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Prohaska, J.R. et al.

Prohaska, Gybina, Broderius, Brokate,

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. No reduction in Cu- rat midbrain PAM protein was detected although PAM activity was reduced 40%. In 12-day-old ( P12) mouse pups derived from dams that began Cu deficiency on day 7 of gestation, there was a parallel reduction in brain PAM activity and protein of 40-50%. PAM mRNA levels assessed in atria and brains from Cu+ and Cu- rats and mice were not altered by dietary treatment, suggesting a posttranscriptional mechanism for lower PAM protein when Cu is limiting in the cell, perhaps due to enhanced apoprotein turnover.[1]

References

Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice. Prohaska, J.R., Gybina, A.A., Broderius, M., Brokate, B. Arch. Biochem. Biophys. (2005) [Pubmed]

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