Hydrogen peroxide-induced phospholipase D2 activation in lymphocytic leukemic L1210 cells

B. D. Lee, J. H. Kim, S. D. Lee, Y. Kim, P. G. Suh, S. H. Ryu

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Extracellular hydrogen peroxide (H2O2) has been implicated in the activation of phospholipase D (PLD). However, it was still unclear how this activation occurs and what the molecular identity of the H2O2-stimulated PLD isozyme is. This study shows that H2O2 potently increases the PLD activity in mouse lymphocytic leukemic L1210 cells, which contain exclusively PLD2. In addition, H2O2 increased PLD activity only in PLD2-transfected COS-7 cells and not in PLD1-transfected cells. This suggests that PLD2 is selectively activated by H2O2. Depletion of extracellular Ca2+ with EGTA completely blocked the H2O2-induced PLD activation, indicating that Ca2+ influx is required. Moreover, pretreatment of the cells with the protein kinase C (PKC) inhibitors GF-109203X and RO-31-8220 and down-regulation of PKCα by prolonged treatment with 4β-phorbol 12-myristate 13-acetate inhibited the H2O2-stimulated PLD2 activity, which points to the involvement of PKCα. Based on these new findings we suggest that PLD2 activity is specifically up-regulated by H2O2 and that the H2O2-induced PLD2 activation is mediated by Ca2+ influx and PKCα activation.

Original languageEnglish (US)
Pages (from-to)630-636
Number of pages7
JournalJournal of Leukocyte Biology
Issue number5
StatePublished - 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology
  • Cell Biology


  • Calcium
  • Protein kinase C


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