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

Friend erythroleukaemic cells can be induced to mature along the erythroid differentiation pathway when an inducing agent such as dimethyl sulphoxide is included in the medium. In the absence of the inducing agent, the 707B line of Friend erythroleukaemic cells is highly agglutinable by the lectins concanavalin A or wheat germ agglutinin. However, 48 h after the induction of differentiation, there is a marked decrease in the agglutination of the cells in the presence of either lectin. This suggests that early in differentiation a change occurs in the cell membrane preceding the onset of globin synthesis which starts approximately 72 h after induction. The change in agglutination by concanavalin A also occurs in the presence of reagents which do not induce haemoglobin synthesis in the 707B line of Friend erythroleukaemic cells but which are able to stimulate the synthesis of this protein in other erythroleukaemic cell lines. The reduction in the agglutinability of the differentiating cells does not seem to result from a reduction in the number of concanavalin A receptors on the cells, nor does it reflect a change in the clustered distribution of concanavalin A receptors in the differentiating cells. Both the control and dimethyl sulphoxide-induced cells show a similar patchy distribution of ferritin-labelled concanavalin A when examined by electron microscopy. Polyacrylamide gel electrophoresis shows little change in the total pattern of protein synthesis by control and differentiating cells when pulse-labelled with [35S] methionine. However, use of 125I-labelled concanavalin A to stain polyacrylamide gels, on which the total proteins of control and differentiating cells had been separated, revealed a profound change in the composition of the concanavalin A-binding proteins. The control, undifferentiated cells contained eleven or more classes of concanavalin A-binding glycoproteins, many of which stained to a lesser degree as the cell density increased. After the onset of differentiation, 2 new concanavalin A-binding glycoproteins appeared within 48 h. One of these proteins has a molecular weight in excess of 180 000 while the other migrated with an apparent molecular weight of approximately 100 000. After erythroid differentiation had progressed for 120 h, these newly synthesized glycoproteins became the major concanavalin A-binding proteins of the erythroleukaemic cells.
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PMID:The interaction of lectins with the surface of differentiating erythroleukaemic cells. 29 32

Low density lipoprotein (LDL) oxidation mediated by phorbol myristate acetate (PMA)- and formylmethionylleucylphenylalanine (FMLP) -stimulated human neutrophils was enhanced by 70% in the presence of ferritin. Iron released from ferritin by the superoxide anion generated in the respiratory burst of stimulated neutrophils is shown to be involved in lipoprotein oxidation. Ascorbate (100 microM), superoxide dismutase (10 micrograms/ml) and uric acid (430 microM) showed inhibitory effects of 30% [corrected], 70% and 50% on LDL oxidation, respectively. Ceruloplasmin (2.7 microM) potentiated LDL oxidation by stimulated neutrophils and ferritin, both alone and in the presence of methionine. Methionine (1 mM) and catalase (30 micrograms/ml) increased LDL oxidation by stimulated neutrophils and ferritin. These data suggest that LDL oxidation by stimulated neutrophils and ferritin may be relevant in inflammation when both neutrophils and ferritin are increased.
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PMID:Low density lipoprotein oxidation by stimulated neutrophils and ferritin. 133 54

1. Infant rats and rabbits received intraperitonal aluminium (Al) chloride (5, 10 or 20 mg Al/kg body weight) every third day from one to four weeks of age. 2. When the polysomal fraction was tested in a protein synthesizing system, a significant increase in the incorporation of [14C] leucine, [14C] phenylalanine, or [35S] methionine into proteins in vitro was observed at the higher doses in rats but not rabbits. 3. The incorporation of [35S]methionine into brain ferritin was measured using polysomal mRNA or mRNA "stored" in the ribonucleoprotein (RNP) particle fraction. 4. The results suggest that Al exposure causes the mobilization of ferritin mRNA from the latter fraction to the polysomal fraction for increased ferritin synthesis.
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PMID:Some effects of aluminium on rat brain protein synthesis. 136 9

