Lysophosphatidic acid increases intracellular H2O2 by phospholipase D and RhoA in Rat-2 fibroblasts

Incheol Shin, Soo Mi Kweon, Zee Won Lee, Seung Il Kim, Cheol O. Joe, Jae Hong Kim, Young Mok Park, Kwon Soo Ha

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


We have investigated the possible roles of phospholipase D (PLD) and RhoA in the production of intracellular H2O2 and actin polymerization in response to lysophosphatidic acid (LPA) in Rat-2 fibroblasts. LPA increased intracellular H2O2, with a maximal increase at 30 min, which was blocked by the catalase from Aspergillus niger. The LPA-stimulated production of H2O2 was inhibited by 1-butanol or PKC-downregulation, but not by 2-butanol. Purified phosphatidic acid (PA) also increased intracellular H2O2 and the increase was inhibited by the catalase. The role of RhoA was studied by the scrape-loading of C3 transferase into the cells. The C3 toxin, which inhibited stress fiber formation stimulated by LPA, blocked the H2O2 production in response to LPA or PA, but had no inhibitory effect on the activation of PLD by LPA. Exogenous H2O2 increased F-actin content by stress fiber formation. In addition, catalase inhibited actin polymerization activated by LPA, PA, or H2O2, indicated the role of H2O2 in actin polymerization. These results suggest that LPA increased intracellular H2O2 by the activation of PLD and RhoA, and that intracellular H2O2 was required for the LPA-stimulated stress fiber formation.

Original languageEnglish
Pages (from-to)292-299
Number of pages8
JournalMolecules and cells
Issue number3
Publication statusPublished - 1999 Jun 30
Externally publishedYes


  • HO
  • Lysophosphatidic Acid
  • Phospholipase D
  • RhoA
  • Stress Fibers

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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