On the defect of synthesis ceruloplasmin in the liver polyribosomes in Wilson's disease

Gaitskhoki, V. S.; Kisselev, O.I.; Moshkov, K. A.; Puchkova, L. V.; Shavlovski, Mikhail M.; Shulman, V. S.; Vacharlovski, V. G.; Neifakh, S. A.

doi:10.1007/bf00484913

Cited by 14 publications

(4 citation statements)

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“…[3H]-Borohydride reduction of end groups in RNA was carried out essentially according to Cory et al (10) with minor modifications. A sample of a total volume 30 #1, containing 10 #g RNA in 10 mM EDTA, pH 8.0, was heated in a siliconized capillary tube at 65 ~ for 5 rain and then oxidized with 9 #1 of freshly prepared 2.5 mM sodium periodate.…”

Section: End-group Analysismentioning

confidence: 99%

“…The special interest in the mechanisms of CP biosynthesis and control of this process is related to the fact that Wilson disease (hepatolenticular degeneration), a severe human autosomal-recessive disease is associated with both structural anomalies of CP (9) and quantitative defects in its synthesis by liver polyribosomes (10). Further analysis of the possible molecular mechanisms underlying the inherited defects of CP synthesis is to be based on the knowledge of normal pathways of synthesis, maturation and secretion of this protein, Information of that kind as well as the data on the control of the expression of CP gene in normal hepatocytes are evidently insufficient.…”

Section: Introductionmentioning

confidence: 99%

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Highly purified ceruloplasmin messenger RNA from rat liver

et al. 1981

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Highly purified ceruloplasmin mRNA was isolated from rat liver polyribosomes. The molecular weight of ceruloplasmin mRNA is in a range from 1.05 to 1.25 . 10(6) daltons which is large enough to code for a putative precursor of ceruloplasmin (approximately 700 amino acid acids). Ceruloplasmin mRNA contains 3'-terminal poly(A) the length of which varies from 38 to 165 nucleotides. The 5'-end of ceruloplasmin mRNA is blocked with confronting m7G residue which is a component of cap I (m7G5'ppp5'XmpAp). The addition of ceruloplasmin mRNA to wheat-germ cell free system programmed the synthesis of a product that was largely precipitated by anti-ceruloplasmin immunoglobulins. The translation product was homogeneous in polyacrylamide gel-sodium dodecylsulfate electrophoresis. Cell-free translation of ceruloplasmin mRNA was sensitive to inhibition by cap analogue.

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Section: End-group Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Highly purified ceruloplasmin messenger RNA from rat liver

et al. 1981

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“…The changes in its structure and insufficiency of its synthesis are phenotypic manifestations of Wilson mutation (hepatolenticular degeneration) in man (2,3). However the molecular mechanisms underlying the deficiency in the synthesis, maturation and secretion of CP in the homozygous carrier of this mutation remain unclear.…”

Section: Introductionmentioning

confidence: 98%

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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“…However, with respect to coeruloplasmin as a protein with peculiar copper transfer functions [4] these problems remain to be studied. The interest in the synthesis and secretion of coeruloplasmin is evoked by the fact that selective insufficiency of the synthesis of this protein is a characteristic feature of hepatolenticular degeneration, or Wilson disease, a serious human hereditary disease [1,5]. Of significant interest would be the identification of the primary mutation-induced defect of coeruloplasmin synthesis in various forms of this disease, which is known as a genetically heterogeneous trait.…”

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confidence: 99%

Intracellular Distribution of Rat-Liver Polyribosomes Synthesizing Coeruloplasmin

Gaitskhoki¹,

L'vov²,

Monakhov³

et al. 2005

European Journal of Biochemistry

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Three independent approaches (binding of 12'I-antibodies to polysomes, cell-free translation of polyadenylated mRNA in a wheat germ system and hybridization of RNA with a specific complementary DNA probe) were used to study the intracellular distribution of polysomes involved in the synthesis of coeruloplasmin as well as of coeruloplasmin mRNA sequences in rat liver. It was shown that only membrane-bound polyomes contain both nascent chains of coeruloplasmin and coeruloplasmin mRNA sequences. The size of coeruloplasmin polysomes is 16-18 monomers/mRNA molecule and their proportion is about 0.4-0.6y/, of total liver polysomes. The proportion of coeruloplasmin mRNA is 0.0025 of the total polysomal RNA and 0.29 x of poly(A)-containing mRNA. These values correspond to coeruloplasmin mRNA concentration about 400-535 molecules per parenchymatous liver cell, 90 % of those mRNA molecules were recovered from polysomes while the remaining 10 x were from postpolysomal supernatant.

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On the defect of synthesis ceruloplasmin in the liver polyribosomes in Wilson's disease

Cited by 14 publications

References 14 publications

Highly purified ceruloplasmin messenger RNA from rat liver

Highly purified ceruloplasmin messenger RNA from rat liver

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

Intracellular Distribution of Rat-Liver Polyribosomes Synthesizing Coeruloplasmin

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