Role of phospholipase D-derived phosphatidic acid as a substrate for phospholipase A2 in RBL-2H3 cells

K. Kitatani, S. Akiba, T. Sato

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

The implications of phospholipase D (PLD) in cytosolic phospholipase A2 (cPLA2) activation were studied in a mast cell line, RBL-2H3, upon stimulation with antigen. Antigen-stimulated prostaglandin D2 generation was apparently suppressed by ethanol with a concomitant decrease in phosphatidic acid (PA) formation. The prostaglandin D2 generation was also inhibited almost completely by methyl arachidonyl fluorophosphonate (MAFP), an inhibitor of cPLA2, but not by diacylglycerol lipase inhibitor. Furthermore, stimulation with antigen resulted in an increase in lysophosphatidic acid formation, which was suppressed by MAFP in parallel with an increase in PA formation. These results suggest that PA formed by the catalytic action of PLD is used as a substrate for cPLA2, thus PLD regulates cPLA2 activation in antigen-stimulated RBL-2H3 cells.

Original languageEnglish
Pages (from-to)1430-1433
Number of pages4
JournalBiological and Pharmaceutical Bulletin
Volume23
Issue number12
DOIs
Publication statusPublished - 2000

Keywords

  • Cytosolic phospholipase A
  • Mast cell line
  • Phosphatidic acid
  • Phospholipase D
  • Prostaglandin D

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

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