Abstract
Adrenalectomy results in significant changes in the mechanism of adrenergic activation of hepatic glycogenolysis. In adrenalectomized rats a greater role for the beta-adrenergic receptor is observed, whereas the alpha 1-adrenergic-mediated phosphorylase activation declines. Our present findings document that adrenalectomy causes a significant decrease in the high-affinity population of the alpha 1-adrenergic receptor labelled with [3H]adrenaline. Our data indicate a large increase in the number of beta-adrenergic binding sites after adrenalectomy. This increase was not consistent with the observed modest increase in the beta-adrenergic-mediated activation of cyclic AMP accumulation and glycogen phosphorylase. When alpha-adrenergic antagonists are present along with the catecholamine, a 100% increase in the adrenaline-mediated accumulation of cyclic AMP in hepatocytes from adrenalectomized rats was observed. Adrenalectomy was also shown to cause a significant increase in the hepatic alpha 2-adrenergic binding sites. These data are consistent with an inhibitory role on the beta-adrenergic-mediated activation of glycogenolysis by the hepatic alpha 2-adrenergic receptor in adrenalectomy.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
10 articles.
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