Proteolytic activation of protein kinase C by membrane-bound protease in rat liver plasma membrane.
Incubation of rat liver plasma membrane produced histone phosphorylating activity at 75 mM Mg2+ in the soluble fraction. The release of the kinase activity was inhibited by leupeptin and bovine pancreatic trypsin inhibitor, suggesting the involvement of membrane-bound protease. When partially purified protein kinase C from rat liver cytosol was treated with the trypsin-like protease purified from rat liver plasma membrane, histone phosphorylating kinase which was independent of Ca2+ and phospholipids, produced with a molecular weight of about 5 X 10(4). These results suggest that membrane-bound, trypsin-like protease activates protein kinase C in plasma membrane and the activated kinase is released from the membrane to the soluble fraction.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D004789:Enzyme Activation; D008099:Liver / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000502:physiology*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D011493:Protein Kinase C; D010447:Peptide Hydrolases