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)

Fluid shear force may deform point-attached erythrocytes to become droplike shaped and anchored by a single long or 2-4 short tethers. By addition of glutaraldehyde to the medium the cells were fixed such as to stabilize this deformation for ensuing SEM, freeze-fracture, fine structural, and ultrahistochemical studies. Freeze-fracture specimens revealed identical numbers and distribution patterns of membrane particles in both the membrane of tethers and of the droplike portions of red cells. Segregated vesicles most often were located adjacent to the attachment site of the tether. All of the vesicles were devoid of membrane particles. Irrespective of their length, the tethers were about 0.1 micrometer in diameter. Cross-sections of the tether membrane and the plasmalemma of the major part of the cell appeared identical. Ultrahistochemical studies revealed the same intensity of iron binding capacity and affinity to ferritin labelled anti AHP at either area of the deformed erythrocyte membrane. Segregating vesicles were also stained by colloidal iron and by fer-anti AHP. By means of the DAB-reaction no haemoglobin was demonstrated within the vesicles. All of these findings corroborate the notion, that lipid molecules were segregated from the membrane whose curvature increased considerably during the formation of the tether.
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PMID:Lipid segregation from human erythrocyte tethers. 616 75

Ferritin (Fer) is the major iron storage protein in man. Its synthesis is regulated both at the translational and transcriptional levels. In previous studies on transcriptional regulation of the human H-ferritin-encoding gene (FERH), a 160-bp promoter segment was analyzed [Bevilacqua et al., Gene 111 (1992) 255-260]. In order to obtain a more complete view of the elements involved in the transcriptional regulation of FERH, we have studied, in a further upstream region of the human FERH promoter (pFERH), a sequence between -272 and -291, named G-fer, because it contains a stretch of ten G, which binds a nuclear factor present in different cell types. DNA-binding assays and competition experiments suggest that the factor binding to G-fer has binding properties very similar to inhibitory factor-1 (IF-1), an ubiquitous factor that interacts with G-rich elements in the promoters of the mouse type-I collagen genes. DNA transfection experiments in HeLa cells, using either a wild-type or mutated pFERH fused to a reporter gene, showed that a 3-bp substitution mutation, that abolished the binding of the specific factor to G-fer, increased the promoter activity, thus suggesting an inhibitory role for the G-fer element and its cognate trans-acting factor.
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PMID:A negative cis-acting G-fer element participates in the regulation of expression of the human H-ferritin-encoding gene (FERH). 814 27

Dietary intake and uptake of cadmium (Cd) were studied in nonsmoking women, 20-50 years of age, consuming a mixed diet low in shellfish (N = 34) or with shellfish once a week or more (N = 17). Duplicate diets were collected during 4 consecutive days for the determination of Cd content. The women kept detailed dietary records, and the intake of energy and various nutrients was calculated. The shellfish diets (median 22.3 micrograms Cd/day) contained twice as much Cd as the mixed diets (median 10.5 micrograms Cd/day; p < 0.0001). Cadmium in feces corresponded to 100 and 99% of that in duplicates of shellfish diets and mixed diets, respectively, indicating a low average absorption of the dietary Cd. In spite of the differences in the daily intake of Cd, there was no statistically significant difference in the concentrations of Cd in blood (B-Cd, shellfish group 0.25 micrograms/liter, mixed diet group 0.23 micrograms/liter) or urine (U-Cd, 0.10 micrograms Cd/liter in both groups). This indicates a lower absorption of Cd in the shellfish group than in the mixed diet group or a difference in the kinetics. A higher gastrointestinal absorption of Cd in the mixed diet group could partly be explained by lower body iron stores as measured by the concentrations of serum ferritin (S-fer, median 18 micrograms/liter, compared to 31 micrograms/liter in the shellfish group). In the mixed diet group, S-fer was negatively correlated with B-Cd and the main determining for B-Cd besides U-Cd in the multiple regression analysis, indicating an increased absorption of Cd at low body iron stores. When women with S-fer exceeding 20 micrograms/liter were compared, the higher dietary intake of Cd in the shellfish group compared to the mixed diet group (24 versus 10 micrograms/day) resulted in higher B-Cd (0.26 versus 0.16 micrograms/liter), although not in proportion to the difference in Cd intake. Thus, there seems to be differences in the bioavailability and/or kinetics of dietary Cd related to the type of diet. This is, to our knowledge, the first study where the influence of various types of diets and nutritional factors on the intake and uptake of cadmium in human subjects has been studied.
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PMID:Bioavailability of cadmium from shellfish and mixed diet in women. 861 41

