massillon, D., Barzilai, N., Chen, W., Hu, M.,
and Rossetti, L. (1996) J. Biol. Chem. 271, 9871-9874). We investigated the mechanism(s) in conscious rats.
Hyperglycemia per se caused a rapid and marked increase in
Glc-6-Pase mRNA abundance and protein levels. By contrast,
hyperglycemia decreased the abundance of PEPCK mRNA. Importantly,
inhibition of glucokinase activity by glucosamine infusion blunted both
the stimulation of Glc-6-Pase and the inhibition of PEPCK gene
expression by Glc, suggesting that an intrahepatic signal (metabolite)
generated by the metabolism of glucose at or beyond Glc-6-P was
responsible for the regulatory effect of Glc.
The effect of Glc on the L-type pyruvate kinase gene is
mediated by xylulose-5-P (Doiron, B., Cuif, M., Chen, R., and Kahn, A. (1996) J. Biol. Chem. 271, 5321-5324). Thus, we next
investigated whether an isolated increase in the hepatic concentration
of this metabolite can also reproduce the effects of Glc on Glc-6-Pase and PEPCK gene expression in vivo. Xylitol, which is
directly converted to xylulose-5-P in the liver, was infused to raise
the hepatic concentration of xylulose-5-P by ~3-fold. Xylitol
infusion did not alter the levels of Glc-6-P and of
fructose-2,6-biphosphate. However, it replicated the effects of
hyperglycemia on Glc-6-Pase and PEPCK gene expression and resulted in a
75% increase in the in vivo flux through Glc-6-Pase (total
glucose output).
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