Abstract
In this chapter, we review what we know about the availability of copper in foodstuffs, its intestinal absorption, transport to cells and tissues, uptake by and distribution within cells, and its metabolism, release, and excretion from the body. The emphasis is on the adult human being. More detailed information may be found in books edited by Linder (1,2), Sarkar (3), and Leone and Mercer (4), 1996 reviews by Linder (5) and Linder and Hazegh-Azam (6), and more specialized reviews by Harris (7), Pena et al. (8), Linder et al. (9,10), and others (11,12).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Linder, M. C. (ed.) (1991) Biochemistry of Copper. Plenum, New York.
Linder, M. C. (ed.) (1991) Nutritional Biochemistry and Metabolism, 2nd ed. Appleton amp; Lange, Norwalk, CT.
Sarkar, B. (ed.) (1999) Metals and Genetics. Kluwer Academic/Plenum, New York.
Leone, A. and Mercer, J. F. B. (eds.) (1999) Copper Transport and its Disorders, Advances in Experimental Medicine and Biology, Vol. 448. Kluwer Academic/Plenum, New York.
Linder, M. C. and Hazegh-Azam, M. (1996) Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797S - 811S.
Linder, M. C. (1996) Copper, in Present Knowledge in Nutrition, 7th ed. ( Ziegler, E. E. and Filer, L. J., Jr., eds.), ILSl, Washington, DC, pp. 307–319.
Harris, E. D. (2000) Cellular copper transport and metabolism. Annu. Rev. Nutr. 20, 291–310.
Pena, M. M. O., Lee, J., and Thiele, D. J. (1999) A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129, 1251–1260.
Linder, M. C., Wooten, L., Cerveza, P., Cotton, S., Shulze, R., and Lomeli, N. (1998) Copper transport. Am. J. Clin. Nutr. 67 (Suppl.), 965S - 971S.
Linder, M. C., Lomeli, N. A., Donley, S., Mehrbod, F., Cerveza, P., Cotton, S., et al. (1999) Copper transport in mammals, in Copper Transport and its Disorders ( Leone, A. and Mercer, J. F. B., eds.), Kluwer Academic/Plenum, New York, pp. 1–16.
Vulpe, C. and Packman, S. (1995) Cellular copper transport, Annu. Rev. Nutr. 15, 293–322.
Eide, D. J. (1998) Molecular biology of metal ion transport in Saccharomyces cerevisiae. Annu. Rev. Nutr. 18, 441–469.
Dunham, R. and Smith, H. E. (1992) Lead and copper-a model home approach. Proceedings of the Water Quality Technology Conference, pp. 341–352.
Walker, W. R. (1982) The results of a copper bracelet clinical trial and subsequent studies, in Inflammatory Diseases and Copper ( Sorenson, J. R. J., ed.), Humana, Totowa, NJ, pp. 469–478.
Goode, C. A. (1991) Copper and disease, in Biochemistry of Copper ( Linder, M. C., ed.), Plenum, New York, pp. 331–366.
Scott, K. C. and Turnlund, J. R. (1994) Compartment model of copper metablism in adult men. J. Nutr. Biochem. 5, 342–350.
Turnlund, J. R., Keyes, W. R., Anderson, H. L., and Acord, L. L. (1989) Copper absorption and retention in young men at three levels of dietary copper using the stable isotope 65Cu. Am. J. Clin. Nutr. 49, 870–878.
Trumbo, P., Yates, A. A., Schlicker, S., and Poos, M. (2001) Dietary reference intakes: Vitamin A, vitamin K, arsenic, boron, chromium, copper, iodine, iron, manganese, molybdenum, nickel, silicon, vanadium and zinc. J. Am. Diet. Assoc. 101, 294–301.
Turnlund, J. R., Keyes, W. R., Peiffer, G. L., and Scott, K. C. (1998) Copper absorption, excretion, and retention by young men consuming low dietary copper determined by using the stable isotope 65Cu. Am. J. Clin. Nutr. 67 (Suppl.), 1219–1225.
Wapnir, R. A. and Lee, S. Y. (1993) Dietary regulation of copper absorption and storage in rats: effects of sodium, zinc and histidine-zinc. J. Am. Coll. Nutr. 12, 714–719.
Yu, S., West, C. E., and Beynen, A.C. (1994) Increasing intakes of iron reduce status, absorption and biliary excretion of copper in rats. Br. J. Nutr. 71, 887–895.
Cohen, N. L., Illowsky, B. and Linder, M. C. (1979) Altered copper absorption in tumor bearing and estrogen treated rats. Am. J. Physiol. 236, E309 - E315.
Arredondo, M., Uauy, R., and Gonzalez, M. (2000) Regulation of copper uptake and transport in intestinal cell mono-layers by acute and chronic copper exposure. Biochim. Biophys. Acta 1474, 169–176.
Zerounian, N., Mohammadi, G., and Linder, M. C. (2001) Effects of copper and iron availability on copper absorption in the Caco2 cell intestinal model. J. Trace Elents Exp. Biol. 14, 322 [Abstract].
