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J. Biol. Chem., Vol. 269, Issue 42, 26100-26106, 10, 1994
M Nishimura, S Fedorov and K Uyeda
The effect of glucose on hepatic fructose (Fru) 2,6-P2 in starved rats was
investigated. When livers were perfused with high glucose (40 mM), hexose-P
in the liver increased immediately reaching the maximum within in 2 min,
but Fru 2,6-P2 after a lag period of 4 min increased linearly. The
activation of Fru 6-P,2-kinase and inactivation of Fru 2,6-Pase also showed
a similar lag period. Determination of the phosphate contents of the
bifunctional enzyme after 10 min of glucose perfusion revealed that 90% of
the enzyme was in the dephospho form while only 10% of the control liver
enzyme was dephosphorylated. Comparison of crude extracts of liver perfused
with either high glucose or normal glucose (5.6 mM) showed that high
glucose livers contained 50% higher protein phosphatase activity, which
dephosphorylated the bifunctional enzyme. Subcellular fractionation of the
extract showed that activation of the protein phosphatase occurred in the
cytosol. Desalting of the cytosolic fraction resulted in a 50% loss of the
protein phosphatase activity. The low molecular weight activator in the
cytosol was isolated, and by various chemical and enzymatic methods it was
identified as xylulose 5-P. The activation of protein phosphatase by
xylulose 5-P showed a highly sigmoidal saturation curve. The rate of
formation of xylulose 5-P in the perfused liver showed a lag period of
approximately 2 min, and after 4 min its concentration reached 10 microM,
the minimum concentration necessary for the activation of the protein
phosphatase. We conclude that the mechanism of glucose-induced Fru 2,6-P2
synthesis was not due to increased Fru 6-P as generally thought but
occurred as a result of dephosphorylation of Fru 6-P,2- kinase:Fru
2,6-Pase. Moreover, the dephosphorylation was enhanced by increased
xylulose 5-P, which activated a specific protein phosphatase. The results
suggest a mechanism for coordinated regulation of glycolysis and the
pentose shunt pathway that is mediated by xylulose 5- P.
Glucose-stimulated synthesis of fructose 2,6-bisphosphate in rat liver. Dephosphorylation of fructose 6-phosphate, 2-kinase:fructose 2,6- bisphosphatase and activation by a sugar phosphate
Department of Veterans Affairs Medical Center, Dallas, Texas 75216.
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