GLUCOSE HAS TO BE PHOSPHORYLATED TO ACTIVATE GLYCOGEN-SYNTHASE, BUT NOT TO INACTIVATE GLYCOGEN-PHOSPHORYLASE IN HEPATOCYTES

GLUCOSE HAS TO BE PHOSPHORYLATED TO ACTIVATE GLYCOGEN-SYNTHASE, BUT NOT TO INACTIVATE GLYCOGEN-PHOSPHORYLASE IN HEPATOCYTES
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DOI:
10.1016/0014-5793(92)80381-p
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发表时间:
1992-01-20
期刊:
影响因子:
3.5
通讯作者:
GUINOVART, JJ
GUINOVART, JJ
中科院分区:
生物学3区
文献类型:
--
作者:
CARABAZA, A;CIUDAD, CJ;GUINOVART, JJ

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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 of 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.