Oxidized SOD1 alters proteasome activities in vitro and in the cortex of SOD1 overexpressing mice

FEBS Lett. 2005 Jul 4;579(17):3613-8. doi: 10.1016/j.febslet.2005.05.048.

Abstract

Premature ageing, one of the characteristics of Down syndrome (DS), may involve oxidative stress and impairment of proteasome activity. Transgenic mice overexpressing the human copper/zinc superoxide dismutase (SOD1) gene are one of the first murine models for DS and it has been shown that SOD1 overexpression might be either deleterious or beneficial. Here, we show a reduction in proteasome activities in the cortex of SOD1 transgenic mice and an associated increase in the content of oxidized SOD1 protein. As we demonstrate that in vitro oxidized SOD can inhibit purified proteasome peptidase activities, modified SOD1 might be partially responsible for proteasome inhibition shown in SOD1 transgenic mice.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cerebral Cortex / enzymology*
  • Down Syndrome / enzymology*
  • Down Syndrome / genetics
  • Humans
  • Mice
  • Mice, Transgenic
  • Oxidation-Reduction
  • Proteasome Endopeptidase Complex / analysis
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors*
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism*
  • Superoxide Dismutase-1
  • Transcriptional Activation

Substances

  • Proteasome Inhibitors
  • SOD1 protein, human
  • Sod1 protein, mouse
  • Superoxide Dismutase
  • Superoxide Dismutase-1
  • Proteasome Endopeptidase Complex