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)

The distribution and quantitation of the iron-binding proteins of rat small intestinal mucosa was studied, in iron-deficient and replete animals, to explore their role in the absorption of iron. Adsorption (mucosal uptake) of iron in in situ ligated loops of small intestinal mucosa was found to be uniform throughout the length of the small intestine whereas absorption (carcass uptake) showed a steep decreasing gradient from the duodenum to the ileum. The disrupted, in vivo labeled mucosal cells were fractionated by isopycnic centrifugation and transferrin and ferritin were quantitated by radioimmunoassay. Transferrin derived from mucosal cells was shown to have a higher affinity for the antibody than transferrin in serum. Of the transferrin present in the mucosal extract, only a portion could be accounted for by contamination from the serum; the proteolysis resistant and intrinsic transferrin may be mucosal cell specific. Transferrin was found in similar amounts in all regions of the small intestine, was not affected by iron loading but doubled in response to iron deficiency. Mucosal ferritin was found in greater amounts in the iron-absorbing areas of the intestine, increased in the duodenum of iron-loaded animals, and decreased in iron-deficient animals. The incorporation of newly absorbed radioiron into ferritin was only found in iron absorbing regions and was completely inhibited by colchicine and cytochalasin-B, suggesting that ferritin was loaded with iron at the point of iron absorption and that the process is associated with vesicle movement and not simple diffusion. Transferrin and ferritin-specific immunoabsorption and also gel filtration established that no other soluble iron binding proteins were involved in absorption.
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PMID:Iron binding proteins of iron-absorbing rat intestinal mucosa. 685 22

Dietary iron intake and hematocrit, hemoglobin, serum iron, transferrin saturation and serum ferritin were studied longitudinally in 425 French-Canadian children from upper-middle class families at 3, 6, 9, 12, 15, 18, 24 and 36 months. At 3 to 9 months, the median iron intake exceeded the amount recommended (7 mg/d), at 12 to 36 months it was close to the amount recommended (8 mg). The proportion of anaemic children as diagnosed by low hematocrit and hemoglobin values did not exceed 5 percent except at three months of age. Transferrin saturation lower than 16 percent was detected in 12 percent of the children aged 12-18 months and 8 percent of those aged 24-36 months. Serum ferritin increased from 18 to 36 months of age; between 18 months and 3 years, the proportion of children with deficient serum ferritin (SF less than 10 ng/ml) and low iron reserves (SF 10-20 ng/ml) declined respectively from 29 to 2 percent and 55 to 26 percent. Thus, as the children grew older the iron intake still permitted the improvement of hematologic parameters of iron status in most subjects. The progressive increase of hematological values with age emphasizes the need for more specific standards for children of various ages.
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PMID:Iron status of French-Canadian children: a three year follow-up study. 687 11

Selected populations of human peripheral blood T lymphocytes, B lymphocytes, monocytes and polymorphonuclear cells were examined for their intracellular content of lactoferrin transferrin and ferritin by an indirect immunofluorescence technique. Lactoferrin was found in polymorphs but not in lymphoid cells. Two different lactoferrin staining patterns were observed which we designated 'perinuclear', characterized by a ring of positive material round the nucleus, and cytoplasmic, in which most positive material was distributed in the cytoplasm. The former staining pattern was found in high density polymorphs the latter was associated with low density polymorphs occasionally found contaminating the peripheral blood mononuclear cell suspension. After incubation in vitro, the perinuclear pattern changed to cytoplasmic staining. Transferrin was found in T cells and polymorphs. In contrast, only a few transferrin containing cells were detected in the B cell and monocyte fractions. Following overnight incubation, a halo of positive material was found surrounding T cells stained for transferrin, suggesting that T cells released transferrin during incubation. Ferritin was also found in T cells and adherent cells. Following latex particle ingestion, the intensity of ferritin staining was markedly increased. Only a small proportion of lymphoid cells and monocytes stained for transferrin or ferritin in the total peripheral blood mononuclear cell suspension. The results indicate, therefore, that in response to manipulation procedures used routinely for the selection of human peripheral blood lymphoid cells, detectable amounts of transferrin and ferritin are present in T but not B cells. The fact that T cells are equipped with proteins known to participate in binding and storage of iron may constitute, at least in part, the basis for the contribution of these cells to the regulation of other major biological systems.
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PMID:Iron binding proteins in selected human peripheral blood cell sets: immunofluorescence. 700 Jan 58

