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ORIGINAL RESEARCH ARTICLE

Copper, Zinc-Superoxide Dismutase Protein but not mRNA Is Lower in Copper-Deficient Mice and Mice Lacking the Copper Chaperone for Superoxide Dismutase

Department of Biochemistry and Molecular Biology, University of Minnesota Duluth School of Medicine, Duluth, Minnesota 55812

Cu, Zn-superoxide dismutase (SOD1) is an abundant metalloenzyme important in scavenging superoxide ions. Cu-deficient rats have lower SOD1 activity and protein, possibly because apo-SOD1 is degraded faster than holo-SOD1. Previous work with mice lacking the Cu chaperone for SOD1 (CCS) indicated a drastic loss of SOD1 activity but not protein, suggesting an accumulation of apo-SOD1. We produced dietary Cu deficiency in mice to clarify this issue. Compared with Cu-deficient rats, reduction in liver SOD1 activity and protein was much less than Cu-deficient mouse dams and offspring. However, after perinatal Cu deficiency, 4-week-old mouse pups had lower levels of SOD1 activity and protein in liver and heart, but not brain, compared with Cu-adequate controls. Reduction in brain Cu was greater than liver. In CCS –/– mice, there was severe reduction in liver, heart, and brain SOD1 activity and protein. In fact, the reduction in activity was similar to the loss of protein. Neither Cu-deficient mouse liver nor CCS –/– mouse liver had altered SOD1 mRNA levels compared with control values. These results in mice are comparable with rats and suggest a posttranscriptional mechanism for reduction of SOD1 protein when Cu is limiting in SOD1.

Key Words: copper-deficient • rats • mice • copper, zinc-superoxide dismutase • CCS • chaperone • enzyme activity, mRNA, Western blots

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