Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells.
- Author:
Bong Hyun AHN
1
;
Gyesik MIN
;
Yoe Sik BAE
;
Young Seuk BAE
;
Do Sik MIN
Author Information
1. Cardiovascular Branch National Heart, Lung and Blood Institute (NHLBI), NIH Bldg 10/CRC 5-3288, 10 Center Drive, Bethesda, MD 20892, USA.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
casin kinase II;
cell proliferation;
phospholipase D;
phosphorylation
- MeSH:
1-Butanol/pharmacology;
Astrocytoma/*enzymology/metabolism/pathology;
Blotting, Western;
Casein Kinase II/analysis/*pharmacology;
Cell Line, Tumor;
Cell Proliferation/drug effects;
Dose-Response Relationship, Drug;
Enzyme Activation;
Enzyme Inhibitors/pharmacology;
Glutathione Transferase/metabolism;
Humans;
Kinetics;
Phospholipase D/genetics/*metabolism;
Phosphorylation/drug effects;
Precipitin Tests;
Recombinant Fusion Proteins/metabolism;
Research Support, Non-U.S. Gov't;
Tetradecanoylphorbol Acetate/pharmacology
- From:Experimental & Molecular Medicine
2006;38(1):55-62
- CountryRepublic of Korea
- Language:English
-
Abstract:
Elevated expression of protein casein kinase II (CKII) stimulated basal phospholipase D (PLD) activity as well as PMA-induced PLD activation in human U87 astroglioma cells. Moreover, CKII-selective inhibitor, emodin and apigenin suppressed PMA-induced PLD activation in a dose-dependent manner as well as basal PLD activity, suggesting the involvement of CKII in the activation of both PLD1 and PLD2. CKII was associated with PLD1 and PLD2 in co-transfection experiments. Furthermore, CKII induced serine/threonine phosphorylation of PLD2 in vivo, and the multiple regions of PLD2 were phosphorylated by CKII in vitro kinase assay using glutathione S-transferase-PLD2 fusion protein fragments. Elevated expression of CKII or PLD increased cell proliferation but pretreatment of cells with 1-butanol suppressed CKII-induced cell proliferation. These results suggest that CKII is involved in proliferation of U87 cells at least in part, through stimulation of PLD activity.
