Abstract
The distribution of dietary copper after its absorption from the intestinal tract appears to occur in two stages. In the first stage, copper moves from the intestinal mucosa to the liver and kidney, and in the second stage, it moves from the liver to peripheral tissues. Evidence for these two stages of distribution comes from tracing the path of radiocopper after its intraduodenal or intragastric intubation (or direct injection) into rats. Immediately after intraduodenal administration, radioactive tracer is found in the portal blood, where it attaches to albumin, and transcuprein. The involvement of albumin in the initial transport of incoming copper is well documented (Owen, 1965 and 1971; Marceau and Aspin, 1971; Campbell et al., 1981; Gordon et al., 1987), and albumin has long been known to carry a high affinity copper binding site at its N-terminus (Breslow, 1964; Lau and Sarkar, 1971). The Kd for human albumin has been measured as 10-17 M in the absence of amino acids, and 10-22 M in the presence of L-histidine. As it is by far the most abundant plasma protein, albumin can theoretically bind up to about 40 μg Cu per ml of plasma or serum (assuming about 42 mg of albumin per ml). Nevertheless, albumin is normally relatively unsaturated with copper, binding only about 150 ng Cu per ml in normal adult humans, or less than 15% of the total copper in blood plasma.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Barnes, G., Frieden, E., 1984. Ceruloplasmin receptors of erythrocytes, Bioch. Biophvs. Res. Comm. 125:157–162.
Barrow, L., Tanner, M.S., 1988. Copper distribution among serum proteins in paediatric liver disorders and malignancies, Eur. J. Clin. Invest. 18: 555–560.
Breslow, E., 1964. Comparison of cupric ion-binding sites in myoglobin derivatives and serum albumin, J. Biol. Chem. 239:3252–3259.
Campbell, C.H., Brown, R., Linder, M.C., 1981. Circulating ceruloplasmin is an important source of copper for normal and malignant cells, Biochim. Biophys. Acta 678:27–38.
Dameron, C. T., Harris, E.D., 1987b. Regulation of aortic copper/zinc superoxide dismutase. Ceruloplasmin and albumin reactivate and transfer copper to the enzyme in culture, Bioch. J. 248:669–675.
Dameron, C. T., Harris, E.D., 1987a. Regulation of aortic copper/zinc superoxide dismutase with copper. Effects in vivo, Bioch. J. 248:663–668.
Dameron, C. T., Harris, E.D., 1987b. Regulation of aortic copper-zinc superoxide dismutase. Ceruloplasmin and albumin reactivate and transfer copper to the enzyme in culture, Bioch. J. 248:669–675.
Darwish, H.M., Cheney, J.C., Schmitt, R.C., Ettinger, M.J., 1984. Mobilization of copper (II) from plasma components and mechanism of hepatic copper transport. Am. J. Phvsiol. 246: G72–G79.
Frieden, E., 1981. Ceruloplasmin: A multifunctional metalloprotein of vertebrate plasma, in Metal Ions in Biological Systems, H. Sigel (ed.), New York and Basel: Marcell Dekker, pp. 1171–42.
Goode, CA., Almezedah, F., Linder, M.C., 1989. Forms of ceruloplasmin in the serum of the rat and man. Am. J. Cell Biol. Abstract #3623.
Gordon, D.T., Leinart, A.S., Cousins, J.R., 1987. Portal copper transport in rats by albumin, Am. J. Phys. 252.E327–333.
Harris, E.D., DiSilvestro, R.A., 1981. Correlation of lysyl oxidation activation with the p-phenylenediamine oxidase activity (ceruloplasmin) in serum, Proc. Soc. Exp. Med. 166:528–531.
Hartter, D.E., Barnea, A., 1988. Brain tissue accumulates 67Cu by two ligand-dependent saturable processes, J. Biol. Chem. 263:799–805.
Hsieh, S., Frieden, E., 1975. Evidence for ceruloplasmin as a copper transport protein, Biochem. Biophys. Res. Commun. 67:1326–1331.
Kataoka, M., Tavassoli, M., 1985. Identification of ceruloplasmin receptors on the surface of human blood monocytes, granulocytes and lymphocytes, Exp. Hematol. 13: 806–810.
Lau, S., Sarkar, B., 1971. Ternary coordination complex between human serum albumin, copper(II) and L-histidine, J. Biol. Chem. 246:5938–5943.
Lau, S., Sarkar, B., 1984. Comparative studies of manganese(II)-, nickel(II)-, zinc(II)-, copper(II)- cadmium(II)-, and iron(III)- binding components in human cord and adult sera, Can. J. Biochem. Cell Biol. 62:449–455.
Levy, M., Sober, T., 1960. A simple chromatographic method for preparation of gamma globulin, Proc. Soc. Exp. Biol. Med. 103: 250–252.
Linder, M.C., 1988): The biochemistry of copper (Series on the biochemistry of the elements, E. Frieden (ed.), New York: Plenum, in preparation.
Linder, M.C. (1985): Nutritional biochemistry of the trace elements. In Nutritional biochemistry and metabolism, M.C. Linder (ed.), pp. 151–197. New York: Elsevier.
