Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes
A Carabaza, CJ Ciudad, S Baqué, JJ Guinovart - FEBS letters, 1992 - Elsevier
A Carabaza, CJ Ciudad, S Baqué, JJ Guinovart
FEBS letters, 1992•ElsevierDeoxyglucose and 5-thioglucose, in the same fashion as glucose, cause the inactivation of
the rat hepatocyte glycogen phosphorylase and the activation of glycogen synthase.
However, 6-deoxyglucose and 1, 5-anhydroglucitol inactivate phosphorylase without
increasing the activation state of glycogen synthase. With 3-O-methylglucose no changes in
the activity or these enzymes occurred. These results prove that while glucose is the
molecule that triggers the inactivation of phosphorylase, glucose 6-phosphate is the signal …
the rat hepatocyte glycogen phosphorylase and the activation of glycogen synthase.
However, 6-deoxyglucose and 1, 5-anhydroglucitol inactivate phosphorylase without
increasing the activation state of glycogen synthase. With 3-O-methylglucose no changes in
the activity or these enzymes occurred. These results prove that while glucose is the
molecule that triggers the inactivation of phosphorylase, glucose 6-phosphate is the signal …
Abstract
2-Deoxyglucose and 5-thioglucose, in the same fashion as glucose, cause the inactivation of the rat hepatocyte glycogen phosphorylase and the activation of glycogen synthase. However, 6-deoxyglucose and 1,5-anhydroglucitol inactivate phosphorylase without increasing the activation state of glycogen synthase. With 3-O-methylglucose no changes in the activity or these enzymes occurred. These results prove that while glucose is the molecule that triggers the inactivation of phosphorylase, glucose 6-phosphate is the signal for glucose synthase activation and that a metabolite control of the activation state of glycogen synthase is operative in hepatocytes.
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