α1-Adrenergic stimulation of Ca2+ mobilization without phosphorylase activation in hepatocytes from phosphorylase <i>b</i> kinase-deficient <i>gsd/gsd</i> rats
Biochemical JournalPublished 15 August 1981Open access
P F Blackmore, John H. Exton
Citations31
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TL;DR
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.
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.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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