Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A single diethylstilbestrol (DES) injection (5 mg DES/100 g body wt) was administrated to several lots (three specimens each) of adult male quail (Coturnix coturnix japonica). The birds were sacrificed 24, 48, 72 and 96 hr after the DES injection. A significant increase in liver weight and a clear drop in the hemoglobin concentration were observed after 24 hr. Later, a progressive rise was observed in plasma iron, total iron binding capacity, plasma copper and the phosphoprotein (vitellogenin), which reached highest values after 96 hr. In the liver, the iron showed an initial increase (24 hr), due to a rise in non-ferritin iron followed by a progressive decrease. Ferritin iron increased slowly but was significantly higher after 96 hr. This experimental model on male quail suggests an estrogen response in birds that could be more general and uniform than in mammals.
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PMID:Iron mobilization in estrogenized male quail. 614 35

Ferritin binds a large quantity of Be2+ (Price D.J. and Joshi, J.G. J. Biol. Chem. 258 (1983) 10873) as well as other divalent metal ions. Therefore the ability of this protein to protect enzymes against or reverse the inhibition by metal ions was studied. Evidence presented here shows that the inhibition by Be2+ of the enzymes Na+K+ATPase, alkaline phosphatase and phosphoglucomutase is reversed by ferritin. Be2+ can be transferred reversibly between phosphoglucomutase and ferritin depending upon the relative concentrations of the 2 proteins. Ferritin also reactivated phosphoglucomutase inhibited by Zn2+, Cu2+, or Cd2+. Incubation of ferritin containing Be2+ with 4-10 fold molar excess of phosphoglucomutase (with respect to Be2+) removed 90% of the Be2+ from ferritin. The rates of inactivation of phosphoglucomutase by Be2+ donated by apoferritin or ferritin were identical. Based upon these observations it is suggested that Be2+ bound to the protein shell and to the iron core are in equilibrium with each other with the equilibrium favoring ferritin-Be2+ complex.
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PMID:Ferritin: protection of enzymatic activity against the inhibition by divalent metal ions in vitro. 633 Sep 34

The effects on iron and copper distribution and metabolism of exposure to high levels of CO2 were studied in the guinea-pig. Mature, male animals were placed in an atmosphere of 15% CO2, 21% O2 (balance N2), and sacrificed from 1 h to 1 week thereafter. Total iron and copper concentrations of blood, liver, spleen and bone, as well as concentrations of heme and ferritin iron, were measured together with blood hematocrit, reticulocytes, plasma hemoglobin, plasma ceruloplasmin and copper concentrations. The results show clearly that rapid and sustained red cell damage or hemolysis ensued several h from the start of CO2 treatment. This resulted in loss of iron and copper from the blood, an influx of both elements into liver, spleen and bone, and a rise in plasma ceruloplasmin. Influx of iron into liver and spleen caused an accumulation of ferritin, the main site for iron storage in cells. Following the effect on red cells, there was an accumulation of heme iron, and a decreased hematocrit, best explained by a depressed activity of the reticuloendothelial and erythropoietic systems. A period of adaptation succeeded these events, in which all blood parameters and most tissue values returned to normal, despite the continuing presence of high CO2. The only changes not reversed were the elevations in liver, spleen and bone iron stores. These remained high, with a net accumulation of greater than 2 mg iron, or 3-4 times more than originally present. The results indicate that at least in the guinea-pig, high CO2 exposure results in red cell damage and other events leading to an accumulation of additional iron in the body; also, that iron accumulated as ferritin and hemosiderin in liver and spleen may not be readily available to restore blood hemoglobin concentrations on an acute basis.
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PMID:Effects of CO2 exposure on distribution of various forms of iron and copper in guinea-pig tissues. 640 60