Lee, J., Prohaska, J. R., Dagenais, S. L., Glover, T. W., and Thiele, D. J. (2000) Isolation of a murine copper transporter gene, tissue specific expression and functional complementation of a yeast copper transport mutant. Gene 254, 87–96.
Dancis, A., Yuan, D. S., Haile, D. Askwith, D., Eide, D., Moehle, C., et al. (1994) Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell 76, 393–402.
Dancis, A., Haile, D., Yuan, D. S., and Klausner, R. D. (1994) The Saccharomyces cerevisiae transport protein (ctrlp). Biochemical characterization, regulation by copper, and physiological role in copper uptake. J. Biol. Chem. 269, 25,66025, 667.
Labbe, S. and Thiele, D. J. (1999) Pipes and wiring: the regulation of copper uptake and distribution in yeast. Trends Microbiol. 7, 500–505.
Zhou, B. and Gitschier, J. (1997) hCTR1: a human gene for copper uptake identified by complementation in yeast. Proc. Natl. Acad. Sci. USA 94, 7481–7486.
Kuo, Y.-M., Zhou, B., Cosco D., and Gitschier, J. (2001) The copper transporter CTR1 provides an essential function in mammalian embryonic development. Proc. Natl. Acad. Sci. USA 98, 6836–6841.
Moller, L. B., Petersen, C., Lund, C., and Horn, N. (2000) Characterization of the hCTR1 gene: genomic organization, function, expression and identification of a highly homologous processed gene. Gene 257, 13–22.
Lee, J., Prohaska, J. R. and Thiele, D. J. (2001) Essential role for mammalian copper transporter Ctrl in copper homeostasis and embryonic development. Proc. Natl. Acad. Sci. USA 98, 6842–6847.
DeRome, L. and Gadd, G. M. (1987) Measurement of copper uptake in Saccharomyces cerevisiae using a Cue+-selective electrode. FEMS Microbiol. Lett. 43, 283–287.
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., et al. (1997) Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388, 482–488.
Fleming, M. D., Trenor, C. C. III, Su, M. A., Foernsler, D., Beier, D. R., Dietrick, W. F. et al. (1997) Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nature Genet. 16, 383–386.
Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D., and Andrews, N. C. (1998) Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. USA 95, 1148–1153.
Roy, C. N. and Enns, C. A. (2000) Iron homeostasis: new tales from the crypt. Blood 96, 4020–4027.
Andrews, N. C. (2000) Intestinal iron absorption: current concepts circa 2000. Dig. Liver Dis. 32, 56–61.
Hentze, M. W., Muckenthaler, M., Brennan, K., Galy, B., Hubert, N., and Hentze, S. (2001) Genome-wide analysis of iron metabolism. Biolron 2001.
Zoller, H., Theurl, I., Vogel, W., and Weiss, G. (2001) Pathways for iron dependent regulation of divalent metal transporter1 and ferroportin 1. Biolron 2001.
Zerounian, N.R. and Linder, M.C. (2001) Effects of copper and ceruloplasmin on iron transport in the Caco2 cell intestinal model..1. Nutr. Biochem. 13, 138–148.
Arredondo, M., Mazariegos, D., and Nunez, M. T. (2001) The activity of the iron transporter DMT1 is inhibited by the hereditary hemochromatosis gene product. Biolron 2001.
Klomp, L. W., Lin, S. J., Yuan, D. S., Klausner, R. D., Culotta, V. C., and Gitlin, J. D. (1997) Identification and functional expression of HAH1: a novel human gene involved in copper homeostasis. J. Biol. Chem. 272, 9221–9226.
Larin, D., Mekios, C., Das, K., Ross, B., Yang, A. S., and Gilliam, T. C. (1999) Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic chaperone, HAH1. J. Biol. Chem. 274, 28,49728, 504.
Culotta, V. C., Klomp, L. W., Strain, J., Casareno, R. L., Krems, B., and Gitlin, J. D. (1997) The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23,469–23, 472.
Casareno, R. L., Waggoner, D., and Gitlin, J. D. (1998) The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J. Biol. Chem. 273, 23,625–23, 628.
Glerum, D.M., Shtanko, A. and Tzagoloff, A. (1996) Characterization of COX17: a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 271, 14,504–14, 509.
Amaravadi, R., Glerum, D. M., and Tzagoloff, A. (1997) Isolation of a eDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. Hum. Genet. 99, 329–333.
Sonsma, T. Hixon, P., McWilliams, K., and Linder, M. C. (1981) Mechanism and regulation of intestinal copper absorption, in Trace Element Metabolism in Man and Animals ( Howell, J. M., Gawthorne, J. M., and White, C. L., eds.), Australian Academy of Science, Canberra, pp. 145–147.
Fischer, P. W. F., Giroux, A., and Labbe, M. R. (1983) Effects of zinc on mucosal copper binding and on the kinetics of copper absorption. J. Nutr. 113, 462–469.
Bremner, I. (1980) Absorption, transport and distribution of copper. Ciba Found. Symp. (1979) Exerpta Med. 79, 23–48.
