Effect of membrane perturbation on protein kinase C activation: treatment with exogenous phospholipase C decreases translocation of enzyme to cellular membranes.
Incubation of mouse epidermal HEL-37 cells with C. perfringens phospholipase C for 30 min caused a partial loss of protein kinase C activity after 30 min incubation. Essentially all the kinase activity was present in the cytosolic fraction of both control and treated cells, despite the continued hydrolysis of phospholipid by the exogenous phospholipase. At shorter incubation times with phospholipase C (5 and 10 min) an association of protein kinase with particulate material was observed, presumably reflecting the accumulation of diacylglycerol. It is proposed that further incubation with phospholipase C renders the plasma membrane unable to bind protein kinase C and that already bound enzyme is destroyed by proteolysis.
Jones
M J
MJ
Murray
A W
AW
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology*; D003016:Clostridium perfringens / Q000201:enzymology; D004075:Diglycerides / Q000378:metabolism; D004789:Enzyme Activation; D051379:Mice; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D013997:Time Factors; D010738:Type C Phospholipases / Q000378:metabolism*
C011439:1,2-diacylglycerol; D004075:Diglycerides; D010703:Phorbol Esters; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C; D010738:Type C Phospholipases; D013755:Tetradecanoylphorbol Acetate