The hepatocyte metabolism of 59Fe-labelled ferritin, haemoglobin-haptoglobin and transferrin has been examined in rats. All three forms of 59Fe became transiently available to desferrioxamine (DF) at the time they would otherwise have entered storage or alternative pathways of iron metabolism. However, differences in both the patterns of spontaneous 59Fe reutilization by normal and iron deficient rats and the partition of chelate iron excretion between bile and urine, suggested that iron in transit within hepatocytes did not behave as a single common pool. Ferritin 59Fe, entering a pool of non-radioactive iron the size of which is determined by liver iron stores, was chelated predominantly into the bile. Transferrin 59Fe was distinguished by a greater reflux to the erythron in iron deficient rats, and by excretion of a larger proportion of 59Fe chelated by DF in the urine. Haemoglobin-haptoglobin 59Fe followed a metabolic pathway which was relatively independent of both the iron stores and DF. If the heterogeneous behaviour of rat hepatocyte transit iron has a parallel in man, alterations in the size of similar chelatable iron pools could explain the dependence of DF-induced urine and faecal iron excretion on both liver iron stores and the level of erythropoiesis.
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PMID:Hepatocyte iron kinetics in the rat explored with an iron chelator. 712 64

Hemolysates, prepared from guinea pig reticulocytes incubated with 59Fe-labelled serum, can be resolved into five peaks utilizing molecular sieve chromatography: ferritin, transferrin, hemoglobin, an Mx 17 000 fraction, and a low molecular weight fraction. The hemoglobin peak also contains a nonhemoglobin component (III-X), demonstrated by heme extraction and by isoelectric focusing. Transferrin, the III-X component and the low molecular weight fraction are the first to accumulate radioactive iron during the reticulocyte incubation. The 59Fe in each of these also chases. Therefore, a role for these components as precursors to iron incorporation into heme is suggested.
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PMID:Early events in guinea pig reticulocyte iron uptake. 722 22

Ferritin concentrations in cord blood were determined in 22 normal term and 32 preterm infants (birth weights 600-2000 g). Eight of the preterms were SGA infants. AGA preterm infants had significantly lower concentrations than term infants, and the SGA preterm newborn had even lower levels. Plasma ferritin in cord blood of the term and AGA preterm infants correlated positively with plasma iron and transferrin saturations, but not with the transferrin level, while plasma iron and transferrin concentrations correlated positively. In a longitudinal study, 17 AGA preterm infants (birth weights 850-1500 g) were followed during the early anaemia of prematurity. Iron was supplemented from 4 weeks of age. Plasma ferritin rose rapidly during the first days after birth, peak levels being reached at 1-4 weeks. Thereafter linear falls (semilog) occurred with similar slopes in different infants. Transferrin concentrations showed a slow progressive increase from 0-8 weeks. Plasma ferritin, after reaching the peak value, correlated negatively with weight gain. No infant had low ferritin values indicating iron deficiency during the early anaemia.
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PMID:Plasma ferritin concentrations in preterm infants in cord blood and during the early anaemia of prematurity. 723 84

Iron studies were performed in 22 pregnant and 18 non-pregnant women with haemoglobinopathies. Mean packed cell volume and mean haemoglobin concentration were significantly lower (p < 0.001) in haemoglobin SS patients than in haemoglobin SC patients, in both the pregnant and non-pregnant groups. Transferrin saturation was significantly lower in pregnant patients (haemoglobin SS and SC) than in the non-pregnant group (p < 0.001). Serum ferritin values in the haemoglobin SS and SC pregnant patients were not significantly different (p > 0.05). There was a strong correlation between serum ferritin levels and transferrin saturation in the pregnant group (r = 0.71; p < 0.001). Fourteen of the 22 pregnant women (63 per cent) and 9 of the 18 non-pregnant women (50 per cent) had scanty or no iron in the bone marrow; the serum ferritin levels increased progressively with greater amount of haemosiderin in the bone marrow. There was evidence of iron deficiency in both the pregnant and non-pregnant women with haemoglobinopathies and this suggests the need for further study on the routine administration of iron in the management of patients with sickle cell disease.
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PMID:Iron studies in pregnant and non-pregnant women with haemoglobin SS or SC disease. 743 71