Ogiso, T., Ogawa, N., and Miura, T. (1979) Inhibitory effect of high dietary zinc on copper absorption in rats. II. Binding of copper and zinc to cytosol proteins in the intestinal mucosa. Chem. Pharm. Bull. 27, 515–521.
Freedman, J. H. and Peisach, J. (1989) Intracellular copper transport in cultured hepatoma cells. Biochem. Biophys. Res. Commun. 164, 134–140.
Freedman, J. H., Ciriolo, M. R., and Peisach, J. (1989) The role of glutathione in copper metabolism and toxicity. J. Biol. Chem. 264, 5598–5605.
Portnoy, M. E., Schmidt, P. J., Rogers, R. S., and Culotta, V. C. (2001) Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae. Mol. Genet. Genom. 265, 873–882.
Hamsa, I., Faisst, A., Prohaska, J., Chen, J., Gruss, P. and Gitlin, J. D. (2001) The metallochaperone Atoxl plays a critical role in perinatal copper homeostasis. Proc. Natl. Acad. Sci. USA 98, 6848–6852.
Kaler, S. G. (1998) Metabolic and molecular bases of Menkes disease and occipital horn syndrome. Pediatr. Dev. Pathol. 1, 85–99.
Masuoka, J., Hegenauer, J., Van Dyke, B. R., and Saltman, P. (1993) Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin. J. Biol. Chem. 268, 21,533–21, 537.
Lau, S. and Sarkar, B. (1971) Ternary coordination complex between human serum albumin, copper(II) and L-histidine. J. Biol. Chem. 246, 5938–5943.
Masuoka, J. and Saltman, P. (1994) Zinc(II) and copper (II) binding to serum albumin. A comparative study of dog, bovine, and human albumin. J. Biol. Chem. 269, 25,557–25, 561.
Wirth, P. L. and Linder, M. C. (1985) Distribution of copper among multiple components of human serum. J. Natl. Cancer Inst. 75, 277–284.
Barrow, L. and Tanner, M. S. (1988) Copper distribution among serum proteins in paediatric liver disorder and malignancies. Eur. J. Clin. Invest. 18, 555–560.
Weiss, K. C. and Linder, M. C. (1985) Copper transport in rats involving a new plasma protein. Am. J. Physiol. 249, E77 - E88.
Liu, N. M., Lo, L. S. L., Askary, S. H.,Goforth, J., Vivas, E., Tsai, M., et al. (2002) Transcuprein is a macroglobulin regulated by copper and iron, in press.
Linder, M. C. (2001) Copper and genomic stability in mammals. Mutat. Res. 475, 151–152.
Huffman, D. L. and O’Halloran, T. V. (2001) Function, structure, and mechanism of intracellular copper trafficking proteins. Annu. Rev. Biochem. 70, 677–701.
Wernimont, A. K., Huffman, D. L., Lamb, A. L., O’Halloran, T. V., and Rosenzweig, A. C. (2000) Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 7, 766–771.
Goforth, J., Vivas, E., Liu, N., Askary, H. S., Lo, L. S. L., and Linder, M. C. (2001) Correspondence between rat transcuprein and human alpha-2-macoglobulin in copper binding. FASEB J. 15 [Abstract A271. 1.
Campbell, C. H., Brown, R., and Linder, M. C. (1981) Circulating ceruloplasmin is an important source of copper for normal and malignant cells. Biochim. Biophys. Acta 678, 27–38.
Lee, S. H., Lancey, R., Montaser, A., Madani, N. and Linder, M. C. (1993) Ceruloplasmin and copper transport during the latter part of gestation in the rat. Proc. Soc. Exp. Biol. Med. 203, 428–439.
Vargas, E. J., Shoho, A. R., and Linder, M. C. (1994) Copper transport in the Nagase analbuminemic rat. Am. J. Physiol. 267, G259 - G269.
Orena, S. J., Goode, C. A., and Linder, M. C. (1986) Binding and uptake of copper from ceruloplasmin. Biochem. Biophys. Res. Commun. 139, 822–825.
Harris, Z. L., Takahashi, Y. Miyajima, H., Serizawa, M., MacGillivray, R. T. A., and Gitlin, J. D. (1995) Aceruloplasminemia: molecular characterization of this disorder of iron metabolism. Proc. Natl. Acad. Sci USA 92, 2539–2543.
Meyer, L. A., Durley, A. P., Prohaska, J. R., and Harris, Z. L. (2001) Copper transport and metabolism are normal in Aceruloplasminemic mice. J. Biol. Chem., 276, 36,857–36, 861.
Hilton, M., Spenser, D. C., Ross, P. Ramsey, A., and McArdle, H. J. (1995) Characterisation of the copper uptake mechanism and isolation of the ceruloplasmin receptor/copper transporter in human placental vesicles. Biochim. Biophys. Acta 1245, 153–160.
Mas, A. and Sarkar, B. (1992) Uptake by 67Cu by isolated human trophoblast cells. Biochim. Biophys. Acta 1135, 123–128.
Percival, S. S. and Harris, E. D. (1990) Copper transport from ceruloplasmin: characterization of the cellular uptake mechanism. Am. J. Physiol. 258, C140 — C146.
