1. Cardiac Cytochrome c Oxidase Activity and Contents of Subunits I and 4 Are Altered in Offspring by Low Prenatal Copper Intake by Rat Dams.
- Author
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Johnson, W. Thomas and Anderson, Cindy M.
- Subjects
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CYTOCHROME oxidase , *CYTOCHROME c , *CYTOCHROMES , *COPPER compounds , *COPPER , *COPPER content of drinking water , *DAMS , *HYDRAULIC structures , *DAM safety - Abstract
It has been reported previously that the offspring of rat dams consuming low dietary copper (Cu) during pregnancy and lactation experience a deficiency in cardiac cytochrome c oxidase (CCO) characterized by reduced catalytic activity and mitochondrial and nuclear subunit content after postnatal d 10. The present study was undertaken to determine whether the cardiac CCO deficiency was caused directly by low postnatal Cu intake or whether it was a prenatal effect of low Cu intake by the dams that became manifest postnatally. Dams were fed either a Cu-adequate diet (6 mg Cu/kg) or Cu- deficient diet (1 mg Cu/kg) beginning 3 wk before conception and throughout gestation and lactation. One day following parturitiori, several litters from Cu-adequate dams were cross fostered to Cu-deficient dams and several litters from Cu- deficient dams were cross fostered to Cu-adequate dams. Litters that remained with their birth dams served as controls. CCO activity, the content of the mitochondrial-encoded CCO subunit 1 )COX1), and the content of the nuclear-encoded subunit COX4 in cardiac mitochondria were reduced in the 21-d-old offspring of Cu-deficient dams. COX1 content was normal in the 21-d-old cross-fostered offspring of Cu-deficient dams, but CCO activity and COX4 were reduced. Cross fostering the offspring of Cu-adequate dams to Cu-deficient dams did not significantly affect CCO activity, COX1 content, or COX4 content in cardiac mitochondria of 21-d-old offspring. These data indicate that low prenatal Cu intake by dams was the determinant of CCO activity in cardiac mitochondria of the 21-d-old offspring and may have led to the assembly of a less-than-fully active holoenzyme. [ABSTRACT FROM AUTHOR]
- Published
- 2008
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