scholarly journals Appearance of the imprinting effect on the specific pattern of intracellular distribution of copper ions in the liver after exposure to high concentrations of copper sulfate

2010 ◽  
Vol 56 (2) ◽  
pp. 195-208 ◽  
Author(s):  
A.I. Bozhkov ◽  
V.I. Sidorov ◽  
V.L. Dlubovskaya ◽  
M.Ya. Shevtsova ◽  
Yu.N. Surov
Keyword(s):  
Rat Liver ◽  
Copper Sulfate ◽  
Liver Cell ◽  
Copper Ions ◽  
Specific Pattern ◽  
Intracellular Distribution ◽  
The Body ◽  
Copper Binding ◽  
Copper Binding Protein ◽  
High Concentrations

Fractions of copper-binding protein (CBP) specifically bound copper ions were extracted from the rat liver cell cytosole. These fractions of 10-14 kDa proteins are involved in specific pattern of intracellular distribution of copper ions. The imprinting effect of specific pattern of copper ions intracellular distribution has been found. The effect was detected 30 days after sequented injections of copper sulfate into the body. It was shown, that after primary injection of copper the ability of CBP to bind copper ions could increase tenfold, regardless of schemes of copper sulfate injection.

scholarly journals Hyaluronate/black phosphorus complexes as a copper chelating agent for Wilson disease treatment

2021 ◽  
Vol 25 (1) ◽  
Author(s):  
Seong-Jong Kim ◽  
Hye Hyeon Han ◽  
Sei Kwang Hahn
Keyword(s):  
Targeted Delivery ◽  
Wilson Disease ◽  
Copper Ions ◽  
Binding Capacity ◽  
Genetic Disorder ◽  
Chelating Agent ◽  
Black Phosphorus ◽  
The Body ◽  
Copper Binding

Abstract Background Wilson disease (WD) is a genetic disorder of copper storage, resulting in pathological accumulation of copper in the body. Because symptoms are generally related to the liver, chelating agents capable of capturing excess copper ions after targeted delivery to the liver are highly required for the treatment of WD. Methods We developed hyaluronate-diaminohexane/black phosphorus (HA-DAH/BP) complexes for capturing copper ions accumulated in the liver for the treatment of WD. Results HA-DAH/BP complexes showed high hepatocyte-specific targeting efficiency, selective copper capturing capacity, excellent biocompatibility, and biodegradability. HA enhanced the stability of BP nanosheets and increased copper binding capacity. In vitro cellular uptake and competitive binding tests verified targeted delivery of HA-DAH/BP complexes to liver cells via HA receptor mediated endocytosis. The cell viability test confirmed the high biocompatibility of HA-DAH/BP complexes. Conclusion HA-DAH/BP complexes would be an efficient copper chelating agent to remove accumulated copper in the liver for the WD treatment.

scholarly journals Silver Ions as a Tool for Understanding Different Aspects of Copper Metabolism

Nutrients ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 1364 ◽  
Author(s):  
Ludmila V. Puchkova ◽  
Massimo Broggini ◽  
Elena V. Polishchuk ◽  
Ekaterina Y. Ilyechova ◽  
Roman S. Polishchuk
Keyword(s):  
Active Sites ◽  
Large Scale ◽  
Copper Ions ◽  
Copper Metabolism ◽  
Silver Ions ◽  
The Body ◽  
Copper Binding ◽  
Safe Delivery ◽  
Protein Motifs ◽  
Wide Range

In humans, copper is an important micronutrient because it is a cofactor of ubiquitous and brain-specific cuproenzymes, as well as a secondary messenger. Failure of the mechanisms supporting copper balance leads to the development of neurodegenerative, oncological, and other severe disorders, whose treatment requires a detailed understanding of copper metabolism. In the body, bioavailable copper exists in two stable oxidation states, Cu(I) and Cu(II), both of which are highly toxic. The toxicity of copper ions is usually overcome by coordinating them with a wide range of ligands. These include the active cuproenzyme centers, copper-binding protein motifs to ensure the safe delivery of copper to its physiological location, and participants in the Cu(I) ↔ Cu(II) redox cycle, in which cellular copper is stored. The use of modern experimental approaches has allowed the overall picture of copper turnover in the cells and the organism to be clarified. However, many aspects of this process remain poorly understood. Some of them can be found out using abiogenic silver ions (Ag(I)), which are isoelectronic to Cu(I). This review covers the physicochemical principles of the ability of Ag(I) to substitute for copper ions in transport proteins and cuproenzyme active sites, the effectiveness of using Ag(I) to study copper routes in the cells and the body, and the limitations associated with Ag(I) remaining stable in only one oxidation state. The use of Ag(I) to restrict copper transport to tumors and the consequences of large-scale use of silver nanoparticles for human health are also discussed.

scholarly journals Hyaluronate – Black Phosphorus Conjugates as a Copper Chelating Agent for Wilson Disease Treatment

2021 ◽  
Author(s):  
Seong-Jong Kim ◽  
Hye Hyeon Han ◽  
Sei Kwang Hahn
Keyword(s):  
Targeted Delivery ◽  
Wilson Disease ◽  
Copper Ions ◽  
Binding Capacity ◽  
Genetic Disorder ◽  
Chelating Agent ◽  
Black Phosphorus ◽  
The Body ◽  
Copper Binding

Abstract Background: Wilson disease (WD) is a genetic disorder of copper storage, resulting in pathological accumulation of copper in the body. Because symptoms are generally related to the liver, chelating agents capable of capturing excess copper ions after targeted delivery to the liver are highly required for the treatment of WD. Methods: We developed hyaluronate - black phosphorus (HA-BP) conjugates for capturing copper ions accumulated in the liver for the treatment of WD.Results: HA-BP conjugates showed high hepatocyte-specific targeting efficiency, selective copper capturing capacity, excellent biocompatibility, and biodegradability. HA enhanced the stability of BP nanosheets and increased copper binding capacity. In vitro cellular uptake and competitive binding tests verified targeted delivery of HA-BP conjugates to liver cells via HA receptor mediated endocytosis. The cell viability test confirmed the high biocompatibility of HA-BP conjugates.Conclusion: HA-BP conjugates would be an efficient copper chelating agent to remove accumulated copper in the liver for the WD treatment.

