Arachidonic acid increases activation of NADPH oxidase in monocytic U937 cells by accelerated translocation of p47-phox and co-stimulation of protein kinase C

Cell Signal. 1996 Aug;8(5):397-402. doi: 10.1016/0898-6568(96)00077-0.

Abstract

Arachidonic acid (AA) has been implicated as an important amphiphilic co-factor in the activation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase in neutrophils and reconstituted cell-free systems. To assess the role of AA in the activation of O2- generation in monocytic cells, we studied pre-monocytic U937 cells differentiated with 1,25-(OH)2-vitamin D3 plus interferon-gamma (IFN-gamma). AA dose-dependently enhanced phorbol myristate acetate (PMA)-stimulated O2- generation, with a maximum increase of 4,5-fold, through: (1) a more than 50% reduction of the lag-phase, defined as the time between addition of PMA and detection of O2-; and (2) a more than 60% increase in the constant rate of O2- generation. Reduction of the lag phase was associated with increased protein kinase C (PKC)-independent translocation of the cytosolic subunit of NADPH oxidase p47-phox to the cell membrane, whereas increased generation of O2- correlated with enhanced activation of PKC. The data indicate that AA increases activation of NADPH oxidase by accelerating its assembly and by co-stimulating PKC in monocytic U937 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonic Acid / pharmacology*
  • Humans
  • Monocytes / cytology
  • Monocytes / drug effects
  • Monocytes / enzymology*
  • NADPH Oxidases / metabolism*
  • Oxides
  • Phospholipases A / metabolism
  • Phosphoproteins / metabolism*
  • Protein Kinase C / metabolism*
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tumor Cells, Cultured

Substances

  • Oxides
  • Phosphoproteins
  • Arachidonic Acid
  • NADPH Oxidases
  • neutrophil cytosolic factor 1
  • Protein Kinase C
  • Phospholipases A
  • Tetradecanoylphorbol Acetate