期刊论文详细信息
FEBS Letters
Glucose has to be phosphorylated to activate glycogen synthase, but not to inactivate glycogen phosphorylase in hepatocytes
Carabaza, Assumpta1  Ciudad, Carlos J.3  Baqué, Susanna2  Guinovart, Joan J.2 
[1] Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain;Departament de Bioquímica i Fisiologia, Universitat de Barcelona, E-08028 Barcelona, Spain;Departament de Ciènces Fisiològiques, Humanes i de la Nutrició, Universitat de Barcelona, E-08028 Barcelona, Spain
关键词: Glycogen synthase;    Glycogen phosphorylase;    Glucose;    Glucose analog;   
DOI  :  10.1016/0014-5793(92)80381-P
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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.

【 授权许可】

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