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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The value of serum ferritin and mean corpuscular volume (MCV) measurement in distinguishing between iron deficient, beta-thalassaemia trait and normal subjects has been studied. Normal subjects had normal ferritin and MCV, iron-deficient ones had low ferritin and low or normal MCV, and thalassaemics had normal ferritin and low MCV. By the combined use of these two measurements it was possible to identify individuals belonging to one of the three categories with an accuracy of over 95%. Although definitive diagnosis of beta-thalassaemia trait requires the demonstration of abnormal haemoglobin A2 levels or reduced beta-chain synthesis, serum ferritin and MCV measurements are useful screening procedures for the initial diagnosis of beta-thalassaemia trait and iron deficiency. Because of the very small amounts of blood required for both of these measurements, they are particularly suitable for surveying large numbers of subjects in populations with a high prevalence of hypochromic-microcytic anaemias.
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PMID:Serum ferritin and mean corpuscular volume measurement in the diagnosis of beta-thalassaemia minor and iron deficiency. 11 17

For electron microscopic demonstration of complex carbohydrates and simple sugars in the mouse lung, anionic dye and lectins were used. After immersion fixation of small lung tissue blocks, the alveolar surfactant system was destroyed and only membrane bound carbohydrates (cell coat) could be demonstrated by means of colloidal iron and ruthenium red. Fixation of the whole lung via the visceral pleura preserved the alveolar surfactant system. Only this technique afforded a distinction between cell coat components and hypophase components. After performance of the Concanavalin A-peroxidase technique and after incubation in ferritin-labed Concanavalin A, Lens culinaris lectin or Ricinus communis lectin, various saccharide moieties were demonstrable by immune electron microscopy in the hypophase of the alveolar surfactant system.
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PMID:Electron microscopic demonstration of a saccharide moieties in the hypophase of the alveolar surfactant system. 12 9

Mice undergoing prolonged (5 to 8 weeks) immunization with cadium-free feeritin were studied 1 to 32 days following the last ferritin injection. Urine protein was measured and renal tissue examined by light, immunofluorescence, and electron microscopy. Immunized animals developed significant proteinuria and circulating antibody to ferritin.by light microscopy, proetinuric animals had a proliferative glomerular lesion with mesangial hypercellularity and martrix increase, focal and segmental necrosis, fibrin deposits, and occasional crescents. Iron stains revealed prominent mesangial iron deposition. In immunized animals, IgG and C3 deposits were localized mainly in the mesanglium. Electron microscopic studies revealed marked deposition of ferratin complexesexpanded mesangial matrix and mesangial interposition. Ferratin immune complexes were also visualized in epithelial spaces. In the latter location ferritin immune complexes occasionally formed characteristic electron-dense subepithelial deposits. In this model, mesangial and subepithelial localization of autologous ferritin immune complexes is associated with development of glomerulonephritis and characteristic mesangial lesions resembling those seen in some types of human glomerulonephritis.
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PMID:Experimental glomerulonephritis in the mouse associated with mesangial deposition ofautologous ferritin immune complexes. 12 61

The clinical and laboratory findings in three patients with primary acquired sideroblastic anemia (PASA) are described. The results demonstrate that what seems to be a well defined entity of the large group of sideroblastic anemias, is in itself a heterogeneous subgroup, with differences capable of detection by more extensive studies. Electron microscopic examination of erythroid cell precursors confirmed previously described features such as deposition of large amounts of iron, mainly in the mitochondria. The precipitated serum proteins revealed an increased content of ferritin molecules only in the patients and not in control individuals, suggesting an increased supply of iron to the erythroid precursors. This finding could serve as an additional mechanism for the accumulation of iron in the erythroid precursors, considering also the defect in heme synthesis and increased permeability of the erythroid membrane for iron, described in this condition.
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PMID:Clinical and ultrastructural observations in primary acquired sideroblastic anemia. 13 33

A high correlation coefficient r = -0.832 (P r +/- 0 less than 0.0001) was estimated in man for the inverse relationship between the diagnostic 59Fe2+-absorption and the serum ferritin concentration which is very close to the correlation r = -0.88 as described for the relationship between the diagnostic 59Fe2+-absorption and the diffuse cytoplasmic storage iron in the bone marrow macrophages. The increase of the diagnostic 59Fe2+-absorption seems to be an earlier and more sensitive indicator of depleted iron stores whereas the serum ferritin decreases somewhat later during the development of iron deficiency.
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PMID:Correlation between diagnostic 59Fe2+-absorption and serum ferritin concentration in man. 14 49

