Enhancement of phospholipase A2 activation by phosphatidic acid endogenously formed through phospholipase D action in rat peritoneal mast cell

FEBS Lett. 1993 May 24;323(1-2):23-6. doi: 10.1016/0014-5793(93)81440-b.


Contribution of phosphatidic acid (PA) generated by activated phospholipase (PL) D to PLA2 activation was studied in rat peritoneal mast cells. Exogenous didecanoyl PA induced arachidonate liberation in the permeabilized cells which was inhibited by p-bromophenacyl bromide. Upon exposure of the cells to ethanol in a high enough concentration to prevent PA formation, A23187-induced arachidonate liberation was suppressed by 50% and the rest was completely inhibited by p-bromophenacyl bromide. In contrast, propranolol, which enhanced PA accumulation, significantly increased the arachidonate liberation. These results suggest that A23187-induced PLA2 activation may be potentiated, at least in part, by PA generated through PLD action.

MeSH terms

  • Animals
  • Calcimycin / pharmacology
  • Enzyme Activation
  • Kinetics
  • Male
  • Mast Cells / enzymology*
  • Peritoneum / cytology
  • Peritoneum / enzymology
  • Phosphatidic Acids / metabolism
  • Phosphatidic Acids / physiology*
  • Phospholipase D / metabolism*
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Rats
  • Rats, Wistar


  • Phosphatidic Acids
  • Calcimycin
  • Phospholipases A
  • Phospholipases A2
  • Phospholipase D