Localization of ceruloplasmin biosynthesis in human and monkey liver cells and its copper regulation

Neifakh, S. A.; Monakhov, N. K.; Shaposhnikov, A. M.; Zubzhitski, Yu. N.

doi:10.1007/bf01899902

Cited by 34 publications

(7 citation statements)

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“…Ceruloplasmin (CP)* is the main copper-binding plasma protein that is synthesized in liver parenchymatous cells (1). The changes in its structure and insufficiency of its synthesis are phenotypic manifestations of Wilson mutation (hepatolenticular degeneration) in man (2,3).…”

Section: Introductionmentioning

confidence: 99%

Preproceruloplasmin is a primary product of cell-free translation of ceruloplasmin messenger RNA

et al. 1981

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Biosynthesis of ceruloplasmin was studied in wheat germ extract programmed with polysomal RNA from rat liver. Optimal potassium concentration for the total protein-synthesizing activity and for the synthesis of immunoreactive ceruloplasmin was 96 and 186 mM respectively. 7-methylguanosine 5'-monophosphate caused two-fold inhibition of the cell-free synthesis of ceruloplasmin. Immunoprecipitated ceruloplasmin that was synthesized at optimal potassium concentration was a homogeneous polypeptide of a molecular weight about 84 kD. The addition of membrane fractions from rat liver to the incubation mixture caused the conversion of the 84 kD polypeptide into 80 kD and 65 kD polypeptides that are similar to proceruloplasmins synthesized in rat liver during in vivo pulse labelling. The suggestion is made that 84 kD polypeptide is a primary product of the translation of ceruloplasmin mRNA (preproceruloplasmin).

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Section: Introductionmentioning

confidence: 99%

Preproceruloplasmin is a primary product of cell-free translation of ceruloplasmin messenger RNA

et al. 1981

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“…The isoforms are coded by two molecular variants of Cp-mRNA, which are formed by alternative splicing of Cp gene transcript. sCp is synthesized by the cells of organs that produce extracellular fluids: the liver [ 127 ], mammary gland [ 128 ], and choroid plexus [ 129 , 130 ]. GPI-Cp is synthesized in Sertoli cells [ 131 ], glial cells of various brain regions [ 129 , 132 , 133 ], peripheral blood lymphocytes and macrophages, and hepatocytes [ 134 ].…”

Section: The Points In Which Iav-induced Inflammation Cross With Copper Metabolismmentioning

confidence: 99%

The Crossroads between Host Copper Metabolism and Influenza Infection

Puchkova

Kiseleva

Polishchuk

et al. 2021

IJMS

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Three main approaches are used to combat severe viral respiratory infections. The first is preemptive vaccination that blocks infection. Weakened or dead viral particles, as well as genetic constructs carrying viral proteins or information about them, are used as an antigen. However, the viral genome is very evolutionary labile and changes continuously. Second, chemical agents are used during infection and inhibit the function of a number of viral proteins. However, these drugs lose their effectiveness because the virus can rapidly acquire resistance to them. The third is the search for points in the host metabolism the effect on which would suppress the replication of the virus but would not have a significant effect on the metabolism of the host. Here, we consider the possibility of using the copper metabolic system as a target to reduce the severity of influenza infection. This is facilitated by the fact that, in mammals, copper status can be rapidly reduced by silver nanoparticles and restored after their cancellation.

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“…The liver appears to be the main site of synthesis and secretion of caeruloplasmin [8]. Recent evidence suggests that the major 135 000Mr form of caeruloplasmin peptide is also synthesized by rat sertoli cells [9,10] and alveolar macrophages [11], rat mammary glands [12], mouse embryonic fibroblasts transformed by the Rous-sarcoma virus [13], human synovial tissue [14] and in human lung (Hs242T) and breast (MCF-7) adenocarcinoma cell lines [12].…”

Section: Introductionmentioning

confidence: 99%

Caeruloplasmin biosynthesis by the human uterus

Schilsky

Stockert

Pollard

1992

Biochemical Journal

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The blue copper protein caeruloplasmin is synthesized mainly by hepatocytes. An alternative transcript for caeruloplasmin produced in certain extrahepatic tissues, CP-1, contains an additional 12 nucleotides encoding 4 amino acids not present in the hepatic transcript, CP-2 [Yang, Friedrichs, Cupples, Bonifacio, S Sanford, Horton & Bowman (1990) J. Biol. Chem. 265, 10780-10785]. We have demonstrated transcription of caeruloplasmin mRNA by a well-differentiated human uterine epithelial adenocarcinoma cell line, Ishikawa, and by human uterine endometrium and purified endometrial glands. Identical CP-2 nucleotide sequences were obtained for partial caeruloplasmin transcripts from human liver and Ishikawa cells, indicating that CP-2 transcripts are produced by uterine epithelial lining cells. The synthesis of caeruloplasmin protein was demonstrated for Ishikawa cells and another uterine adenocarcinoma cell line, ECC1. Peptide-mapping analysis indicated that caeruloplasmin secreted by Ishikawa cells was structurally identical with the protein synthesized by the human hepatoblastoma cell line HepG2. The secretion of a 135,000-M(r) caeruloplasmin by Ishikawa and ECC1 cells, comparable with that of the human hepatoblastoma cell line, HepG2, indicated similar processing of uterine and hepatic caeruloplasmin. Incorporation of 67Cu into caeruloplasmin was demonstrated for Ishikawa and ECC1 cells, suggesting that the human uterus produces a bioactive form of caeruloplasmin and possesses the necessary metal transporters and intracellular machinery for copper incorporation into this protein.

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Localization of ceruloplasmin biosynthesis in human and monkey liver cells and its copper regulation

Cited by 34 publications

References 0 publications

Preproceruloplasmin is a primary product of cell-free translation of ceruloplasmin messenger RNA

Preproceruloplasmin is a primary product of cell-free translation of ceruloplasmin messenger RNA

The Crossroads between Host Copper Metabolism and Influenza Infection

Caeruloplasmin biosynthesis by the human uterus

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