Molecular pathology of ceruloplasmin

Neifakh, S. A.; Vasiletz, I. M.; Shavlovsky, M. M.

doi:10.1007/bf00486406

Cited by 20 publications

(9 citation statements)

References 13 publications

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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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Section: Introductionmentioning

confidence: 98%

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

et al. 1981

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“…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%

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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“…Our interest in the research on ceruloplasmin is primarily due to the fact that the alteration in its structure [2] and biosynthesis [3 -51 might be related to a severe hereditary disease in man: the hepatolenticular degeneration (Wilson-Konovalov's disease) [6]. The data on the number and size of polypeptide chains appearing during the dissociation of human ceruloplasmin are rather contradictory.…”

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confidence: 99%

Proteolysis of Human Ceruloplasmin

Moshkov¹,

Lakatos

Hajdu

et al. 1979

European Journal of Biochemistry

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Highly purified human ceruloplasmin was isolated from fresh donor blood in the presence of inhibitors of proteolysis and from stored retroplacental blood serum both with and without inhibitors of proteolysis. According to the data of electrophoresis. ultracentrifuge sedimentation velocity and sedimentation equilibrium, all the ceruloplasmin samples were homogeneous, their molecular weight being 130 000. The dissociation of the samples treated by dodecylsulphate, guanidine · HCl, and urea was studied by means of quantitative analytica and preparative electrophoresis, and sedimentation equilibrium. The dissociation patterns depended on whether inhibitors were used in the isolation procedure. Polypeptides with molecular weights of 130 000, 112 000 and 16 000 (minor component) were obtained, if phenylmethylsulfonyl fluoride and/or 6‐aminohexanoic acid were used; if these compounds were not used, the dissociation yielded additional polypeptides of molecular weights of 100 000 (minor component), 64 000 and 48 000. Under proteolysis‐favouring conditions the relative amount of these polypeptides increased. Prolonged storage of samples under sterile conditions without inhibitors of proteolysis resulted in a decrease of the relative amount of polypeptides with molecular weights of 130 000, 112 000, 100 000, 64 000 and 48 000, contrary to that of the 16 000‐Mr polypeptide, which increased. At the same time new polypeptides appeared with molecular weights of 42 000 and 21 500–23 000. Spontaneous specific fragmentation of the ceruloplasmin molecule is due to trace amounts of proteases, which seem to originate from blood plasma. Limited tryptic hydrolysis of the ceruloplasmin globule resulted in the appearance of polypeptides with the same molecular weights which were observed in spontaneous fragmentation. A conclusion is drawn that the ceruloplasmin molecule in vivo is a single polypeptide chain with at least five bonds which in vitro are the points of specific proteolytic fragmentation, yielding six principal fragments.

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Molecular pathology of ceruloplasmin

Cited by 20 publications

References 13 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

Highly purified ceruloplasmin messenger RNA from rat liver

Proteolysis of Human Ceruloplasmin

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