Linder, M.C, Goode, CA., Weiss, K.C, Wirth, P.L., Vu, H.M., 1988. Mammalian copper transport: Review and recent findings. Proceedings of the Symposium on Metabolism of Minerals and Trace Elements in Human Disease, New Delhi/Aligarh/Srinagar, India, Sept., 1987, M. Abdulla, B. Sarkar (eds.), London: Libbey, in press.
Linder, M.C., Goode, CA., 1988. Evidence for transfer of copper from ceruloplasmin to the plasma membrane of rat brain cells during copper uptake, FASEB J. 2: Abstract #.
Linder, M.C, Houle, P.A., Isaacs, E., Moor, J.R., Scott, L.E., 1979b. Copper regulation of ceruloplasmin in copper deficient rats, Enzyme 24:23–35.
Linder, M.C, Weiss, K.C., Vu, H.M., 1987. Structure and function of transcuprein in transport of copper by mammalian blood plasma, Proceedings of the 6th International Conference on Trace Elements in Man and Animals (TEMA-6), Asilomar, CA.
Linder, M.C, Moor, J.R., Wright, K, 1981. Ceruloplasmin assays in diagnosis and treatment of human lung, breast and gastrointestinal cancer, J. Nat. Cancer Inst. 67:263–275.
Linder-Horowitz, M., Ruettinger, R.T., Munro, H.N., 1970. Iron induction of electorphoretically -different ferritins in rat liver, heart, and kidney, Bioch. Biophys. Acta 200: 442–448.
McArdle, H.J., Guthrie, J.R., Ackland, M. L., Danks, D.M., 1987. Albumin has no role in the uptake of copper by human fibroblasts, J. Inorg. Chem. 28:00–000.
McKee, D.J., Frieden, Earl, 1971. Binding of transition metal ions by ceruloplasmin (ferroxidase), Biochem. 10:3880–3883.
Marceau, N., Aspin, N., 1973. The intracellular distribution of the radiocopper derived from ceruloplasmin and from albumin, Biochim. Biophys. Acta 328:338–350.
Morgan, W.T., 1985. The histidine-rich glycoprotein of serum has a domain rich in histidine, proline, and glycine that binds heme and metals, Biochem. 24:1496–1501.
Morley, C.G.D., Bezkorovainy, A., 1985. Cellular iron uptake from transferrin: is endocytosis the only mechanism? Internat. J. Bioch. 17:553–564.
Mulligan, M., Althaus, B.A., Linder, M.C., 1986. Non-ferritin, non-heme iron pools in rat tissues. Internat. J. Bioch. 18: 791–798.
Neumann, P.Z., Sass-Kortsak, A., 1967. The state of copper in human serum: evidence for an amino acid-bound fraction, J. Clin. Invest. 46:646–658.
Nunoz, M.T., Cole, E.S., Glass, J., 1983. The reticulocyte plasma membrane pathway of iron uptake as determined by the mechanism of alpha, alpna’-dipyridyl inhibition, J. Biol. Chem. 258:1146–1151.
Orena, S.J., Goode, C.A., Linder, M.C., 1986. Binding and uptake of copper from ceruloplasmin, Biochem. Biophys. Res. Commun. 139:822–829.
Owen, C.A., Jr., 1965. Metabolism of radiocopper (Cu64) in the rat, Am. J. Physiol. 209:900–904.
Owen, C.A., Jr., 1971. Metabolism of copper 67 by the copper-deficient rat, Am. J. PhysioL 221:1722–1727.
Peters, T., 1977. Serum albumin: recent progress in the understanding of its structure and biosynthesis, Clin. Chem. 23:5–12.
Sarkar, B., Kruck, T.P.A., 1966. Copper-amino acid complexes in human serum, in Biochemistry of Copper. J. Peisach, P. Aisen, W.E. Blumberg (eds.), New York: Academic Press, pp. 183–1961.
Sarkar, B., Laussac, J.-P., Lau, S.-JY, 1983. Transport forms of copper in human serum, in Biological Aspects of Metals and Metal-Related Diseases. B. Sarkar (ed.), Raven Press, New York, pp. 23–40.
Stevens, M.D., DiSilvestro, R.A., Harris, E.D., 1984. Specific receptor for cerulosplasmin in membrane fragments from aortic and heart tissues, Biochem. 23:261–1266.
Weiss, K.C., Linder, M.C., and the Los Alamos Radiological Medicine Group, 1985. Copper transport in rats involving a new plasma protein, Am. J. Physiol. 249:E77–E88.
Wirth, P.L., Linder, M.C., 1985. Distribution of copper among components of human serum, J. Nat. Cancer Inst. 75:277–284.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
Goode, C.A., Dinh, C.T., Linder, M.C. (1989). Mechanism of Copper Transport and Delivery in Mammals: Review and Recent Findings. In: Kies, C. (eds) Copper Bioavailability and Metabolism. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0537-8_11
Download citation
DOI: https://doi.org/10.1007/978-1-4613-0537-8_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-7855-9
Online ISBN: 978-1-4613-0537-8
eBook Packages: Springer Book Archive