Rat liver plasma membranes contain a lipid-dependent protein kinase activity.
The treatment of rat liver plasma membranes with EDTA resulted in substantial release of a protein kinase activity. Using histones as external substrates both phosphatidylserine (PS) and diolein activated the enzyme. The activatory effect of PS but not that of diolein depended on Ca2+. In contrast, the enzyme activity was inhibited by both PS and diolein when the substrate was protamine. The inhibition by PS, unlike by diolein, depended on Ca2+. Data suggest that mobilization of plasma membrane-bound Ca2+ by physiological stimuli may be accompanied by release of the lipid-dependent protein kinase into the cytoplasm.
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology*; D003593:Cytoplasm / Q000378:metabolism; D004075:Diglycerides / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D010718:Phosphatidylserines / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D004075:Diglycerides; D010718:Phosphatidylserines; D004492:Edetic Acid; D011494:Protein Kinases; D002118:Calcium; C013965:diolein