Isolation and partial characterization of molecular forms of ceruloplasmin from human bile

Verbina, I A; Puchkova, L. V.; Gaitskhoki, V. S.; Neifakh, S. A.

doi:10.1016/0014-5793(92)80032-c

Cited by 20 publications

(7 citation statements)

References 6 publications

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“…It is also reported that normal human bile contains two molecular forms of ceruloplasmin. One is identical to the serum ceruloplasmin, and the other is similar to the ceruloplasmin without oxidase activity detected in patients with Wilson's disease (35).…”

Section: Biliur! Copper ~~C R C T I O T~supporting

confidence: 55%

Impaired Hepatic Copper Homeostasis in Long-Evans Cinnamon Rats: Reduced Biliary Excretion of Copper

Suzuki

Aoki

1994

Pediatr Res

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Section: Biliur! Copper ~~C R C T I O T~supporting

confidence: 55%

Impaired Hepatic Copper Homeostasis in Long-Evans Cinnamon Rats: Reduced Biliary Excretion of Copper

Suzuki

Aoki

1994

Pediatr Res

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“…In addition, both Cu-ATPases are possibly involved in efflux/influx of copper ions by the cell (Cox and Moore, 2002;Qian et al ., 1997), using for this purpose Cp secreted by cells (Gaitskhoki et al, 1990;Verbina et al, 1992). The choice of the listed brain regions, which can be easily identified anatomically, allowed us to compare the activity of CMS in neurosecretory cells (pituitary and hypothalamus), ependyma (choroid plexus), and different types of neurons (brain cortex, cerebellum, amygdala, and hippocampus).…”

Section: Methodsmentioning

confidence: 99%

In vivo expression of copper-transporting proteins in rat brain regions

Platonova

Barabanova

Povalikhin

et al. 2005

Biol Bull Russ Acad Sci

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Expression of two copper-transporting P1-type ATPases (ATP7A and ATP7B), the CTR1 protein, a high-affinity copper transporter, and ceruloplasmin (Cp), a copper-containing ferroxidase was studied. The level of mRNA of these proteins was determined by RT-PCR analysis, the distribution of polypeptides encoded by these genes was determined by immunoblotting, and the type of cells expressing these genes was identified immunohistochemically. It was found that the major product of Cp gene in the brain is the cell membranebound Cp. Secretory Cp, whose molecule contains the greatest number of weakly associated copper atoms, is synthesized in the choroid plexus. CTR1 mRNA is evenly distributed in the brain; however, its content is twice higher in the vascular plexus. The Atp7a gene is active in all brain regions, whereas the Atp7b gene is active only in the hypothalamus. The membrane-bound Cp is expressed in glial cells of all types and in ependyma cells. ATP7B and ATP7A are expressed predominantly in ependymyocytes and neurons, respectively. The organization of copper transport in mammalian brain is discussed.

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“…This polypeptide was tentatively assigned by predominance and molecular mass to a subunit of α-2-macroglobulin (α2MG) 60 that can bind both copper and silver. 61…”

Section: Interaction Of Agnps With Cp and Other Serum Proteins In Vitromentioning

confidence: 99%

Size-Dependent Bioactivity of Silver Nanoparticles: Antibacterial Properties, Influence on Copper Status in Mice, and Whole-Body Turnover

Skomorokhova¹,

Sankova²,

Orlov³

et al. 2020

NSA

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The ability of silver nanoparticles (AgNPs) of different sizes to influence copper metabolism in mice is assessed. Materials and Methods: AgNPs with diameters of 10, 20, and 75 nm were fabricated through a chemical reduction of silver nitrate and characterized by UV/Vis spectrometry, transmission and scanning electronic microscopy, and laser diffractometry. To test their bioactivity, Escherichia coli cells, cultured A549 cells, and C57Bl/6 mice were used. The antibacterial activity of AgNPs was determined by inhibition of colony-forming ability, and cytotoxicity was tested using the MTT test (viability, %). Ceruloplasmin (Cp, the major mammalian extracellular copper-containing protein) concentration and enzymatic activity were measured using gel-assay analyses and WB, respectively. In vitro binding of AgNPs with serum proteins was monitored with UV/Vis spectroscopy. Metal concentrations were measured using atomic absorption spectrometry. Results: The smallest AgNPs displayed the largest dose-and time-dependent antibacterial activity. All nanoparticles inhibited the metabolic activity of A549 cells in accordance with dose and time, but no correlation between cytotoxicity and nanoparticle size was found. Nanosilver was not uniformly distributed through the body of mice intraperitoneally treated with low AgNP concentrations. It was predominantly accumulated in liver. There, nanosilver was included in ceruloplasmin, and Ag-ceruloplasmin with low oxidase activity level was formed. Larger nanoparticles more effectively interfered with the copper metabolism of mice. Large AgNPs quickly induced a drop of blood serum oxidase activity to practically zero, but after cancellation of AgNP treatment, the activity was rapidly restored. A major fraction of the nanosilver was excreted in the bile with Cp. Nanosilver was bound by alpha-2-macroglobulin in vitro and in vivo, but silver did not substitute for the copper atoms of Cp in vitro. Conclusion:The data showed that even at low concentrations, AgNPs influence murine copper metabolism in size-dependent manner. This property negatively correlated with the antibacterial activity of AgNPs.

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Isolation and partial characterization of molecular forms of ceruloplasmin from human bile

Cited by 20 publications

References 6 publications

Impaired Hepatic Copper Homeostasis in Long-Evans Cinnamon Rats: Reduced Biliary Excretion of Copper

Impaired Hepatic Copper Homeostasis in Long-Evans Cinnamon Rats: Reduced Biliary Excretion of Copper

In vivo expression of copper-transporting proteins in rat brain regions

Size-Dependent Bioactivity of Silver Nanoparticles: Antibacterial Properties, Influence on Copper Status in Mice, and Whole-Body Turnover

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