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J Biol Chem, Vol. 274, Issue 6, 3597-3601, February 5, 1999
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From INSERM, By using a rapid procedure of isolation of
microsomes, we have shown that the liver glucose-6-phosphatase activity
was lowered by about 30% (p < 0.001) after refeeding
for 360 min rats previously unfed for 48 h, whereas the amount of
glucose-6-phosphatase protein was not lowered during the same time. The
amount of the regulatory subunit (p85) and the catalytic activity of
phosphatidylinositol 3-kinase (PI3K) were higher by a factor of 2.6 and
2.4, respectively (p < 0.01), in microsomes from
refed as compared with fasted rats. This resulted from a translocation
process because the total amount of p85 was the same in the whole liver
homogenates from fasted and refed rats. The amount of insulin receptor
substrate 1 (IRS1) was also higher by a factor of 2.6 in microsomes
from refed rats (p < 0.01). Microsome-bound IRS1 was
only detected in p85 immunoprecipitates. These results strongly suggest
that an insulin-triggered mechanism of translocation of PI3K onto
microsomes occurs in the liver of rats during refeeding. This process,
via the lipid products of PI3K, which are potent inhibitors of
glucose-6-phosphatase (Mithieux, G., Danièle, N., Payrastre, B.,
and Zitoun, C. (1998) J. Biol. Chem. 273, 17-19), may
account for the inhibition of the enzyme and participate to the
inhibition of hepatic glucose production occurring in this situation.
Unit 449,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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