Exp Mol Med.
2006 Feb;38(1):55-62.
Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells
- Affiliations
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- 1Cardiovascular Branch National Heart, Lung and Blood Institute (NHLBI), NIH Bldg 10/CRC 5-3288, 10 Center Drive, Bethesda, MD 20892, USA.
- 2Department of Microbiological Engineering, Jinju National University, Chilam-dong 150, Jinju 660-758, Korea.
- 3Medical Research Center for Cancer, Molecular Therapy and Department of Biochemistry, College of Medicine, Dong-A University, Busan 602-714, Korea.
- 4Department of Biochemistry, College of Natural Sciences, Kyungpook National University, Daegu 702-701, Korea.
- 5Department of Molecular Biology, College of Natural Science, Pusan National University, Busan 609-735, Korea. minds@pusan.ac.kr
Abstract
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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.