Abstract
The administration of glucose to anesthetized fed rats causes within 1 to 2 minutes the inactivation of phosphorylase; glycogen synthetase is activated only when and if the level of phosphorylase α has been taken down below a threshold value equal to approximately 10% of the total phosphorylase. The same conclusion has been reached in a study with anesthetized fed mice. These observations are adequately explained by the previously described stimulation of the phosphorylase phosphatase reaction by glucose and inhibition of synthetase phosphatase by phosphorylase α. In some experiments, insulin caused a partial inactivation of liver phosphorylase in the liver of normal rats, but more often was without effect. When effective in the diabetic animal, insulin produced the inactivation of glycogen phosphorylase and the activation of glycogen synthetase. Glucocorticoids displayed two effects: a greater activity of phosphorylase phosphatase and a decreased inhibition of synthetase phosphatase by phosphorylase α.
The mechanism is discussed by which glucokinase and glucose 6-phosphatase adapt their rate of reaction to that of glycogen synthetase and of glycogen phosphorylase when glycogen synthesis or degradation is greatly stimulated.
This work was supported by the Fonds de la Recherche Scientifique Médicale and by NIH Grant AM 9235. W. Stalmans and H. De Wulf are fellows of the NFWO; L. Hue is a fellow of the FNRS.
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Hers, H.G., Stalmans, W., De Wulf, H., Laloux, M., Hue, L. (1974). The Control of Glycogen Metabolism in the Liver. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_9
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DOI: https://doi.org/10.1007/978-3-642-80817-3_9
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