Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice.

Peptidylglycine-alpha-amidating monooxygenase (PAM) is a copper-dependent enzyme involved in peptide posttranslational activation. Dietary Cu deficiency (Cu-) was studied to determine if lower PAM activity was due to reduction in protein or cofactor limitation. PAM activity was lower in cardiac atria of Cu- rats than Cu-adequate (Cu+) rats and there was a 50% equivalent reduction in PAM protein.

Copper, zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase.

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.

The timing of perinatal copper deficiency in mice influences offspring survival.

Copper is an essential metal during development. Female Swiss Webster mice were fed a modified AIN-76A diet low in copper (0.3 mg Cu/kg and 43 mg Fe/kg; -Cu).