Rapid activation of glycogen phosphorylase by steroid hormones in cultured rat hepatocytes.

Testosterone (40-300 microM), oestradiol (20-500 microM), progesterone (20-500 microM), dexamethasone (10 nM-1 microM) and corticosterone (1-10 microM) activate glycogen phosphorylase rapidly when added directly to hepatocytes. The activation of phosphorylase was concentration-dependent and occurred after 10 min for dexamethasone, 30 min for testosterone and 60 min for oestradiol and progesterone. This rapid effect does not appear to be dependent on a stimulation of protein synthesis, it is independent of an increase in cyclic AMP, and it is not diminished by the presence of ornithine decarboxylase inhibitors. The stimulation of phosphorylase activity is diminished by depleting the incubation medium of Ca2+ in the presence of 0.5 mM-EGTA, and therefore it may involve changes in the distribution of Ca2+ in the hepatocytes. These results may explain some of the pharmacological effects of sex steroids, and also might contribute to the physiological actions of glucocorticoids.