Circulating ceruloplasmin is an important source of copper for normal and malignant animal cells

Campbell, Corinne H.; Brown, R. G.; Linder, Maria C.

doi:10.1016/0304-4165(81)90044-1

Cited by 78 publications

(39 citation statements)

References 24 publications

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“…Our results are in good agreement with those obtained by another group (Campbell et al 1981), who demonstrated the ability of CP to donate copper both to healthy and malignant rat tissues. In our case we can only speak of the CP-mediated copper transport across the placental barrier.…”

Section: Discussionsupporting

confidence: 83%

Embryotoxicity of silver ions is diminished by ceruloplasmin?further evidence for its role in the transport of copper

et al. 1995

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The effect of alimentary administration of silver salts upon embryogenesis in rats was studied. Feeding of female rats throughout the term on a regular diet supplemented with AgCl did not cause alterations of their physiological functions, despite the fact that enzymatically active copper-containing ceruloplasmin (CP) was eliminated from the blood plasma. However, developmental abnormalities of embryos, their prenatal death or the 100% mortality of the newborns in the first 24 h of life was seen. Copper content in placenta and fetal tissues was strongly diminished. Cu, Zn-superoxide dismutase (SOD) activity decreased in cytoplasm of embryonic cells along with a drop, though less pronounced, in the tissues of the pregnant females. Embryotoxicity of AgCl was seriously diminished by repetitive injections of native CP to the pregnant rats. Such treatment resulted in an increase of SOD activity in placenta and embryonic tissues. The mortality of the newborns also became less. It is suggested that the embryotoxic effect of AgCl is caused by its ability to interfere with copper metabolism, in particular by altering the copper-transporting function of CP.

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Section: Discussionsupporting

confidence: 83%

Embryotoxicity of silver ions is diminished by ceruloplasmin?further evidence for its role in the transport of copper

et al. 1995

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“…This blue, multi-copper oxidase appears to have pleotropic functions and has been referred to as a prototypic "moonlighting" protein (Bielli & Calabrese 2002), capable of oxidizing a variety of substrates -from amines to Fe(II) (Harris 2000;Linder 1991;Linder 2002); scavenging radicals (Linder 2001;Linder 2002); and delivering copper to tissues (Campbell et al 1981;Lee et al 1993), probably via specific receptors (Kataoka & Tavassoli 1985;Linder 2002;Stevens et al 1984). Its apparent role in Fe transport (attributed to its ferroxidase activity) has been of particular recent interest.…”

Section: Introductionmentioning

confidence: 99%

Copper binding components of blood plasma and organs, and their responses to influx of large doses of 65Cu, in the mouse

et al. 2008

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To establish for the first time how mice might differ from rats and humans in terms of copper transport, excretion, and copper binding proteins, plasma and organ cytosols from adult female C57CL6 mice were fractionated and analyzed by directly coupled size exclusion HPLC-ICP-MS, before and after i.p. injection of large doses of 65 Cu. Plasma from untreated mice had different proportions of Cu associated with transcuprein/macroglobulin, ceruloplasmin and albumin than in humans and rats, and two previously undetected copper peaks (Mr 700k and 15k) were observed. Cytosols had Cu peaks seen previously in rat liver (Mr >1000k, 45k and 11k) plus one of 110kDa. 65 Cu (141 μg) administered over 14h, initially loaded plasma albumin and mainly entered liver and kidney (especially 28kDa and 11kDa components). Components of other organs were less, but still significantly enriched. 63 Cu/ 65 Cu ratios returned almost to normal by 14d, indicating a robust system for excreting excess copper. We conclude that there are significant differences but also strong similarities in copper metabolism between mice, rats and humans; that the liver is able to buffer enormous changes in copper status; and that a large number of mammalian copper proteins remain to be identified.

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“…A role for ceruloplasmin in iron metabolism, mediated by its ferroxidase activity, has recently received a confirmation (Harris et al 1995). Ceruloplasmin is also involved in copper homeostasis and has repeatedly been shown to be able to exchange 67Cu with tissues (Campbell et al 1981) and copper enzymes (Dameron & Harris 1987). Studies with the human erythroleukemic K562 cell line have demonstrated that copper exchange appears to be a receptor-mediated process in which only the metal Address for correspondence: G. Musci, c/o Department of Biochemical Sciences, University of Rome 'La Sapienza', P. le Aldo Moro 5, 00185 Rome, Italy.…”

Section: Introductionmentioning

confidence: 99%

Divalent cation binding to ceruloplasmin

Musci

Petruzzelli

et al. 1996

Biometals

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Binding of calcium to human and sheep ceruloplasmin was investigated by metal substitution with manganese and competitive displacement of bound manganese by calcium monitored by electron paramagnetic resonance spectroscopy. The Kd for calcium was found to be 1.4 mM. Magnesium also bound to ceruloplasmin, with Kd = 0.3 and 0.7 mM for the human and sheep protein, respectively. The thermal stability of ceruloplasmin, as studied by differential scanning calorimetry, was affected by calcium but not by magnesium. A considerable increase of the Tm value, from 73.8 to 83.1 degrees C, was observed for sheep ceruloplasmin in the presence of calcium. The Tm value of the human protein was only slightly altered by calcium (from 85.1 to 87 degrees C). The interaction of ceruloplasmin with the chromatographic material used for its isolation, Sepharose 4B derivatized with chloroethylamine, was weakened by calcium. This allowed us to set up a novel purification scheme that made it possible to efficiently isolate ceruloplasmin and prothrombin from plasma with the same single-step chromatography.

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Circulating ceruloplasmin is an important source of copper for normal and malignant animal cells

Cited by 78 publications

References 24 publications

Embryotoxicity of silver ions is diminished by ceruloplasmin?further evidence for its role in the transport of copper

Embryotoxicity of silver ions is diminished by ceruloplasmin?further evidence for its role in the transport of copper

Copper binding components of blood plasma and organs, and their responses to influx of large doses of 65Cu, in the mouse

Divalent cation binding to ceruloplasmin

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