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

The Prussian blue reaction was evaluated at the ultrastructural level as a cytochemical method to identify ferric and ferrous iron in rat bone marrow and splenic macrophages. Satisfactory tissue preservation and staining were achieved after fixation for 1 hr in 3% glutaraldehyde and exposure for 30 min to Perls's ferrocyanide solution before routine osmication and embedding. The acid ferrocyanide solution formed cuboidal and irregular electron-opaque deposits which localized ferric iron in the macrophage siderosomes and hyaloplasm. When thin sections were directly stained with the acid ferrocyanide, the stain deposits were much less distinct. The size and number of cytes exhibited sparse evenly distributed stain deposits. Several cells displayed abundant precipitates on the inner surface of the plasmalemma. Prussian blue precipitates were occasionally seen in mitochondria and nuclear euchromatin. Although osmium tetroxide post-fixation improved tissue preservation, it did not enhance the density of the ferri-ferrocyanide precipitate. The ferrocyanide solution yielded cuboidal deposits also in clots impregnated with ferritin, and electron diffraction analysis confirmed the symmetrical crystal structure of these stain precipitates. Smaller irregular precipitates were formed in clots impregnated with FeCl3, or Fe2 (SO4)3 solutions, despite the equally interpreted as indicating that the iron hydroxide core or protein structure of ferritin and hemosiderin contributed to the formation of the ultrastructurally evident cuboidal precipitates, but were not necessary for the formation of a colored reaction product. The acid ferrocyanide solution failed to stain clots formed in FeCI2, CuCI2 or CuCI solutions. Staining with a ferricyanide solution identified only sparse foci of ferrous iron in some siderosomes. This study demonstrates that the Prussian blue reaction can be used ultrastructurally to localize iron cations bound to some nonheme iron binding proteins.
J Histochem Cytochem 1978 Sep
PMID:Ultrastructural localization of nonheme celluar iron with ferrocyanide. 71 49

The important biological iron bearing molecule ferritin has been studied using the 57Fe Mossbauer resonance. Natural and reconstituted ferritin samples have been studied in the temperature range 4--300 K. At low temperatures six-line magnetic hyperfine spectra are observed but with noticeably asymmetric line shapes, at high temperatures doublets are observed and in an intermediate temperature range (30--40 K) complex spectra characteristic of superparamagnetic behaviour are observed. From a theoretical study of the dependence of the hyperfine splitting parameters on particle size and from the experimental probability distributions obtained for these parameters from the Mossbauer spectra, it has been possible to derive the ferritin micelle particle size distributions for four different samples. It is found that the natural and reconstituted samples have roughly similar distributions except for the sample reconstituted from apoferritin in the presence of a phosphate environment. This sample is shown to have a slightly narrower particle size distribution centred on a smaller mean diameter. The information derived from these Mossbauer measurements are finally shown to be consistent with conclusions reached from separate biochemical experiments.
Phys Med Biol 1978 Sep
PMID:A Mossbauer determination of the iron core particle size distribution in ferritin. 71 1

Electron microscope observations of thin sections of epoxy resin-embeded posterior silk gland cells at the later stage of the fifth instar revealed that the Golgi vacuoles and the secretory granules (fibroin globules) in the cytoplasm and the glandular lumen contain fine fibrous materials. In frozen thin sections these structures appear as electron-dense granules and electron-dense blocks, or a column, respectively. Immunoelectron microscopy has shown that ferritin particles or products of the peroxidase reaction are localized on these structures. It was concluded that the fine fibrous materials most probably represent native fibroin molecules or their aggregates.
J Cell Biol 1976 Sep
PMID:Studies on the posterior silk gland of the silkworm Bombyx mori. V. Electron microscope localization of fibroin in the posterior silk gland at the later stage of the fifth instar. 78 74

The distribution and mobility of anionic sites on the surfaces of baby hamster kidney cells were studied by utilizing the multivalent ligand, polycationic ferritin, as a visual probe. Our observations revealed that anionic sites are distributed over the entire cell surface, with the highest density of sites being located on cell surface microextensions. Following the initial binding of polycationic ferritin to the surface of unfixed cells, the ligand-bound anionic sites redistributed by migrating from the surface of microextensions to the surface of the cell body. In 20 min, this migration resulted in a total clearing of anionic sites from the surface of microextensions concomitant with the formation of patches of anionic sites on the surface of the cell body. Polycationic ferritin-induced migration and patch formation of anionic sites was not prevented by 2,4-dinitrophenol, N-ethylmaleimide, colchicine, or cytochalasin B. However, the ligand-induced redistribution of cell surface anionic sites was prevented by prefixation of cells with glutaraldehyde.
J Cell Biol 1975 Sep
PMID:The distribution and mobility of anionic sites on the surfaces of baby hamster kidney cells. 80 51

After in vivo infusion, radio-active indium is fixed by liver and bone marrow, but more slowly and less completely than iron. It does not incorporate to haem. It is found as labelled ferritin in the liver, after the fifth day. In the bone marrow, indium is almost exclusively found as labelled transferrin; several arguments suggest the intra-cellular site of the labelled protein. Using indium may enable a better knowledge of the intermediary iron pools.
C R Acad Hebd Seances Acad Sci D 1975 Sep 22
PMID:[Study of proteins binding radioactive indium in vivo]. 81 62

