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Oxidized SOD1 alters proteasome activities in vitro and in the cortex of SOD1 overexpressing mice
Author(s) -
Pecheur Marie Le,
Bourdon Emmanuel,
Paly Evelyne,
Farout Luc,
Friguet Bertrand,
London Jacqueline
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.048
Subject(s) - sod1 , proteasome , genetically modified mouse , in vitro , transgene , superoxide dismutase , chemistry , oxidative stress , dismutase , microbiology and biotechnology , biochemistry , gene , biology
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.