Abstract
THE relationship of liver proteins to the metabolism of copper in the mammalian organism is poorly understood. The cuproprotein engaging the attention of most investigators is ceruloplasmin, which seems to be synthesized in the liver1,2, although its serum concentration is the parameter measured in various physiological and disease states. Other hepatic proteins or enzyme systems have been suggested to be involved in the uptake of copper from the plasma and its incorporation into ceruloplasmin3,4; in the storage of copper in the developing foetus5—in the adult when abnormal amounts of copper enter the organism3,6 or in patients with hepatolenticular degeneration7; and in the transport of copper within the liver cell8. The predilection of copper for binding to proteins8 suggests that this process is important in the metabolism of the metal in the liver, for example, in the maintenance of neutral copper balance after early postnatal growth. If so, interference with protein synthesis could then be expected to result in an altered ability of the liver to retain copper. This hypothesis was tested in subacute experiments by treating rats with copper sulphate and with inhibitors of protein synthesis.
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GREGORIADIS, G., SOURKES, T. Role of Protein in Removal of Copper from the Liver. Nature 218, 290–291 (1968). https://doi.org/10.1038/218290a0
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DOI: https://doi.org/10.1038/218290a0
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