Ferritin is the iron-storage protein of eukaryotic organisms. The nucleotide sequence encoding Azotobacter vinelandii bacterioferritin, a hemoprotein, was determined. The deduced amino acid sequence reveals a high degree of identity with Escherichia coli bacterioferritin and a striking similarity to eukaryotic ferritins. Moreover, derivation of a global alignment shows that virtually all key residues specifying the unique structural motifs of eukaryotic ferritin are conserved or conservatively substituted in the A. vinelandii sequence. The alignment suggests specific methionine residues as heme-binding ligands in bacterioferritins. The overall sequence similarity with conservation of key structural residues implies that all ferritins form a unified family of proteins. The results implicate ferritins as proteins potentially common to all aerobic organisms and as such useful in taxonomic classification, evolutionary analysis, and environmental monitoring.
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PMID:Unification of the ferritin family of proteins. 154 5

A method for the purification of ferritin from rainbow trout liver by heat extraction and gel filtration is described. The number of iron atoms varied from 500 to 2000 in purified ferritin. The neutral sugar composition detected was 86 mol of glucose, 24 mol of fucose, 12 mol of galactose, and 8 mol of mannose per mol of ferritin and apoferritin. Release of iron was achieved using low molecular weight chelating agents. The order of effectiveness of chelators was nitrilotriacetate greater than EDTA greater than citrate. Removal of the iron does not imply reduction of Fe3+. The rate of release of iron increased with decreasing pH. The slowest release was at pH 7.5. The endogenous chelator is not only sulphydrylic but seems to include carbohydrates that participate in the binding of Fe2+. Trout ferritin exhibits heterogeneity upon isoelectric focusing; four isoferritins with pI values of 4.5 to 4.85 were detected. This heterogeneity represents polymorphic, not polymer, forms. The amino acid composition differs from that of ferritins from other species. High concentrations of glutamic and aspartic acids, alanine, leucine, glycine, and lysine were detected along with low concentrations of methionine and cysteine.
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PMID:Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.). 179 41

The iron-responsive regulation of ferritin mRNA translation is mediated by the specific interaction of the ferritin repressor protein (FRP) with the iron-responsive element (IRE), a highly conserved 28-nucleotide sequence located in the 5' untranslated region of ferritin mRNAs. The IRE alone is necessary and sufficient to confer repression of translation by FRP upon a heterologous message, chloramphenicol acetyltransferase, in an in vitro translation system. The activity of FRP is sensitive to iron in vivo. Cytoplasmic extracts of rabbit kidney cells show reduction of FRP activity when grown in the presence of iron, as detected by RNA band shift assay. Using a nitrocellulose filter binding assay to examine the interaction of FRP with the IRE in more detail, we find that purified FRP has a single high-affinity binding site for the IRE with a Kd of 20-50 pM. Hemin pretreatment decreases the total amount of FRP which can bind to the IRE. This effect is dependent on hemin concentration. Interestingly, the FRP which remains active at a given hemin concentration binds to the IRE with the same high affinity as untreated FRP. A variety of hemin concentrations were examined for their effect on preformed FRP/IRE complexes. All hemin concentrations tested resulted in rapid complex breakdown. The final amount of complex breakdown corresponds to the concentration of hemin present in the reaction. The effect of hemin on FRP activity suggests that a specific hemin binding site exists on FRP.
Biol Met 1991
PMID:Characteristics of the interaction of the ferritin repressor protein with the iron-responsive element. 185 87

