Nataliya A. Platonova

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Immunoblotting has been used to detect ceruloplasmin (Cp) polypeptides in rat mitochondria isolated from the brain, liver, testes, and mammary glands. It has been found that Cp is contained in the matrix and inner membranes of mitochondria, and that its molecular weight corresponds to the nonglycosylated form of the protein. Computer analysis has not(More)
ANNOTATION: Translation in all open reading frames (ORF) of human ceruloplasmin (Cp) pseudogene revealed the only translating sequence of 984 nucleotides. The amino acid sequence contains a signal peptide for mitochondrial protein import at N-terminus. The predicted protein without taking the signal peptide into consideration has 92% identity to the(More)
The putative product of CTR1 (SLC31A1 according to the Entrez data base) is regarded as the main candidate for an eukaryotic transmembrane copper importer. The tissue-specific function of mammalian CTR1 is still unknown. A quasi-steady-state level of the CTR1 mRNA was assayed by semiquantitative RT-PCR and compared with the copper status in rat organs(More)
24 Recent data has clearly demonstrated that CTR1, a plasma membrane protein belonging to the family of high-affinity copper importers, is involved in the transport of cisplatin, an extensively used antineoplastic drug, into cells [1]. However, it is hardly probable that the mechanism of Pt(II) binding and transport into the cell is identical to that of Cu(More)
One of the key mammalian proteins involved in carrying iron across cell membranes and transport of extracellular copper is ceruloplasmin (Cp, EC 1.16.3.1), a copper-containing glycoprotein that is synthesized predominantly in the liver and then secreted to the blood stream. In addition to this molecular form of Cp, other tissue-specific soluble Cps are(More)
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,(More)
In vivo biosynthesis of ceruloplasmin (Cp), a copper-containing glycoprotein, which plays an important role in copper transfer between organs and bidirectional iron transport in vertebrates, was studied in 7-day old rats, which are characterized by the embryonic type of copper metabolism. In addition to the liver, Cp is synthesized in the lungs, brain, and(More)
A site of rat DNA (about 1800 b. p.) adjacent to the first ceruloplasmin gene contains, apart from regulatory sequences common for all eukaryotic promotors, cis-elements, which are potential binding sites for soluble nuclear receptors of some hormones. Sequences characteristic of genes expressed in liver cells and mammary gland cells during lactation were(More)
Copper deficiency in adult rats was induced by addition of silver chloride to the feed. The concentrations of silver, copper, iron, and zinc and relative activity of genes for copper transporting proteins and copper enzymes were measured in the cortex, cerebellum, hippocampus, amygdala, pituitary gland, and hypothalamus. Silver was accumulated only in the(More)
CTR1 gene (SLC31A1 according to Entrez data base) product is the main candidate for the role of eukaryotic copper importer, whose tissue-specific function is still unclear. In this research steady state CTR1-mRNA level was measured with semiquantitative RT-PCR analysis and compared with copper status in rat organs, in which copper metabolism is changed(More)