Rat liver homogenates in 0.1 M Tris, pH 7.5, were heated to 80 degrees C, cooled immediately, and centrifuged at 24,000 X g, and 7Be2+ was added to the supernatant. Twenty-five per cent of the radioactivity was bound to a single protein. It was purified to homogeneity and identified to be ferritin as judged by different criteria. These were sucrose density gradient centrifugation, electrophoresis in polyacrylamide gel of the native or sodium dodecyl sulfate-treated protein, reactivity to antibodies, isoelectric focusing, and total amino acid composition. Comparative study of the ability of ferritin or apoferritin to bind Cd2+, Zn2+, Cu2+, and Be2+ was conducted by using a gel equilibrium technique, Centifree micropartition technique, and microcentrifuge desalting technique. Ferritin could be saturated with Cd2+ or Zn2+ or Cu2+ but not with Be2+ even after 800 g atoms of Be2+ were bound. None of the bound Be2+ was dialyzable at 4 degrees C in 0.05 Tris acetate buffer, pH 8.5, but at pH 6.5 over 80% of the bound metal ion was dialyzed after 72 h. By contrast, apoferritin bound similar amounts of all four metal ions, some of which were dialyzable. By spectrophotometric titrations at pH 6.5 of Be2+ with sulfosalicylic acid (SSA), BeKDSSA was calculated to be 5.0 X 10(-6) M and by competition of sulfosalicyclic acid and ferritin for Be2+ the BeKDferritin was calculated to be 6.8 X 10(-6) M.
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PMID:Ferritin. Binding of beryllium and other divalent metal ions. 641 22

Ceruloplasmin, a copper ferroxidase, promotes the incorporation of Fe(III) into the iron storage protein, apoferritin. The product formed is identical to ferritin as judged by polyacrylamide electrophoresis and iron/protein measurements. Of several proteins examined, only apoferritin accumulates the Fe(III) produced by ceruloplasmin. When ceruloplasmin was replaced by tyrosinase, which we have shown to have ferroxidase activity, no iron incorporation into apoferritin was observed. It is proposed that Fe(III) is transferred directly and specifically to apoferritin. These data support a more specific role for ceruloplasmin in iron metabolism than has previously been proposed.
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PMID:The incorporation of iron into apoferritin as mediated by ceruloplasmin. 641 53

A comprehensive immunologic and serologic analysis was performed on 31 untreated patients with Hodgkin's disease. Immune evaluations stressed T-cell functional activity and included traditional parameters (PHA responsiveness and delayed hypersensitivity skin reactivity), as well as newer functional assays (T-cell colony formation, chemotaxis, spontaneous and antibody-dependent cytotoxicity, and concanavalin A-induced suppressor cell activity (CISA). Serum factors included ferritin, prostaglandins, zinc, copper, immune complexes, and thymic hormone activity. Every patient exhibited at least one T-cell or serum abnormality. The greatest percentage of patients exhibited T-cell defects in chemotaxis (85%), colony formation (81%). and PHA reactivity (64%). Immune defects were more common with advanced disease but were not related to absolute T-cell or monocyte count, skin test anergy, or abnormalities of T mu/T gamma cell proportions. Linear relationships were identified among abnormalities in the three assays employing mononuclear cells (PHA, colony formation, CISA) which may have reflected the inhibitory influence of monocytes present in the mononuclear cell preparations. Low serum zinc correlated with marked impairment of T-cell chemotaxis. Elevated prostaglandins were associated with high PHA reactivity and with depressed colony formation. Our results indicate that many complex factors, including intrinsic T-cell defects, contribute to the impaired immunity associated with Hodgkin's disease.
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PMID:Multivariate analysis of T-cell functional defects and circulating serum factors in Hodgkin's disease. 645 60

Zinc levels in plasma and whole blood were investigated in 2 groups of blood donors. The first group consisted of 19 men and 11 women who donated blood for the first time and were followed during 3 phlebotomies. The second group comprised 44 men with 9 or more previous blood donations, their blood being analysed on a single occasion. Plasma concentrations of copper, magnesium, calcium and ferritin were also analysed. The zinc levels in whole blood and plasma in the second group were significantly lower as compared to the first group (P less than 0.001). Furthermore, the second group had significantly higher levels of copper and copper:zinc quotient in plasma as compared to those of the new blood donors (P less than 0.001). Our results indicate that besides the earlier known effect of blood donation on iron stores, there are also signs of zinc depletion when judged from the zinc levels in plasma and in erythrocytes. No significant changes in calcium and magnesium concentrations were seen during phlebotomy.
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PMID:Zinc, copper, magnesium, and calcium in blood and plasma after phlebotomy. 661 29