Copper-chelatin: Purification and properties of a copper-binding protein from rat liver

1975 ◽  
Vol 170 ◽  
pp. 253-266 ◽  
Author(s):  
Dennis R. Winge ◽  
R. Premakumar ◽  
Ralph D. Wiley ◽  
K.V. Rajagopalan
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Copper Binding ◽  
Purification And Properties ◽  
Copper Binding Protein

Structure of the periplasmic copper-binding protein CueP fromSalmonella entericaserovar Typhimurium

2013 ◽  
Vol 69 (10) ◽  
pp. 1867-1875 ◽  
Author(s):  
Bo-Young Yoon ◽  
Yong-Hak Kim ◽  
Nahee Kim ◽  
Bo-Young Yun ◽  
Jin-Sik Kim ◽  
...  
Keyword(s):  
Copper Ions ◽  
Binding Protein ◽  
Copper Resistance ◽  
Structural Basis ◽  
Copper Binding ◽  
Rich Cluster ◽  
Copper And Zinc ◽  
Serovar Typhimurium ◽  
Copper Resistance Gene ◽  
Copper Binding Protein

CueP was initially identified as a copper-resistance gene inSalmonella entericaserovar Typhimurium, which has evolved to survive in the phagosomes of macrophages. Recently, CueP was determined to be a periplasmic copper-binding protein and has been implicated in the transfer of copper ions to SodCII in the periplasm. In this study, the crystal structure of CueP has been determined, revealing a V-shaped dimeric structure. The conserved cysteine and histidine residues are clustered on the surface of one side of the C-terminal domain, suggesting that this cysteine- and histidine-rich region is related to the function of CueP. LC-MS/MS analysis established the presence of a disulfide bond between Cys96 and Cys176 under aerobic conditions. Subsequent biophysical analyses showed that the CueP protein binds copper and zinc, and the mutation of Cys104 to serine (C104S) dramatically reduced the binding affinity for copper and zinc, suggesting that the cysteine- and histidine-rich cluster is responsible for copper binding. This study provides a structural basis for the participation of CueP in the resistance of the intracellular pathogenSalmonellato copper.

scholarly journals Copper and copper-binding protein in fibrolamellar liver cell carcinoma

Cancer ◽  
1983 ◽  
Vol 51 (1) ◽  
pp. 97-100 ◽  
Author(s):  
Jay H. Lefkowitch ◽  
Ruth Muschel ◽  
John B. Price ◽  
Charles Marboe ◽  
Susan Braunhut
Keyword(s):  
Cell Carcinoma ◽  
Liver Cell ◽  
Binding Protein ◽  
Copper Binding ◽  
Liver Cell Carcinoma ◽  
Copper Binding Protein

Effects of Hypophysectomy on the Fine Structure of Rat Liver Cells

1967 ◽  
Vol 25 ◽  
pp. 156-157
Author(s):  
Robert R. Cardell
Keyword(s):  
Electron Microscopy ◽  
Fine Structure ◽  
Rat Liver ◽  
Liver Cell ◽  
Anterior Pituitary ◽  
Liver Cells ◽  
Biochemical Studies ◽  
Liver Functions ◽  
Rat Liver Cells ◽  
And Control

Hypophysectomy of the rat renders this animal deficient in the hormones of the anterior pituitary gland, thus causing many primary and secondary hormonal effects on basic liver functions. Biochemical studies of these alterations in the rat liver cell are quite extensive; however, relatively few morphological observations on such cells have been recorded. Because the available biochemical information was derived mostly from disrupted and fractionated liver cells, it seemed desirable to examine the problem with the techniques of electron microscopy in order to see what changes are apparent in the intact liver cell after hypophysectomy. Accordingly, liver cells from rats which had been hypophysectomized 5-120 days before sacrifice were studied. Sham-operated rats served as controls and both hypophysectomized and control rats were fasted 15 hours before sacrifice.

BIOSYNTHESE DE LA TRANSCORTINE

1969 ◽  
Vol 62 (3) ◽  
pp. 468-476 ◽  
Author(s):  
Jeanine Guidollet ◽  
Pierre Louisot
Keyword(s):  
Biological Activity ◽  
Rat Liver ◽  
Liver Cell ◽  
Binding Activity ◽  
Subcellular Level

ABSTRACT Corticosteroid-binding activity (transcortin) was investigated at the subcellular level of the rat liver cell: it was located exclusively in the cell sap, and not on the ribosomes or membranes. Oestrogens were found to increase the biological activity of this glycoprotein (corticosterone binding) in the plasma and in the cell sap. The isotopic activity of the glucidic fragments of glycoprotein (after incorporation of 14C-D-glucosamine), however, remained constant or decreased in the specific subcellular sites at which they were incorporated (membranes and cell sap). This absence of correlation between these two results is not in agreement with an induction of transcortin synthesis by oestrogens, but in favour of an activation of normally masked molecular sites.

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