Methadone inhibition of glycogen synthase and phosphorylase in rat skeletal muscle |
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Authors: | D R Gourley J D Schwarzmeier |
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Affiliation: | Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22903, USA |
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Abstract: | The activities of glycogen synthase (I and total) and phosphorylase ( and total) in crude extracts of isolated extensor digitorum longus and soleus muscles of the rat incubated in the absence or presence of methadone were very low. Addition of glycogen during homogenization increased the activities of both enzymes in control muscles. Even at optimal concentrations of glycogen, however, the activities of both enzymes from methadone-treated muscles were significantly lower than their activities in control muscles. The activity of phosphoglucomutase was not altered by incubation with methadone or by homogenization with glycogen. It is suggested that the addition of optimal amounts of glycogen during extraction of the enzymes enhances the extractability of glycogen synthase and increases the activity of phosphorylase by some other mechanism and that these processes are interfered with when the muscles are pretreated with methadone. |
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