Identification of ceruloplasmin in human liver cells by fluorescent antibodies and absence of this protein in Wilson disease

Shaposhnikov, A. M.; Zubzitski, Yu. N.; Shulman, V. S.

doi:10.1007/bf01899962

Cited by 11 publications

(3 citation statements)

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“…Our findings are at variance with a study in which fluorescein conjugated anti-caeruloplasmin revealed only small amounts of immunoreactive caeruloplasmin in frozen liver biopsies from three patients with Wilson's disease, whereas significant amounts were found in adult controls (10). These immunofluorescence findings would support the concept that caeruloplasmin synthesis is impaired.…”

Section: Discussioncontrasting

confidence: 99%

Immunocytochemical identification of caeruloplasmin in hepatocytes of patients with Wilson's disease

Epstein

Sherlock

et al. 1982

Liver

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ABSTRACT— Decreased serum caeruloplasmin levels in patients with Wilson's disease have been attributed to decreased caeruloplasmin synthesis in the hepatocyte. An immunoperoxidase procedure was used to identify caeruloplasmin in liver biopsies. The pattern of staining in biopsies from patients with Wilson's disease did not differ from the pattern seen in normal adult or neonatal liver. This indicates that immunoreactive caeruloplasmin is synthesized by the liver cell in Wilson's disease. Low serum levels of caeruloplasmin may reflect an abnormality of copper incorporation into the apoprotein or an abnormality of holocaeruloplasmin export.

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Section: Discussioncontrasting

confidence: 99%

Immunocytochemical identification of caeruloplasmin in hepatocytes of patients with Wilson's disease

Epstein

Sherlock

et al. 1982

Liver

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“…to contain apoceruloplasmin (21), raising the possibility that the formation of the holoprotein is inhibited. However other studies have shown apoceruloplasmin to be almost completely absent in patients with Wilson's disease (22).…”

Section: T-arg MMmentioning

confidence: 89%

Molecular studies of ceruloplasmin deficiency in Wilson's disease.

et al. 1987

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Deficiency of serum ceruloplasmin is a characteristic biochemical abnormality of Wilson's disease, although the mechanism of this finding is unknown. Ceruloplasmin messenger RNA (mRNA) levels were therefore examined in five patients with Wilson's disease and five controls with other types of hepatic disease. Northern and dot blot hybridizations showed that detectable ceruloplasmin mRNA was present in all of the patients with Wilson's disease, including one patient with no detectable serum ceruloplasmin. However, the ceruloplasmin mRNA levels in the Wilson's disease patients were only 33% that of controls (P < 0.001). In contrast, albumin mRNA levels in the Wilson's disease patients averaged 161% that of controls. In an attempt to better delineate the level of gene expression responsible for this decrease in ceruloplasmin mRNA, the nuclear run-on assay was used to analyze transcriptional rates. The amount of ceruloplasmin gene transcription in four Wilson's patients was decreased to 44% that of three controls. These results indicate that the diminished serum ceruloplasmin levels in patients with Wilson's disease are due at least in part to a decrease in ceruloplasmin gene transcription.

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“…Spontaneous specific fragmentation of the ceruloplasmin molecule is due to trace amounts of proteases, which seem to originate from blood plasma. 4. Limited tryptic hydrolysis of the ceruloplasmin globule resulted in the appearance of polypeptides with the same molecular weights which were observed in spontaneous fragmentation.…”

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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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Identification of ceruloplasmin in human liver cells by fluorescent antibodies and absence of this protein in Wilson disease

Cited by 11 publications

References 0 publications

Immunocytochemical identification of caeruloplasmin in hepatocytes of patients with Wilson's disease

Immunocytochemical identification of caeruloplasmin in hepatocytes of patients with Wilson's disease

Molecular studies of ceruloplasmin deficiency in Wilson's disease.

Proteolysis of Human Ceruloplasmin

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