Glucocerebroside inhibits NADPH oxidase activation in cell-free system

Biochim Biophys Acta. 2004 Apr 5;1688(3):197-203. doi: 10.1016/j.bbadis.2003.12.002.

Abstract

We reported earlier that monocytes and macrophages from patients with type I Gaucher disease have a decreased capacity to generate superoxide anion (O(2)(-)) on stimulation with opsonized S. aureus or formyl-methionyl-leucyl-phenylalanine. In this study, various forms of the cell-free assay system were used to probe the hypothesis that glucocerebroside (GC) accumulating in Gaucher patients' phagocytes may interfere with the activation of NADPH oxidase. Xanthine/xanthine oxidase assay was applied to explore the possibility that GC may scavenge O(2)(-). We found that addition of GC to the crude, semirecombinant or fully purified cell-free systems inhibited activation of NADPH oxidase in a concentration-dependent manner. The inhibitory effect of GC could be overcome by increased concentrations of p47(phox) and p67(phox). In contrast, O(2)(-) generation was not decreased by GC added to the assembled, catalytically active enzyme complex. In the xanthine/xanthine oxidase system, GC had no effect on the generation of O(2)(-). These data indicate that assembly of the respiratory burst oxidase of phagocytic cells may be a possible target of the pathologic actions of GC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell-Free System
  • Cloning, Molecular
  • Enzyme Activation / drug effects
  • Glucosylceramides / pharmacology*
  • Humans
  • Kinetics
  • NADPH Oxidases / antagonists & inhibitors
  • NADPH Oxidases / blood*
  • NADPH Oxidases / drug effects
  • Neutrophils / enzymology*
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / metabolism
  • Superoxides / blood
  • Xanthine Oxidase / blood

Substances

  • Glucosylceramides
  • Recombinant Proteins
  • Superoxides
  • Xanthine Oxidase
  • NADPH Oxidases