Stevens, M. D., DiSilvestro, R. A., and Harris, E. D. (1984) Specific receptors for ceruloplasmin in membrane fragments from aortic and heart tissues. Biochemistry 23, 261–266.
Kataoka, M. and Tavassoli, M. (1985) Identification of ceruloplasmin receptors on the surface of human blood monocytes, granulocytes, and lymphocytes. Exp. Hematol. 13, 806–810.
Tavassoli, M., Kishimoto, T., and Kataoka, M. (1986) Liver endothelium mediates the hepatocyte’s uptake of ceruloplasmin. J. Cell Biol. 102, 1298–1303.
Ettinger, M. J., Darwish, H. M., and Schmitt, R. C. (1986) Mechanisms of copper transport from plasma to hepatocytes. Fed. Proc. 45, 2800–2804.
McArdle, H. J., Guthrie, J. R., Ackland, M. L., and Danks, D. M. (1987) Albumin has no role in the uptake of copper by human fibroblasts. J. Inorg. Biochem. 31, 123–131.
Schmitt, R. C., Darwish, H. M., Cheney, J. C., and Ettinger, M. J. (1983) Copper transport kinetics by isolated rat hepatocytes. Am. J. Physiol. 244, G183 - G191.
Zhou, H. and Thiele, D. J. (2001) Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 276, 20,529–20, 535.
Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C., and O’Halloran, T. V. (1999) Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284, 805–808.
Petris, M. J., Mercer, J. F. B., Culvenor, J. G., Lockhart, P., Gleeson, P. A. and Camakaris, J. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15, 6084–6095.
Camakaris, J., Petris, M. J., Bailey, L., Shen, P., Lockhart, P., Glover, T. W., et al. (1995) Gene amplification of the Menkes (MNK; ATP7A) P-type ATPase gene of CHO cells is associated with copper resistance and enhanced copper efflux. Hum. Mol. Genet. 4, 2117–2123.
Petris, M. J. and Mercer, J. F. B. (1999) The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum. Mol. Genet. 8, 2107–2115.
Camakaris, J., Voskoboinik, I., and Mercer, J. F. B. (1999) Molecular mechanisms of copper homeostasis. Biochem. Biophys. Res. Comm. 261, 225–232.
Schaefer, M., Roelofsen, J., Wolters, H., Hofmann, W. J., Muller, M., Kuipers, F., et al. (1999) Localization of the Wilson’s disease protein in human liver. Gastroenterology 117, 1380–1385.
Roelofsen, J., Wolters, H., Van Luyn, J. A., Miura, N., Kuipers, F., and Vonk, R. J. (2000) Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion. Gastroenterology 119, 782–793.
Kressner, M. S., Stockert, R. J., Morell, A. G., and Sternlieb, I. (1984) Origins of biliary copper. Hepatology 4, 867–870.
Chowrimootoo, G. F. E. and Seymour, C. A. (1994) The role of ceruloplasmin in copper excretion. Biochem. Soc. Trans. 22, 190S [Abstract].
Iyengar, V., Brewer, G. J., Dick, R. D., and Owyang, C. (1988) Studies of cholecystokinin-stimulated biliary secretions reveal a high molecular weight copper binding substance in normal subjects that is absent in patients with Wilson’s disease. J. Lab. Clin. Med. 111, 267–274.
Linder, M. C. and Roboz, M. (1986) Turnover and excretion of copper in rats as measured with 67Cu. Am. J. Physiol. 251, E551 - E555.
Bethin, K. E., Cimato, T. R., and Ettinger, M. J. (1995) Copper binding to mouse liver S-adenosyl homocysteine hydrolase and the effects of copper on its levels. J. Biol. Chem. 270, 20,702–20, 711.
Flood, D. G., Reaume, A. G., Gruner, J. A., Hoffmann, E. K., Hirsch, J. D., Lin, Y.-G., et al. (1999) Hindlimb motor neurons require Cu/Zn superoxide dismutase for maintenance of neuromuscular junctions. Am. J. Pathol. 155, 663–672.
Valentine, J. S., Hart, P. J., and Gralla, E. B. (1999) Copper-zinc superoxide dismutase and ALS, in Copper Transport and its Disorders ( Leone, A. and Mercer, J. F. B., eds.), Kluwer Academic/Plenum, New York, pp. 193–203.
Cam, M. T., Battistoni, A., Ferri, A., Gabbianelli, R. and Rotilio, G. (1999) A study of the dual role of copper in superoxide dismutase as antioxidant and pro-oxidant in cellular models of amyotropic lateral sclerosis, in Copper Transport and its Disorders ( Leone, A. and Mercer, J. F. B., eds.), Kluwer Academic/Plenum, New York, pp. 205–213.
Johnson, M. A., Macdonald, T. L., Mannick, J. B., Conaway, M. R., and Gaston, B. (2001) Accelarated S-nitrosothiol breakdown by amyotropic lateral sclerosis mutant copper, zinc-superoxide dismutase. J. Biol. Chem., 276, 39,87239, 878.
