Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phospholipase D
/
Phosphorylation
/
Astrocytoma
/
Recombinant Fusion Proteins
/
Precipitin Tests
/
Tetradecanoylphorbol Acetate
/
Kinetics
/
Blotting, Western
/
1-Butanol
/
Cell Line, Tumor
Limits:
Humans
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2006
Type:
Article
Similar
MEDLINE
...
LILACS
LIS