A cDNA clone encoding a subunit of the tobacco hornworm Manduca sexta (Ms) hemolymph (serum) ferritin (Fer) has been identified and sequenced. The deduced amino acid (aa) sequence shows approx. 50% similarity to vertebrate Fer subunit sequences, and the nucleotide sequence contains a stem-loop structure in the 5' untranslated region that could serve as an iron-responsive element (IRE). The stem-loop of this putative IRE exhibits high identity to vertebrate IRE that play an essential role in the control of Fer synthesis. The Ms Fer subunit lacks one of the three Tyr residues required for the rapid biomineralization of iron shown in vertebrate heavy-chain Fer. In addition, aa residues that comprise the putative ferroxidase centers generally are not conserved, suggesting that the Ms Fer subunit more closely resembles the vertebrate light-chain subunit. Northern blot analyses indicate that the fer mRNA is expressed in the midgut, fat body and hemocytes, with the greatest expression in the midgut.
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PMID:Manduca sexta hemolymph ferritin: cDNA sequence and mRNA expression. 868 13

In yellow fever mosquito cells (Aag2 clone), iron treatment induces a threefold increase in ferritin message (fer mRNA) and protein (ferritin) by 16 h. These data contrast with work in mammalian hepatocytes and fibroblasts in which fer mRNA levels do not change with iron stimulation, but ferritin levels increase 50-fold. Pretreatment of the Aag2 cells with actinomycin D blocks induction of fer mRNA and reduces the ferritin subunit synthesis, suggesting that iron induction of ferritin subunit synthesis is subjected to transcriptional control. A putative iron-regulatory protein has also been identified in cytoplasmic extracts from Aag2 cells.
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PMID:Transcriptional control is relevant in the modulation of mosquito ferritin synthesis by iron. 1054 70

Serum erythropoietin levels (s-[epo]), haemoglobin concentration ([Hb]), haematocrit (hct), and ferritin concentration ([fer]) were measured in seven healthy male volunteers (20-23 years) exposed continuously to hypoxia (PO(2) 14 kPa) for 10 days. Serum erythropoietin concentration increased significantly from 9.5 +/- 3.51 to 33.6 +/- 11.64 U L(-1) (P < 0.05) after 2 days of hypoxia. Thereafter, s-[epo] decreased. However, after 10 days s-[epo] was 18.7 +/- 5.83 U L(-1) which was still increased above the pre-hypoxia level (P < 0.05). Serum haemoglobin concentration and hct increased over the 10 days of hypoxia, [Hb] from 152 +/- 8.9 to 168 +/- 9.2 gL(-1) (P < 0.001), and hct from 43 +/- 2.4 to 49 +/- 2.6% (P < 0.001). Ferritin concentration decreased significantly during the hypoxic exposure from 82 +/- 46.9 to 44 +/- 31.7 mmol L(-1) after 10 days (P < 0.01). In conclusion, the initial increase of s-[epo] under controlled normobaric hypoxia was marked, 353%, and levelled off after 5-10 days at 62-97% above normoxia level. There was also a significant increase in [Hb] and hct and a decrease in [fer] after 10 days of exposure to normobaric hypoxia.
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PMID:Erythropoietin concentrations during 10 days of normobaric hypoxia under controlled environmental circumstances. 1190 21

The aim of the study was to assess the role of serum tumour markers (NSE, Cyfra 21-1, CEA, LDH, ferritin) as a prognostic and predictive factors in 79 patients with advanced NSCLC treated with chemotherapy. Objective response to treatment was significantly more frequent in the patient with serum NSE > 12.5 ng/ml. Progression of disease was observed more often in patients with serum Cyfra 21-1 >10 ng/ml or LDH >480 U/L. CEA >3 ng/ml, LDH >480 U/L, for coefficient >1, NSE >20 ng/ml and Cyfra 21-1 >10 ng/ml had a negative impact on survival in univariate analysis. Independent negative prognostic significance of fer coefficient >1 was confirmed by multivariate analysis.
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PMID:[The significance of the serum tumour markers as a prognostic and predictor factors in nonsmall cell lung cancer patients]. 1698 65