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Experimental & Molecular Medicine ; : 55-62, 2006.
Article in English | WPRIM | ID: wpr-77901

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.


Subject(s)
Humans , 1-Butanol/pharmacology , Astrocytoma/enzymology , Blotting, Western , Casein Kinase II/analysis , Cell Line, Tumor , Cell Proliferation/drug effects , Dose-Response Relationship, Drug , Enzyme Activation , Enzyme Inhibitors/pharmacology , Glutathione Transferase/metabolism , Kinetics , Phospholipase D/genetics , Phosphorylation/drug effects , Precipitin Tests , Recombinant Fusion Proteins/metabolism , Tetradecanoylphorbol Acetate/pharmacology
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