Amidating monooxygenase

In an attempt to identify a sensitive and improved marker of mammalian copper status during neonatal development experiments compared two plasma cuproenzymes, peptidylglycine α-amidating monooxygenase (PAM ), an enzyme involved in peptide posttranslational activation, to ceruloplasmin (Cp), a ferroxidase involved in iron mobilization.Dietary Cu deficiency (Cu−) was studied in dams and offspring at postnatal age 3 (P3), P12, and P28.Furthermore, PAM activity has not been evaluated in neonatal mammals.The purpose of the current studies was to compare Cp and PAM activity in two rodent models during lactation to determine if PAM might be a more suitable biochemical marker than Cp to evaluate copper status during this physiological state.PAM is normally a membrane bound or vesicular enzyme but is detected in plasma (Eipper et al., 1985).Previous research has indicated that the in vitro biochemical activity of PAM is lower in tissues and plasma of copper deficient rats (Prohaska et al., 1995; Peterson and Prohaska, 1999).With proper controls, each enzyme can be used to assess copper status.Mammals rely on many exogenous dietary factors to ensure proper development and homeostasis.

Cp, an alpha-2 globulin, is an acute phase protein that is highly expressed during inflammation, which can be a common confounding variable using Cp to assess copper status.Rodent Cp activity rose during lactation whereas PAM activity fell.Reduction in Cp activity was more severe than reduction in PAM activity in Cu− offspring and dams.Both Cp and PAM activity were influenced by age and dietary copper intake.) were purchased commercially (Harlan Sprague Dawley, Indianapolis, IN, USA).Animals received one of two dietary treatments, copper-deficient (Cu−) or copper-adequate (Cu ), consisting of a copper-deficient purified diet (Teklad Laboratories, Madison, WI, USA) and either low copper drinking water or copper-supplemented drinking water, respectively.

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