Iron stimulates ferritin synthesis in whole cells and animals, by increasing the entry of ferritin mRNA into polyribosomes. Dissection of the regulation at the molecular level has identified a 28-nucleotide, conserved, regulatory sequence (IRE = iron regulatory element) in the 5' non-coding region of ferritin mRNAs, plus trans-acting factor(s), one of which is a 90-kDa protein. The site of iron action is not entirely characterized but may involve heme; sequences in the 3' non-coding region of ferritin mRNA can modulate regulation. Ferritin mRNA is the first eukaryotic mRNA for which a conserved regulatory sequence and regulator protein have been identified. The same RNA-protein motif is used, through iron-dependent degradation of transferrin receptor mRNA, to decrease synthesis of the receptor and cellular iron uptake. The regulatory structure of the transferrin receptor mRNA is composed, in part, of five copies of the IRE in the 3' non-coding region. IRE structure, probed by cleavage with RNases T1, V1, 1,10-phenanthroline-Cu or modification with dimethyl sulfate, is a hairpin loop with conformational variations dependent on magnesium; a base-paired region flanking the IRE is also structurally sensitive to magnesium. Similar results were obtained with a synthetic 55-mer containing the IRE and with a full-length in vitro transcript with a G----A substitution in the loop.(ABSTRACT TRUNCATED AT 250 WORDS)
Biol Met 1991
PMID:Ferritin mRNA probed, near the iron regulatory region, with protein and chemical (1,10-phenanthroline-Cu) nucleases. A possible role for base-paired flanking regions. 185 88

The binding of Phaseolus vulgaris (PHA) isolectins L4 and E4 to the brush border membrane of differentiated Caco-2 cells was studied and the impact on cellular metabolism and microvilli was assessed. Computer analysis of the data based on binding experiments with peroxidase conjugated isolectins gave mean (SD) values for maximal binding of 2540 (151).10(-9) M for PHA-L4 and 2104 (140).10(-9) M for PHA-E4 per mg of brush border membrane protein. The dissociation constants for L4 and E4 binding were 4.3 (1.4).10(-6) M and 1.1 (0.8).10(-6) M, respectively. Incubation of differentiated Caco-2 cells for 30 minutes with ferritin conjugated PHA isolectins showed that, as indicated by the number of ferritin particles, PHA-E4 bound to the microvilli to a greater extent than PHA-L4. Ferritin particles were also localised intracellularly over endocytotic invaginations and vesicles. After incubation for 48 hours with PHA-L4 or PHA-E4, the relative incorporation of precursors for DNA, RNA, and (glyco)protein synthesis into the trichloroacetic acid insoluble fraction of the Caco-2 cells was determined. Both isolectins stimulated the incorporation of thymidine and glucosamine, but neither PHA-L4 nor PHA-E4 were able to influence the incorporation of uridine. With respect to fucose, methionine, and N-acetyl mannosamine, the stimulatory effect remained confined to PHA-E4. Since PHA-L4 and PHA-E4 were tested at the same concentrations, PHA-E4 is more effective than PHA-L4. The changes in the uptake of radioactive precursors were lost after heat inactivation of PHA-E4. Compared with control and PHA-L4 incubated Caco-2 cells, the microvilli of PHA-E4 incubated cells were shortened significantly (p less than 0.01).
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PMID:Binding of kidney bean (Phaseolus vulgaris) isolectins to differentiated human colon carcinoma Caco-2 cells and their effect on cellular metabolism. 186 41

The nature of the amino acids whose codons border introns in ferritin genes is novel; the disposition of these intron boundaries within the three-dimensional structure of the 24-subunit molecule differs significantly from that of other proteins. These observations are discussed in relation to the functions of isoferritins.
Biol Met 1991
PMID:The location of exon boundaries in the multimeric iron-storage protein ferritin. 187 82

The cores of ferritins isolated from different organs of human subjects with beta-thalassemia/hemoglobin E (beta-thal/HbE) disease have different size distributions and crystallinities depending on the source organ. These patients have not been treated by hypertransfusion regimen or iron chelation therapy. beta-Thal/HbE spleens and livers yield ferritin cores which are less crystalline than those isolated from normal spleens and livers, reflecting the more rapid deposition of iron in the diseased state. Ferritins isolated from the hearts and pancreases of beta-thal/HbE subjects were found to have larger, more crystalline cores than those from the beta-thal/HbE livers and spleens, possibly as a consequence of the role of the heart and pancreas as long-term iron deposition sites in this iron overload pathology.
Biol Met 1991
PMID:Organ-specific crystalline structures of ferritin cores in beta-thalassemia/hemoglobin E. 193 35


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