Reactive oxygen species are involved in the activation of cellular phospholipase A2

FEBS Lett. 1992 Sep 7;309(2):190-2. doi: 10.1016/0014-5793(92)81092-z.

Abstract

Vanadate (V) potentiated (4- to 10-fold) the activation of cellular phospholipase A2 (PLA2) induced by H2O2 (H), a phorbol ester (T), a Ca(2+)-ionophore (A) and opsonized zymosan in macrophages. V+H induced in intact cells the activation and translocation of PLA2 and protein kinase C (PKC) to the plasma membrane. V+H and V+T+A induced strong chemiluminescence (CL) which was abrogated by a specific NADPH oxidase inhibitor diphenylene iodonium (DPI). DPI markedly suppressed the stimulation of PLA2 by V+T+A and V+OZ. The results suggest that the formation of endogenous reactive oxygen species (ROS) is important for PLA2 activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Enzyme Activation
  • Female
  • Hydrogen Peroxide / pharmacology
  • Macrophages / drug effects
  • Macrophages / metabolism
  • Mice
  • Mice, Inbred Strains
  • NADH, NADPH Oxidoreductases / antagonists & inhibitors
  • NADH, NADPH Oxidoreductases / metabolism
  • NADPH Oxidases
  • Onium Compounds / pharmacology
  • Oxygen / metabolism*
  • Phospholipases A / metabolism*
  • Phospholipases A2
  • Protein Kinase C / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Vanadates / pharmacology

Substances

  • Onium Compounds
  • Vanadates
  • diphenyleneiodonium
  • Hydrogen Peroxide
  • NADH, NADPH Oxidoreductases
  • NADPH Oxidases
  • Protein-Tyrosine Kinases
  • Protein Kinase C
  • Phospholipases A
  • Phospholipases A2
  • Oxygen