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Changes in functional ceruloplasmin concentrations of plasma and exudate and the effect of exogenous ceruloplasmin on the carrageenin-induced inflammation in rats.

Changes in functional ceruloplasmin (Cp) concentrations of plasma and exudate during acute and chronic inflammatory processes were studied in detail by measuring Cp oxidase activity in the carrageenin-induced inflammation in rats. In contrast with the plasma functional Cp level as an acute-phase reactant, the exudate functional Cp level was very low during the acute phase, increased in the chronic phase and reached a constant value which was only half value of the plasma functional Cp level. The locally injected Cp had no effect on the carrageenin-induced inflammation, suggesting that exogenous Cp has no anti-inflammatory effect on the inflamed rats eating normal diet.

Animals↗

Molecular forms of ceruloplasmin in hepatolenticular degeneration and their interaction with human erythrocyte ceruloplasmin receptor.

Immunochemical methods were used to show that the sera of homozygous and heterozygous carriers of the Wilsonian gene contain, together with normal ceruloplasmin (CP), a CP-like protein that differs from CP in its enzymatic, immunological, and physicochemical properties. The CP-like protein was isolated from the sera of patients with hepatolenticular degeneration (HLD) by means of affinity chromatography, and monospecific antibodies to this protein were obtained. The presence of an 80 kDa immunoreactive polypeptide specific to the CP-like protein was demonstrated by immunoblotting with antibodies to normal CP and monospecific antibodies to the CP-like protein. Analysis of the ratios of the molecular forms of CP in homozygous and heterozygous carriers of the Wilsonian gene indicated that this ratio reflects the dosage of the mutant gene. The kinetic parameters of the interaction of these proteins with the CP-specific receptor on the erythrocyte membranes from healthy individuals and from patients with Wilson's disease (HLD) were determined. The CP receptor on erythrocyte membranes in HLD patients is not altered and its interaction with normal CP has the same kinetic parameters as the binding of normal CP to the erythrocyte receptors from healthy individuals. The CP-like protein also retains the ability to bind to the CP-specific receptor but the ligand-receptor complex is less stable than in the case of normal CP. The possible mechanism of the molecular heterogeneity of CP in the Wilsonian mutation is discussed.

Ceruloplasmin↗

Interaction between ceruloplasmin and Sendai virus envolpe components. Note IV. Effect of ceruloplasmin on the hemagglutinin and neuraminidase activities of Tween 20-solubilized envelope components separated by adsorption--elution on RBC.

Ceruloplasmin inhibits the hemagglutinin (HA) and neuraminidase (N-ase) activities of envelope fragment populations isolated from Sendai virus disrupted by alkali--Tween 20 treatment. The inhibition induced differs according to adsorption--elution characteristics, value and ratio of HA and N-ase activities and sterical configuration of the envelope fragments.

Ceruloplasmin↗

[Characteristics of ceruloplasmin synthesis in mammalian embryogenesis. 2. The yolk sac as the site of the primary expression of the ceruloplasmin gene in rats].

It was shown that the omphaloid placenta and, first of all, visceral wall of yolk sac is the site of primary synthesis of ceruloplasmin (CP), whereas the activation of CP synthesis in the liver cells is secondary and is revealed from the 12th day of embryo-genesis. The CP synthesis in the yolk sac cells proved by selective CP localization in the cells of the yolk sac visceral wall and, first of all, in the cells of visceral endoderm on sections stained by the method of indirect immunofluorescence and using the reaction of soluble peroxidase-antiperoxidase complex. A specific CP-mRNA has been revealed in the yolk sac cells which is actively translated in the polyribosomes isolated from the yolk sac and in the cell-free translation system from the rabbit reticulocytes. on the 14th day of embryogenesis CP amounts to ca. 4% of all polypeptides secreted by the yolk sac cells. As the embryogenesis proceeds, the relative rate of CP synthesis progressively decreases in the yolk sac and increases in the liver cells. CP synthesized by the yolk sac cells has a molecular mass of ca. 122 kD. Possible causes of differences between the "embryonic" and "adult" rat CPs are discussed. A suggestion has been put forward that the time of activation of CP synthesis coincides with the yolk sac formation (8-9th days of embryogenesis) and the cells of visceral endoderm are the site of primary expression of the CP gene.

Animals↗

[Study of physiological functions of human ceruloplasmin. The effect of ceruloplasmin on immunocytes in a normal state and in pathology].

The immunomodulating effect of ceruloplasmin (CP) on the major components of the immunocompetent system of the organism--the natural resistance system and the specific immune response--has been established. CP can exert various influences on the level of expression of specific markers of T- and B-lymphocytes (as determined by various modifications of the rosette-forming test), on the phagocytic activity of neutrophils and monocytes as well as on the activity of "respiratory burst" enzymes. CP modulation was found to depend predominantly on the initial level of the immunological parameters to be determined, i. e., on the extent of immune inflammation in human patients. Thus, it was found that CP not only plays the roles of an antioxidant and a copper-transporting protein, but is also capable to interact with immunocytes, altering their biological activities. The observed immunotropicity of CP, its ability to directly interact with immunocytes and to model the immune function at the cell level provides evidence for the existence of a universal molecular language of information exchange between the macroorganism cells of various nature and origin.

Adolescent↗