Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells

FEBS Lett. 1997 Sep 8;414(2):365-8. doi: 10.1016/s0014-5793(97)01051-x.

Abstract

We have set up a model system for familial amyotrophic lateral sclerosis (FALS) by transfecting human neuroblastoma cell line SH-SY5Y with plasmids directing constitutive expression of either wild-type human Cu,Zn superoxide dismutase (Cu,ZnSOD) or a mutant of this enzyme (G93A) associated with FALS. We have tested mitochondrial function and determined cytosolic Ca2+ concentration in control cells (untransfected) and in cells expressing either wild-type Cu,ZnSOD or G93A. We report that G93A induces a significant loss of mitochondrial membrane potential, an increased sensitivity toward valinomycin and a parallel increase in cytosolic Ca2+ concentration. The above phenomena are not related to total Cu,ZnSOD content and activity in the cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyotrophic Lateral Sclerosis / enzymology*
  • Calcium / metabolism*
  • Cloning, Molecular
  • Cytosol / metabolism
  • Humans
  • Intracellular Membranes / drug effects
  • Intracellular Membranes / physiology
  • Membrane Potentials / drug effects
  • Membrane Potentials / physiology
  • Mitochondria / physiology*
  • Neuroblastoma
  • Polymerase Chain Reaction
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / metabolism
  • Superoxide Dismutase / biosynthesis*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism
  • Transfection
  • Tumor Cells, Cultured
  • Valinomycin / pharmacology

Substances

  • Recombinant Proteins
  • Valinomycin
  • Superoxide Dismutase
  • Calcium

Grants and funding