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pubmed-article:10461909pubmed:abstractTextWe have investigated the response to oxidative stress in a model system obtained by stable transfection of the human neuroblastoma cell line SH-SY5Y with plasmids directing constitutive expression of either wild-type human Cu,Zn superoxide dismutase or a mutant of this enzyme (H46R) associated with familial amyotrophic lateral sclerosis. We report that expression of mutant H46R Cu,Zn superoxide dismutase induces a selective increase in paraquat sensitivity that is reverted by addition of D-penicillamine. Furthermore, expression of this mutant enzyme affects the activity of the endogenous wild-type enzyme both in basal conditions and in copper overloading experiments. Our data indicate that aberrant metal chemistry of this mutant enzyme is the actual mediator of oxidative stress and that concurrent impairment of the activity of wild-type endogenous enzyme compromises the cell's ability to respond to oxidative stress.lld:pubmed
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pubmed-article:10461909pubmed:articleTitleAberrant copper chemistry as a major mediator of oxidative stress in a human cellular model of amyotrophic lateral sclerosis.lld:pubmed
pubmed-article:10461909pubmed:affiliationIRCCS S. Lucia, Rome, Italy.lld:pubmed
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