Levy, M. A., Tsai, Y. H., Reaume, A., and Bray, T. M. (2001) Cellular response of antioxidant metalloproteins in Cu/ Zn SOD transgenic mice exposed to hyperoxia. Am. J. Physiol. 281, L172 — L182.
Kang, Y. J. (1999) The antioxidant function of metallothionein in the heart. Proc. Soc. Exp. Biol. Med. 222, 263–273.
Ghoshal, K., Majumder, S., Li, Z., Bray, T. M., and Jacob, S. T. (1999) Transcriptional induction of MT-I and II genes in the livers of Cu/Zn-SOD knockout mice. Biochem. Biophys. Res. Commun. 264, 735–742.
Ragan, H. A., Nacht, S., Lee, G. R., Bishop, C. R., and Cartwright, G. E. (1969) Effect of ceruloplasmin on plasma iron in copper deficient swine. Am. J. Physiol. 217, 1320–1323.
Osaki, S. and Johnson, D. A. (1969) Mobilization of liver iron by ferroxidase (ceruloplasmin). J. Biol. Chem. 244, 5757–5761.
Tran, T., Ashraf, M., Jones, L. T., Westbrook, T., Hazegh-Azam, M., and Linder, M. C. (2001) Dietary iron status has little effect on expression of ceruloplasmin but alters that of ferritin in rats. J. Nutr. 132, 351–356.
Harris, Z. L., Durley, A. P., Man, T. M., and Gitlin, J. D. (1999) Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. USA 96, 10,812–10, 817.
Yoshida, K., Furihata, K., Takeda, S., Nakamura, A., Yamamoto, K., Hiyamuta, S., et al. (1995) A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nature Genet. 9, 267–272.
Roeser, H. P., Lee, G. R., Nacht, S., and Cartwright, G. E. (1980) A role of ceruloplasmin in iron metabolism. J. Clin. Invest. 49, 2408–2417.
Patel, B. N. and David, S. (1997) A novel glcosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes. J. Biol. Chem. 272, 20,185–20, 190.
Salzer, J. L., Lovejoy, L., Linder, M. C., and Rosen, C. (1998) Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin. J. Neurosci. 54, 147–157.
Patel, B. N., Dunn, R. J., and David, S. (2000) Alternative RNA splicing generates a glycosylphosphatidylinositolanchored form of ceruloplasmin in mammalian brain. J. Biol. Chem. 275, 4305–4310.
Harris, Z. L., Klomp, L. W., and Gitlin, J. D. (1998) Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Am. J. Clin, Nutr. 67 (Suppl.), 972S - 977S.
Mukhopadhyay, C. K., Mazumder, B., and Fox, P. L. (1999) Role of hypoxia inducible factor-1 in transcription activation of ceruloplasmin by iron deficiency. J. Biol. Chem. 275, 21,048–21, 054.
Mukhopadhyay, C. K. and Fox, P. L. (2001) Dual regulation of ceruloplasmin transcription by insulin in HepG2 cells. Bioiron 2001.
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., et al. (1999) Hephaestin, a ceruloplasmin homolog implicated in intestinal iron transport, is defective in the sla mouse. Nature Genet. 21, 195–199.
Vulpe, C. D., Attieh, Z. K., Allaeddine, R. M., and Su, T. (2001) Identification of a ferroxidase activity for hephaestin. FASEB J. 15 [Abstract] A800.
Fife, R. S. Moody, S., Houser, D., and Proctor, C. (1994) Studies of copper transport in cultured bovine chondrocytes. Biochim. Biophys. Acta 1201, 19–22.
Fife, R. S. Palmoski, M. J., and Brandt, K. D. (1986) Metabolism of cartilage matrix glycoprotein in normal and osteoarthritic canine articular cartilage. Arthritis Rheum. 29, 1256–1262.
Haddad, A. De Almedia, J. C., Laicine, E. M., Fife, R. S., and Pelletier, G. (1990) The origin of the intrinsic glycoproteins of the rabbit vitreous body: an immunohistochemical and autoradiographic study. Exp. Eye Res. 50, 555–561.
Trackman, P. C., Pratt, A. M., Wolanski, A., Tang, S. S., Offner, G. D., Troxler, R. F., et al. (1990) Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence. Biochemistry 29, 4863–4870.
Hamalainen, E. R., Jones, T. A., Sheer, D., Taskinen, K., Pihlajaniemi, T., and Kivirikko, K. I. (1991) Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.2–31.2. Genomics 11, 508–516.
Tang, C. and Klinman, J. P. (2001) The catalytic function of bovine lysyl oxidase in the absence of copper. J. Biol. Chem. 276, 30,575–30, 578.
Wang, S. X., Mure, M., Medzihradszky, K. F., Burlingame, A. L., Brown, D. E., Dooley, D. M., et al. (1996) A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science 273, 1078–1084.
Rucker, R. B., Kosonen, T., Clegg, M. S., Mitchell, A. E., Rucker, B. R., Uriu-Hare, J. Y., et al. (1998) Copper, lysyl oxidase, and extracellular matrix protein cross-linking. Am. J. Clin. Nutr. 67 (Suppl.), 996S - 1002S.
