Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Bong Hyun Ahn, Gyesik Min, Yoe Sik Bae, Young Seuk Bae, Sik Min Do

Research output: Contribution to journalArticle

20 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)55-62
Number of pages8
JournalExperimental and Molecular Medicine
Volume38
Issue number1
DOIs
Publication statusPublished - 2006 Feb 28

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry

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