The Cu,Zn superoxide dismutase in neuroblastoma SK-N-BE cells is exported by a microvesicles dependent pathway

Brain Res Mol Brain Res. 2003 Jan 31;110(1):45-51. doi: 10.1016/s0169-328x(02)00583-1.

Abstract

The antioxidant enzyme Cu,Zn superoxide dismutase has so far been considered costitutively expressed and exclusively localized into cytosol. In this paper we investigated Cu,Zn superoxide dismutase export in neuroblastoma SK-N-BE cells by flow cytometry analysis, confocal immunofluorescence analysis and enzyme-linked immunosorbed assay. Immunofluorescence analysis shows that the enzyme is exported by microvesicular granules; moreover the treatment of cells with brefeldin A and with 2-deoxy-D-glucose and sodium azide strongly decreases the amount of CuZn superoxide dismutase detected in the medium. Therefore the involvement of ATP-dependent mechanisms, likely including BFA-sensitive intracytoplasmic vesicles in Cu,Zn SOD export from SK-N-BE cells, has to be hypothesized. Microvesicular-mediated Cu,Zn SOD export in neurons could represent a relevant phenomenon able to influence cell excitability that is affected by reactive oxygen species.

MeSH terms

  • Blotting, Western
  • Brefeldin A / pharmacology
  • Cytoplasmic Vesicles / physiology*
  • Cytoskeleton / metabolism
  • Deoxyglucose / pharmacology
  • Enzyme Inhibitors / pharmacology
  • Flow Cytometry
  • Humans
  • Methylamines / pharmacology
  • Neuroblastoma*
  • Protein Synthesis Inhibitors / pharmacology
  • Protein Transport / drug effects
  • Protein Transport / physiology*
  • Sodium Azide / pharmacology
  • Superoxide Dismutase / metabolism*
  • Tumor Cells, Cultured

Substances

  • Enzyme Inhibitors
  • Methylamines
  • Protein Synthesis Inhibitors
  • Brefeldin A
  • Sodium Azide
  • Deoxyglucose
  • methylamine
  • Superoxide Dismutase