Jourdan-Le Saux, C., Tronecker, H., Bogic, L., Bryant-Greenwood, G. D., Boyd, C. D., and Csiszar, K. (1999) The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues. J. Biol. Chem. 274, 12,939–12, 944.
Maki, J. M. and Kivirikko, K. I. (2001) Cloning and characterization of a fourth human lysyl oxidase isoenzyme. Biochem. J. 355, 381–387.
Brown, D. R. (2001) Prion or prejudice: normal protein and the synapse. Trends Neurosci. 24, 85–90.
Aronoff-Spencer, E., Burns, C. S., Avdievich, N. I., Gerfen, G. J., Peisach, J., Antholine, W. E., et al. (2000) Identification of the Cu2+/— binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry 39, 12, 760–13, 771.
Miura, T., Hori-I, A., and Takeuchi, H. (1996) Raman spectroscopy study on the copper(II) binding mode of prion octapeptide and its pH dependence. FEBS Lett. 396, 248–252.
McMahon, H. E. M., Mange, A., Nishida, N., Cerminon, C., Casanova, D., and Lehmann, S. (2001) Cleavage of the amino terminus of the prion protein by reactive oxygen species. J. Biol. Chem. 276, 2286–2291.
Brown, D. R., Clive, C., and Haswell, S. J. (2001) Antioxidant activity related to copper binding of native prion protein. J. Neurochem. 76, 69–76.
Brown, D. R., Wong, B.-S., Hafiz, F., Clive, C., Haswell, S. J., and Jones, I. M. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344, 1–5.
Brown, D. R., Hafiz, F., Glasssmith, L. L., Wong, B.-S., Jones, I. M., Clive, C., et al. (2000) Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J. 19, 1180–1186.
Milhavet, O., McMahon, H. E. M., Rachidi, W., Nishida, N., Katamine, S., Mange, A., et al. (2000) Prion infection impairs the cellular response to oxidative stress. Proc. Natl. Acad. Sci. USA 97, 13,937–13, 942.
Klamt, F., Dal-Pizzol, F., Conte da Frota M. L., Jr., Walz, R., Andrades, M. E., Gomes da Silva, E., et al. (2001) Imbalance of antioxidant defense in mice lacking cellular prion protein. Free Radical Biol. Med. 30, 1137–1144.
Brown, D. R. (1999) Prion protein expression aids cellular uptake and veratidine-induced release of copper. J. Neurosci. Res. 58, 717–725.
Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1997) Expression of prion protein in PC12 is enhanced by exposure to oxidative stress. Int. J. Del). Neurosci. 15, 961–972.
Sumudhu, W., Perera, S., and Hooper, N. M. (2001) Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat. Curr. Biol. 11, 519–523.
Brockes, J. P. (1999) Topics in prion cell biology. Curr. Opin. Neurobiol. 9, 571–577.
Linder, M. C., Donley, S., Dominguez, D., Wooten, L., Mehrbod, F., Cerveza, P., et al. (1999) Copper transport and ceruloplasmin during lactation and pregnancy, in Metals and Genetics ( Sarkar, B., ed.), Kluwer Academic/ Plenum, New York, pp. 117–129.
Kuo, Y.-M., Gitschier, J., and Packman, S. (1997) Developmental expression of the mouse mottled and toxic milk genes suggests distinct functions for the Menkes and Wilson disease copper transporters. Hum. Mol. Genet. 6, 1043–1049.
McArdle, H. J. and Erlich, R. (1989) Copper uptake and transfer to the mouse fetus during pregnancy. J. Nutr. 121, 208–214.
McArdle, H. J. and van den Berg, G. J. (1992) The accumulation of copper by microvilli isolated from human term placenta. J. Nutr. 122, 1260–1265.
Tong, K. K. and McArdle, H. J. (1995) Copper uptake by cultured trophoblast cells isolated from human term placenta. Biochim. Biophys. Acta 1269, 233–246.
Meyer, L. A., Durley, A. P., Prohaska, J. R., and Harris, Z. L. (2001) Copper transport and metabolism are normal in aceruloplasminemia. J. Biol. Chem. 276, 36,857–36, 861.
Muramatsu, Y., Tamada, T., Moralejo, D. H., Suzuki, Y., and Matsumoto, K. (1998) Fetal copper uptake and a homolog (Atp7b) of the Wilson’s disease gene in rats. Res. Commun. Mol. Pathol. Pharmacol. 101, 225–231.
Oga, M., Matsui, N., Anai, T., Yoshimatsu, J., Inoue, I., and Miyakawa, I. (1993) Copper disposition of the fetus and placenta in a patient with untreated Wilson’s disease. Am. J. Obstet. Gynecol. 169, 196–198.
Mann, J., Camakaris, J., and Danks, D. M. (1980) Copper metabolism in mottled mouse mutants. Defective placental transfer of 64Cu to foetal brindled (Mohr) mice. Biochem. J. 186, 629–631.
Coni, E., Bocca, B., Galoppi, B., Alimonti, A., and Caroli, S. (2000) Identification of chemical species of some trace and mnor elements in mature breast milk. Microchem. J. 67, 187–194.
