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Am J Physiol Endocrinol Metab (December 4, 2001). doi:10.1152/ajpendo.00098.2001
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Articles in PresS, published online ahead of print December 4, 2001
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00098.2001
Submitted on March 6, 2001
Accepted on November 19, 2001

ACTIVATION OF LIVER GLUCOSE-6 PHOSPHATASE IN RESPONSE TO INSULIN-INDUCED HYPOGLYCEMIA AND EPINEPHRINE INFUSION IN THE RAT

Isabelle Bady1, Carine Zitoun1, Ludovic Guignot1, and Gilles Mithieux1*

1 INSERM U.449, Faculte de Medecine Laennec, Lyon Cedex, France

* To whom correspondence should be addressed. E-mail: mithieux{at}laennec.univ-lyon1.fr.

This study has been conducted to test the hypothesis of the activation of glucose-6 phosphatase (Glc6Pase) in the situations where the liver is supposed to sustain high glucose supply, such as during the counterregulatory response to hypoglycemia. Hypoglycemia has been induced by insulin infusion in anesthetized rats. Despite hyperinsulinemia, endogenous glucose production (EGP), assessed by 3[3H]glucose tracer dilution, was paradoxically not suppressed in hypoglycemic rats. Glc6Pase activity, assayed in a freeze-clamped liver lobe, was increased by 30% in hypoglycemia (p<0.01 vs saline infused controls). The infusion of epinephrine (1 µg/kg/min) in normal rats induced a dramatic 80% increase in EGP and 60% increase in Glc6Pase activity. In contrast, the infusion of dexamethasone had no effect on these parameters. Similar insulin-induced hypoglycemia experiments performed in adrenalectomized rats did not induce any stimulation of Glc6Pase. The infusion of epinephrine in adrenalectomized rats restored a stimulation of Glc6Pase similar to that triggered by hypoglycemia in normal rats. These results strongly suggest that specific activatory mechanisms of Glc6Pase take place and contribute EGP in the situations where the latter is supposed to be sustained.




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