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Vol. 273, Issue 1, 17-19, January 2, 1998
From the Institut National de la Santé et de la Recherche
Médicale, We have studied the effect of various
phospholipids on the activity of glucose-6-phosphatase (Glc6Pase) in
untreated and detergent-treated rat liver microsomes. Glc6Pase is
inhibited in the presence of phosphoinositides in a
dose-dependent manner within a range of concentration
0.5-10 µM. The order of efficiency in untreated microsomes is: phosphatidylinositol (PI) 3,4,5P3 > PI3,4P2 = PI4,5P2 > PI3P = PI4P > PI. In contrast, Glc6Pase is not inhibited in the presence of
phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine, diacylglycerol, and inositol 1,4,5-trisphosphate at concentrations up
to 100 µM. The mechanism of Glc6Pase inhibition by
PI4,5P2, PI3,4P2, and PI3,4,5P3 is
competitive in both untreated and detergent-treated microsomes. In
untreated microsomes, the Ki for
PI3,4,5P3 (1.7 ± 0.3 µM, mean ± S.D. n = 3) is significantly lower (p < 0.01) than that for PI3,4P2 (5.0 ± 0.8 µM) and for PI4,5P2 (4.7 ± 0.7 µM). In detergent-treated microsomes, Glc6Pase is less
sensitive to the inhibition and there is no difference anymore among
the Ki values for the three compounds: 8.3 ± 0.8, 11.1 ± 0.5 and 8.9 ± 0.4 µM for
PI3,4,5P3, PI3,4P2, and PI4,5P2,
respectively. This inhibition phenomenon might be of special importance
with regards to the insulin's inhibition of hepatic glucose
production.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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