Serum ferritin was measured in 2982 blood donors. First-time male donors had a geometric mean of 127 microgram/liter and female donors 46 microgram/liter. While values were essentially constant in the women between the ages of 18 and 45, there was a rapid increase in the men between 18 and 30 years of age consistent with the establishment of iron stores during that time. Blood donation was associated with a decrease in serum ferritin. One unit per year, equivalent to an increased requirement of 0.65 mg/day, halved the serum ferritin level in the male. More frequent donations were associated with further decreases. From the data obtained it would appear that male donors, while depleting their iron stores, were able to donate 2-3 U/yr without an appreciable incidence of iron deficiency. Women could donate only about half that amount, and more frequent donations were associated with a high incidence of iron deficiency and donor dropout. These data have provided information on the effect of graded amounts of iron loss through bleeding on iron balance.
Blood 1977 Sep
PMID:Effect of blood donation on iron stores as evaluated by serum ferritin. 88 21

Twenty-four hours after the administration of Ga-67 citrate and Fe-59 citrate, rabbits were killed and their livers removed and homogenized. Labile proteins in the filtered liver homogenates were denatured; ferritin was then crystallized from the supernatants by cadmium sulfate. Sephadex G-200 gel filtration of the ferritin fractions was done to determine the distribution of molecular weights in the substances associated with Ga-67 and Fe-59. It was found that Ga-67 was incorporated into the crystallizable ferritin fraction of rabbit hepatocytes with approximately one-sixth the uptake of simultaneously administered Fe-59. Gel-filtration chromatography confirmed that both the Ga-67 and the Fe-59 of the crystallizable ferritin fraction were associated with substances of the appropriate molecular weight for ferritin.
J Nucl Med 1977 Sep
PMID:The incorporation of Ga-67 into the ferritin fraction of rabbit hepatocytes in vivo. 89 95

Human lactoferrin (Lf) labeled with 125I and/or 59Fe was found to be ingested in vitro by mouse peritoneal macrophages (MPM). The uptake measured after 15 h incubation reached a saturation point at a concentration of 200 microgram/ml in the culture medium, whatever was the iron content of Lf. In such conditions, the uptake of transferrin (Tf) used as a control was 10 times lower. At a concentration of 80 microgram/ml in the medium, one cell picked up about 0.7 X 10(6) molecules of Lf per hour, and 0.13 X 10(6) molecules of Tf per hour. Iron-saturated Lf disappeared from MPM with a half life of 14.5 h, whereas the halflife of iron-free Lf was 4.2 h. Concomitant with the intracellular digestion of Lf, the iron was transmitted to ferritin. These data provide additional support for the hypothesis that Lf plays a key role in iron turnover, especially at the level of the reticuloendothelial system where iron is recovered from the catabolism of erythrocytes.
J Exp Med 1977 Sep 01
PMID:The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin. 89 89

Peripheral blood lymphocytes from patients with all stages of untreated Hodgkin's disease and from normal healthy adults were shown to synthesize and release ferritin in vitro. Ferritin synthesis was confirmed by immunoelectrophoresis, double immunodiffusion and autoradiography. Hodgkin's disease lymphocytes synthesized ferritin 4.2 times faster and released it 2.4 times faster than did normal lymphocytes, whereas total protein synthesis was faster in normal lymphocytes. Patients with nodular sclerosis and perhaps those with absence of fever had the highest synthetic rates; however no relationship was observed between relative rates of lymphocyte ferritin synthesis and sex, age, anatomical stage and presence of splenic or hepatic involvement by tumor. Addition of iron to normal human lymphocytes produced little or no change in ferritin synthesis. These data indicate that part of the intracellular ferritin detected in peripheral blood lymphocytes from patients with Hodgkin's disease and from normal individuals resulted from de novo synthesis rather than from uptake and storage of serum ferritin, and suggests that elevated ferritin levels detected in the serum and tumor tissue of Hodgkin's disease patients originate from lymphocytes.
Int J Cancer 1977 Sep 15
PMID:Increased ferritin synthesis and release by Hodgkin's disease peripheral blood lymphocytes. 90 87

MODIFICATIONS IN RABBIT SPERM PLASMA MEMBRANES DURING EPIDIDYMAL PASSAGE AND AFTER EJACULATION WERE INVESTIGATED BY USED OF THREE LECTINS: concanavalin A (Con A); Ricinus communis I (RCA(I)); and wheat germ agglutinin (WGA). During sperm passage from caput to cauda epididymis, agglutination by WGA drastically decreased, and agglutination by RCA(I) slightly decreased, although agglutination by Con A remained approximately unchanged. After ejaculation, spermatozoa were agglutinated to a similar degree or slightly less by Con A, WGA, and RCA(I), compared to cauda epididymal spermatozoa. Ultrastructural examination of sperm lectin-binding sites with ferritin- lectin conjugates revealed differences in the densities of lectin receptors in various sperm regions, and changes in the same regions during epididymal passage and after ejaculation. Ferritin-RCA(I) showed abrupt changes in lectin site densities between acrosomal and postacrosomal regions of sperm heads. The relative amounts of ferritin-RCA(I) bound to heads of caput epididymal or ejaculated spermatozoa. Tail regions were labeled by ferritin RCA(I) almost equally on caput and cauda epididymal spermatozoa, but the middle-piece region of ejaculated spermatozoa was slightly more densely labeled than the principal-piece region, and these two regions on ejaculated spermatozoa were labeled less than on caput and cuada epididymal spermatozoa. Ferritin-WGA densely labeled the acrosomal region of caput epididymal spermatozoa, although labeling of cauda epidiymal spermatozoa was relatively sparse except in the apical area of the acrosomal region. Ejaculated spermatozoa bound only a few molecules of ferritin-WGA, even at the highest conjugate concentrations used. Caput epididymal, but not cauda epididymal or ejaculated spermatozoa, bound ferritin-WGA in the tail regions. Dramatic differences in labeling densities during epididymal passage and after ejaculation were not found with ferritin-Con A.
J Cell Biol 1977 Sep
PMID:Lectin-binding sites on the plasma membranes of rabbit spermatozoa. Changes in surface receptors during epididymal Maturation and after ejaculation. 90 74


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