α1-Adrenergic stimulation of Ca2+ mobilization without phosphorylase activation in hepatocytes from phosphorylase b kinase-deficient gsd/gsd rats
- 15 August 1981
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 198 (2), 379-383
- https://doi.org/10.1042/bj1980379
Abstract
Phenylephrine, vasopressin and the bivalent cation ionophore A23187 mobilized Ca2+ normally, but failed to activate phosphorylase, in hepatocytes from gsd/gsd rats with a deficiency of liver phosphorylase b kinase. These data provide strong evidence that phosphorylase b kinase is the site of action of the Ca2+ mobilized intracellularly during .alpha.1-adrenergic activation of phosphorylase in liver cells.This publication has 24 references indexed in Scilit:
- Evidence for mitochondrial localization of the hormone-responsive pool of Ca2+ in isolated hepatocytes.Journal of Biological Chemistry, 1979
- Studies on alpha-adrenergic activation of hepatic glucose output. The role of mitochondrial calcium release in alpha-adrenergic activation of phosphorylase in perfused rat liver.Journal of Biological Chemistry, 1979
- The role of calcium ion as a mediator of the effects of angiotensin II, catecholamines, and vasopressin on the phosphorylation and activity of enzymes in isolated hepatocytes.Journal of Biological Chemistry, 1979
- Evidence for two alpha-adrenergic binding sites in liver plasma membranes. Studies with [3H]epinephrine and [3H]dihydroergocryptine.Journal of Biological Chemistry, 1979
- The effect of solvents on nucleotide regulation of glycogen phosphorylase.Journal of Biological Chemistry, 1979
- The effects of glucagon, catecholamines, and the calcium ionophore A23187 on the phosphorylation of rat hepatocyte cytosolic proteins.Journal of Biological Chemistry, 1978
- Comparison of Calcium-Activated, Cyclic Nucleotide-Independent Protein and Adenosine 3′: 5′-Monophosphate-Dependent Protein as Regards the Ability to Stimulate Glycogen Breakdown In Vitro1The Journal of Biochemistry, 1978
- Studies on alpha-adrenergic activation of hepatic glucose output. Relationship between alpha-adrenergic stimulation of calcium efflux and activation of phosphorylase in isolated rat liver parenchymal cells.Journal of Biological Chemistry, 1978
- Studies on alpha-adrenergic activation of hepatic glucose output. Studies on role of calcium in alpha-adrenergic activation of phosphorylase.Journal of Biological Chemistry, 1977
- On the role of calcium as second messenger in liver for the hormonally induced activation of glycogen phosphorylaseBiochimica et Biophysica Acta (BBA) - General Subjects, 1977