Using precipitating antibodies to ACI rat liver ferritin and to sodium-dodecyl-sulfate-dissociated protein subunits of ACI rat liver ferritin, we have demonstrated the presence of ferritin-positive sites and subunit-positive sites in situ in several rat hepatoma cell lines by immunofluorescence. Hepatoma cells from three transplantable rat hepatomas (Reuber H-139, Reuber H-35, and Morris 5123) were explanted and propagated. Rabbit antibodies specific for either protein subunits of ferritin or ferritin were prepared by affinity chromatography or by dissociation of antibody-antigen complexes with 0.1 M acetic acid followed by differential ultracentrifugation. Explants of Reuber H-139, Reuber H-35, and Morris 5123 hepatoma cells, grown either in ordinary McCoy's 5a medium or in such medium enriched with iron (0.002% Fe), gave positive immunofluorescence for subunits as well as ferritin. Exposure of a clonal strain of Morris 5123 hepatoma cells to iron-enriched culture medium for varying lengths of time of up to 24 hours resulted in progressive increase in the quantity of ferritin-specific immunofluorescent cytoplasmic material, which was at first present diffusely, and later in clumps. By contrast, during the initial 24-hour period, subunit-specific immunofluorescence remained at relatively low intensity, with diffuse distribution through the cytoplasma. Our findings indicate a) the presence, in the cytoplasm, of the three kinds of hepatoma cells, of unassembled or only partly assembled subunits of fragments of subunits as well as of ferritin, and b) rapid assembly of the protein subunits into apoferritin and ferritin after administration of iron, so that the concentration of subunits in the cytoplasm was not significantly increased.
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PMID:Production of ferritin by rat hepatoma cells in vitro. Demonstration of protein subunits and ferritin by immunofluorescence. 16 99

Ferritins purified from horse spleen and from rat liver, kidney, heart and hepatoma were analyzed by quantitative polyacrylamide gel electrophoresis. From the migration characteristics of these ferritins at several gel concentrations, Ferguson plots were constructed and the molecular sizes and charges (apparent valences) together with their statistical variability were obtained by applying Rodbard computer programs to the data. Finally, ellipses were drawn describing the 95% confidence limits of these data for size and charge and were used to identify those ferritins that differed in size and/or charge. By these criteria, many of the tissue ferritins were differentiated from one another in terms of their molecular size and/or charge. Among the various tissue ferritin monomers, the molecular sizes were essentially similar (420 000-490 000) except for the two heart ferritins which were larger (530 000 and 626 000, respectively). However, the estimated charges on rat liver, kidney and hepatoma monomers (30-38 net protons per molecule) differed from that of spleen monomer (51 net protons per molecule) while the larger rat heart ferritin also had a greater charge (83 net protons) than the smaller (40 net protons). Apoferritins prepared chemically by removal of iron from the holoferritins had migration properties indistinguishable from the parent holoferritins. The migration properties of minor (dimeric) ferritin bands on the gels were compared with those of the monomer bands. The molecular sizes of the minor bands were larger than those of the major bands, and were not inconsistent with a doubling in size. However, charge differences varied, being either similar for major and minor forms (spleen ferritin), approximately twice for the minor form (rat hepatoma ferritin) or five times greater for the minor form (rat liver ferritin). These differences in behavior were confirmed by using minimally sieving gels, on which the major bands of horse spleen ferritin failed to separate whereas those of rat liver ferritin were readily separable. It is concluded that dimers of ferritins from different tissues may associate in different ways.
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PMID:Size and charge heterogeneity of rat tissue ferritins. 17 45

Characteristic cytoplasmic and intranuclear fibrillar bodies were produced, within 24 hours, in epithelial cells of the proximal convoluted renal tubules of rats and mice by injecting a single dose of lead acetate either intraperitoneally (100 mug Pb/g) or into the heart (10 mug Pb/g). The frequency of cytoplasmic fibrillar bodies (CFB) rose during the first 4 days following injection of lead and diminished thereafter. Ten days after intracardiac injection of lead no CFB were found; 10 days after intraperitoneal injection, they were still present, though probably in diminished number. Disappearance of CFB may be related to autophagocytosis. Intranuclear fibrillar bodies did not disappear, perhaps because nuclei lack a lysosomal apparatus. Within the first 3 days after injection of lead, clusters or paracrystalline arrays of ferritin molecules were frequently situated in the immediate vicinity of CRB or abutted against CFB; after the third day, little or no ferritin was found near CFB. Intramuscular injection of iron-dextran complex (50 mg Fe/ml) 24 hours prior to intraperitoneal administration of lead did not increase incidence or size of ferritin clusters in the vicinity of CFB in rats. The presence of ferritin near CFB may have been an indirect consequence of inhibition, by lead, of synthesis of heme prosthetic groups.
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PMID:Evolution of cytoplasmic fibrillar bodies induced by lead in rat and mouse kidneys. 17 27

Measurement of the incorporation of iron into liver cells and liver ferritin of the rat revealed that both incorporated less iron under tumor-bearing condition than in the normal state.
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PMID:Iron incorporation into liver cells and ferritin of tumor-bearing rats. 19 25

Ferritin and its protein subunits in rat hepatoma cell clone M-5123-C1 were biosynthetically labeled with [14C]leucine and 59Fe. Radioimmunoassays of ferritin/apoferritin and of protein subunits in the free polyribosome, membrane-bound polyribosome, smooth membrane, and cytosol fractions were done with ferritin-specific and subunit-specific rabbit IgG antibodies at various time intervals after pulsing. Much more 59Fe was bound by ferritin/apoferritin than by subunits in all of the cell fractions. Binding of iron to subunits may have been a random process. When hepatoma cells were simultaneously pulse-labeled with 59Fe and [14C]leucine, uptake of much of the 59Fe by ferritin occurred relatively early, in comparison to incorporation of [14C]leucine, in all of the cell fractions examined. Thus, 59Fe was readily incorporated into pre-existing ferritin. We conclude that most, if not nearly all, of the iron is incorporated after assembly of protein subunits.
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PMID:Biosynthesis of ferritin in rat hepatoma cells and rat livers. II. Binding of iron by ferritin protein. 19 51


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