In the haematological malignant diseases, especially Hodgkin's disease and other lymphomas, many of the disturbed biological tests reflect the inflammatory process and therefore lack any specificity. Of particular interest are blood sedimentation, the protein-C-reactive test, serum iron, transferrin, serum copper and ferritin. Other tests such as lactic dehydrogenase and beta 2-microglobulin appear to be in the nature of "markers". In 118 patients, serum levels of beta 2-microglobulin above 2.50 mg/l were observed in 83% of the lymphoproliferative disorders and also in 16% of patients without malignant diseases. However, the highest values (greater than 5.00 mg/l) were observed only in 12 patients with lymphoproliferative disorders and 1 patient with "acquired immunodeficiency syndrome".
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PMID:[Usefulness of biologic tests in malignant hemopathies]. 661 75

Ferritin with high and low iron content, 2000 and 790 iron atoms/molecule, was isolated from the spleens of copper-poisoned and control lambs, respectively. Differences in the iron content in vivo were reflected in the properties of the apoferritin protein shells, since the apoprotein from the low iron ferritin took up iron relatively more slowly (0.52 +/- 0.09) and released it more rapidly (1.68 +/- 0.06) in vitro. Although the two types of apoferritin were indistinguishable in terms of surface charge (pI range 4.98-5.43) and in consisting of both heavy and light subunits, the subunit interactions differed markedly; 40-50% of the subunits of low iron ferritin were in dimers stable to reduction and carboxylmethylation, 4% mercaptoethanol, 8% sodium dodecyl sulfate, and 100 degrees C for 30 min, 70% formic acid, and 30% methanol. Subunit dimers were also observed in liver ferritin from mouse and neonatal pig and were enriched in a low iron fraction of horse spleen ferritin. Based on cyanogen bromide fragmentation and NH2-terminal analysis, the natural and chemically cross-linked subunit dimers had two peptides in common; natural subunit dimers also appeared to have a second region cross-linked, suggesting the possibility of both intra- and intersubunit links in the natural dimers. In sheep spleen ferritin, both heavy and light subunits appeared to participate in subunit dimerization. Natural subunit dimers were enriched in low iron ferritin fractions of all ferritin preparations tested (linear correlation = 0.94) and can explain, at least in part, the previously observed effects of iron core size on the apoferritin shell. Whether the subunit cross-links represent part of the subunit assembly process subsequently cleaved by iron (or copper) or whether the cross-links form after iron core formation in vivo has yet to determined. In either case, it is clear that such post-translational variations can affect iron uptake and release and emphasize the importance of the protein shell in determining the iron storage properties of ferritin.
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PMID:Subunit dimers in sheep spleen apoferritin. The effect on iron storage. 661 39

Twelve voluntary adult subjects twice took a 30-min sauna bath, at a temperature of 80 degrees C with a 30-min rest between each, every 12 h for 1 week. Measurements of serum iron, copper, zinc, ferritin and ceruloplasmin were performed before the experiment, after the first and second 30 min in the sauna and at the end of the week. The first two sauna baths did not significantly change the concentrations of the trace elements measured. After the week the mean serum copper concentration had decreased from 15.0 (SD 1.7) mumol x 1-1 to 13.5 (SD 2.0) mumol x 1-1 (p less than 0.02). The mean zinc concentration decreased from 13.8 (SD 2.4) mumol x 1-1 to 9.8 (SD 1.8) mumol x 1-1 (p less than 0.001) during the week of the experiment. At the beginning of the study period two subjects had zinc concentrations below the reference values and after the week nine subjects had zinc concentrations below the reference values. The concentration of serum ferritin decreased from 142.2 (SD 103) micrograms x 1-1 to 111.3 (SD 89) micrograms x 1-1 (p less than 0.02) whereas the values of ceruloplasmin remained unchanged. Our findings confirm the earlier suggestion that heavy exposure to heat can cause a loss of some trace elements, especially zinc.
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PMID:Serum iron, copper, zinc, ferritin, and ceruloplasmin after intense heat exposure. 668 31


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