Hormonal regulation of phosphorylase phosphatase activity in rat liver.
The effect of glucagon and insulin on rat liver phosphorylase phosphatase activity in vivo was investigated. The activity of phosphatase was found to decrease following the administration of glucagon and increase with insulin in a reversible manner. No change was detected in the activity of heat-stable phosphatase inhibitors in the hormone-treated samples. Liver protein kinases (regulatory subunit of cAMP-dependent protein kinase and/or Ca2+-dependent phosphorylase kinase) are suggested to regulate the activity of hepatic phosphorylase phosphatase (type 1 and 2A).
D000818:Animals; D002850:Chromatography, Gel; D005260:Female; D005934:Glucagon / Q000502:physiology*; D007328:Insulin / Q000502:physiology*; D008099:Liver / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000032:analysis*; D010764:Phosphorylase Kinase / Q000032:analysis; D010765:Phosphorylase Phosphatase / Q000032:analysis*; D011494:Protein Kinases / Q000502:physiology; D051381:Rats; D011919:Rats, Inbred Strains
D007328:Insulin; D005934:Glucagon; D011494:Protein Kinases; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases; D010765:Phosphorylase Phosphatase