Wooten, L., Shulze, R. A., Lancey, R. W., Lietzow, M., and Linder, M. C. (1996) Ceruloplasmin is found in milk and amniotic fluid and may have a nutritional role. J. Nutr. Biochem. 7, 632–639.
Cerveza, P. J., Mehrbod, F., Cotton, S. J., Lomeli, N., Linder, M. C., Fonda, E. G., et al. (2000) Milk ceruloplasmin and its expression by mammary gland and liver in pigs. Arch. Bioch. Biophys. 373, 451–461.
Donley, S. A., Ilagan, B. J., Rim, H., and Linder, M. C. (2002) Copper transport to mammary gland and milk during lactation in rats, submitted.
Michalczyk, A. Rieger, J., Allen, K., Mercer, J., and Ackland, M. (2000) Defective trafficking of the Wilson disease protein ATP7B in the mammary gland of the toxic milk mouse. Biochem. J. 352, 565–571.
Rauch, H. (1983) Toxic mik, a new mutation affecting copper metabolism in the mouse. J. Heredity 74, 141–144.
Dorea, J. G. (2000) Iron and copper in human milk. Nutrition 16, 209–220.
Olivares, M., Pizarro, F., Speisky, H., Lonnerdal, B., and Uauy, R. (1998) Copper in infant nutrition: safety of World Health Organization provisional guideline value for copper content of drinking water. J. Pediat. Gastroenterol. Nutr. 26, 251–257.
Olivares, M., Araya, M., and Uauy, R. (2000) Copper homeostasis in infant nutrition: deficit and excess. J. Pediatr. Gastroenterol. 31, 102–111.
Chierici, R., Saccomandi, D., and Vigi, V. (1999) Dietary supplements for the lactating mother: influence on the trace element content of milk. Acta Paediatr. 88 (Suppl.), 7–13.
Hopkins, R. G. and Failla, M. L. (1999) Transcriptional regulation of interleukin-2 gene expression is impaired by copper deficiency in Jurkat human T lymphocytes. J. Nutr. 129, 596–601.
Percival, S. S. (1998) Copper and immunity. Am. J. Clin, Nutr. 67 (Suppl.), 1064S - 1068S.
Huang, Z. L. and Failla, M. L. (2000) Copper deficiency suppresses effector activities of differentiated U937 cells. J. Nutr. 130, 1536–1542.
Gengelbach, G. P. and Spears, J. W. (1998) Effects of dietary copper and molybdenum on copper status, cytokine production, and humoral immune response of calves. J. Dairy Sci. 81, 3286–3292.
Linder, M. C., Morris, H. P., and Criss, W. (1977) Iron and copper metabolism in cancer as exemplified by ferritin and ceruloplasmin in rats with transplantable tumors, in Morris Hepatomas: Mechanisms of Regulation ( Criss, W. ed.), Plenum, New York, pp. 643–664.
Linder, M. C., Moor, J. R., and Wright, K. (1981) Ceruloplasmin assays in diagnosis and treatment of human lung, breast and gastrointestinal cancer. J. Natl. Cancer Inst. 67, 263–275.
Gullino, P. M., Ziche, M., and Alessandri, G. (1990) Ganglioside, copper ions and angiogenic capacity of adult tissues. Cancer Metastasis Rev. 8, 239–251.
Hu, G. F. (1998) Copper stimulates proliferation of human endothelial cells under culture. J. Cell Biochem. 69, 326–335.
Soncin, F., Guitton, J. D., Cartwright, T., and Badet, J. (1997) Interaction of human angiogenin with copper modulates angiogenin binding to endothelial cells. Biochem. Biophys. Res. Commun. 236, 604–610.
Lane, T. F., Iruela-Arispe, M. L., Johnson, R. S., and Sage, E. H. (1994) SPARC is a source of copper-binding peptides that stimulate angiogenesis. J. Cell Biol. 125, 929–943.
Yoshida, D., Ikeda, Y. and Nakazawa, S. (1995) Copper chelation inhibits tumor angiogenesis in the experimental 9L gliosarcoma model. Neurosurgery 37, 287–292.
Brewer, G. J. (2001) Copper control as an antiangiogenic anticancer therapy: lessons from treating Wilson’s disease. Exp. Biol. Med. 226, 665–673.
Goode, C. A. (1991) Copper and disease, in Biochemistry of Copper ( Linder, M. C., ed.), Plenum, New York, pp. 331–366.
Mercer, J.F.B., Livingston, J., Hall, B., Paynter, J.A., Begy, C., Chandrasekharappa, S., et al. (1993) Isolation of a partial candidate gene for Menkes disease by positional cloning. Nature Genet. 3, 20–25.
Vulpe, C., Levinson, B., Whitney, S., Packman, S., and Gitschier, J. (1993) Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nature Genet. 3, 7–13.
Chelly, J., Tumer, Z., Tonnesen, T., Petterson, A., Ishikawa-Brush, Y., Tommerup, N., et al. (1993) Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein. Nature Genet. 3, 14–9.
Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J. R., and Cox, D. W. (1993) The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nature Genet. 5, 327–337.
Tanzi, R. E., Petrukhin, K., Chernov, I., Pellequer, J. L., Wasco, W., Toss, B., et al. (1993) The Wilson disease gene is a copper-transporting ATPase with homology to the Menkes disease gene. Nature Genet. 5, 344–350.
Harris, E. D., Reddy, M. C., Qian, Y., Tiffany-Castingliano, E., Majumdar, S., and Nelson, J. (1999) Multiple forms of the Menkes CuATPase. Adv. Exp. Med. Biol. 448, 39–51.
Harris, E. D., Reddy, M. C., and Majumdar, S. (2001) Evidence for two promoters in the Menkes disease gene. FASEB J. 15 [Abstract A271].
Majumdar, S., Reddy, M. C., and Harris, E. D. (2001) Indication of a nuclear copper transporter in human cells. FASEB J. 15 [Abstract A775].
Wu, J., Forbes, J. R., Chen, H. S., and Cox, D. W. (1994) The LEC rat has a deletion in the copper transporting ATPase gene homologous to the Wilson disease gene. Nature Genet. 7, 6541–6545.
Theophilos, M. B., Cox, D., and Mercer, J. F. B. (1996) The toxic milk mouse is a murine model of Wilson disease. Hum. Mol. Genet. 5, 1619–1624.
Okayasu, T., Tochimaru, H., Takahashi, T., Takekoshi, Y., Li, Y., Togashi, Y., et al. (1992) Inherited copper toxicity in Long-Evans Cinnamon rats exhibiting spontaneous hepatitis: a model of Wilson’s disease. Pediatr. Res. 31, 253–257.
Buiakova, O. I., Xu, J., Lutsenko, S., Zeitlin, S., Das, K., Das, S., et al. (1999) Null mutation of the murine ATP7B (Wilson disease) gene results in intracellular copper accumulation and late-onset hepatic nodular transformation. Hum. Mol. Genet. 9, 1665–1671.
Strausak, D., Mercer, J. F., Dieter, H. H., Stremmel, W., and Multhaup, G. (2001) Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases. Brain Res. Bull. 55, 175–185.
Mercer, J. F. (2001) The molecular basis of copper-transport diseases. Trends Mol. Med. 7, 64–69.
Cox, D. W. (1999) Disorders of copper transport. Br. Med. Bull. 55, 544–555.
Menkes, J. H. (1999) Menkes disease and Wilson disease: two sides of the same copper coin. Part I. Menkes disease. Eur. J. Paediatr. Neurol. 3, 147–158.
Menkes, J. H. (1999) Menkes disease and Wilson disease: two sides of the same copper coin. Part II. Wilson disease. Eur. J. Paediatr. Neurol. 3, 245–253.
Gitlin, J. D. (1998) Aceruloplasminemia. Pediatr. Res. 44, 271–276.
Cherry, R. A., Atwood, C. S. A., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., et al. (2001) Treatment with a copper-zinc chelator inhibits beta-amyloid accumulation in Alzheimer’s disease transgenic mice. Neuron 30, 665–676.
Suzuki, K., Miura, T. and Takeuchi, H. (2001) Inhibitory effect of copper(II) on zinc(II)-induced aggregation of amyloid beta-peptide. Biochem. Biophys. Res. Commun. 285, 991–996.
Tanner, M. S. (1999) Indian childhood cirrhosis and Tyrolean childhood cirrhosis, in Copper Transport and Its Disorders ( Leone, A. and Mercer, J. F. B., eds.), Kluwer Academic/Plenum, New York, pp. 127–137.
Lockhart, P. J. (1999) Molecular analysis of copper transport in sheep, doctoral thesis, University of Melbourne, Melbourne, Victoria, Australia.
Montaser, A., Tetreault, C., and Linder, M. C. (1992) Comparison of copper binding proteins in dog serum with those in other species. Proc. Soc. Exp. Biol. Med. 200, 321–329.
Dagenais, S. L., Guevara-Fujita, M., Loechel, R., Burgess, A. C., Miller, D. E., Yusbasiyan-Gurkan, V., et al. (1999) The canine copper toxicosis locus is not syntenic with ATP7B or ATX1 and maps to a region showing homology to human 2p21. Mamm. Genome 10, 753–756.
van der Sluis, B. J. A., Breen, M., Nanji, M., van Wolferen, M., de Jong, P., Binns, M. M., et al. (1999) Genetic mapping of the copper toxicosis locus in Bedlington terriers to dog chromosome 10, in a region syntenic to human chromosome region 2p13-p16. Hum. Mol. Genet. 8, 501–507.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media New York
About this chapter
Cite this chapter
Linder, M.C. (2002). Biochemistry and Molecular Biology of Copper in Mammals. In: Massaro, E.J. (eds) Handbook of Copper Pharmacology and Toxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-288-3_1
Download citation
DOI: https://doi.org/10.1007/978-1-59259-288-3_1
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-61737-266-7
Online ISBN: 978-1-59259-288-3
eBook Packages: Springer Book Archive