An immunohistochemical study was performed to investigate the presence of alpha-1-antitrypsin (alpha 1-AT), alpha-1-antichymotrypsin (alpha 1-ACT), transferrin and ferritin in 32 ameloblastomas and to evaluate the co-expression of these antibodies. Histologically, we recognized the following 6 patterns in the series of 32 ameloblastomas and at least 2 patterns in variable proportions were present in each of our cases: follicular pattern (21 cases, 66%), plexiform pattern (17 cases, 53%), cystic pattern (21 cases, 66%), acanthomatous pattern (10 cases, 31%), granular cell type (2 cases, 6%), and hyalinized stromal pattern (20 cases, 63%). Neoplastic epithelia of cystic pattern were divided into superficial cell, basal cell and whole layer to compare the immunohistochemical localization. The results made on the various patterns of ameloblastomas were as follows: (1) alpha 1-AT positivity in plexiform, cystic and hyalinized stromal patterns was significantly higher than that of alpha 1-ACT (P < 0.05). (2) The incidence of transferrin in follicular and plexiform patterns was markedly higher than that of ferritin in the same patterns (P < 0.025 and P < 0.01). Transferrin strongly stained metaplastic squamous cells of acanthomatous pattern and basal cells of cystic epithelium. (3) Granular cells reacted with transferrin and ferritin. (4) In follicular and acanthomatous patterns, coexpression of alpha 1-AT and alpha 1-ACT, alpha 1-AT and transferrin, or alpha 1-ACT and transferrin was higher than that of another combination. On the other hand, co-expression of alpha 1-AT and transferrin in plexiform and cystic patterns was higher than that of other antibodies. These results of co-expression of 4 antibodies used in the present study, suggest that the histogenesis of follicular and acanthomatous patterns is different from that of plexiform and cystic patterns.
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PMID:Immunohistochemical detection of alpha 1-antitrypsin, alpha 1-antichymotrypsin, transferrin and ferritin in ameloblastoma. 749 17

Inadequate iron supply is probably the most common and most easily treated cause of sub-optimal response to recombinant human erythropoietin (r-HuEPO). A low ferritin value is a reliable indicator of iron deficiency, provided that patients are in equilibrium (e.g. without infection, bleeding, vitamin or folate deficiency). Normal or high ferritin values do not necessarily preclude iron deficiency. Transferrin saturation is not always a reliable indicator of iron deficiency. The measure which best reflects iron supply to the erythron is the percentage of hypochromic red cells. Iron supplementation should be targeted at keeping serum ferritin > 100 micrograms/l, transferrin saturation > 20%, and hypochromic red cells < 10%. Iron status should be monitored monthly for the first few months after initiation of r-HuEPO, and thereafter at 2-3 month intervals. For haemodialysis patients, who have a very high rate of iron loss, i.v. iron administration is preferable and may also be appropriate for patients on continuous ambulatory haemodialysis (CAPD) and pre-dialysis patients. Recent studies with i.v. iron supplementation have shown no difference between the s.c. and i.v. routes of administration of r-HuEPO. Both the i.v. and the s.c. route are appropriate for patients on haemodialysis, whereas patients on CAPD or pre-dialysis patients should receive s.c. r-HuEPO. The optimum frequency of s.c. administration in the vast majority of patients is 2-3 times weekly. For a small number of patients, once weekly s.c. administration may be suitable. When satisfactory haemoglobin values are reached, the dose of r-HuEPO should be titrated down gradually. It should not be stopped abruptly unless there are life-threatening complications.
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PMID:How to get the best out of r-HuEPO. 764 13

The purpose of this study was to evaluate the sensitivity and specificity of laboratory methods in the diagnosis of posterythropoietin-era, iron-deficient, chronic renal failure patients. The patient population comprised 25 anemic (hemoglobin < 11 g/dL) patients with creatinine greater than 3 mg/dL; 20 were dialysis patients, two were transplant patients, and three patients had renal failure from other causes. Criteria for study inclusion were as follows: bone marrow iron was the reference standard and was graded 0 to +4, ranging from absent to diffuse homogeneous iron staining; serum ferritin concentration and serum transferrin saturation were tested in terms of sensitivity and specificity. The reference standard indicated that iron deficiency existed in 40% of patients. Neither serum ferritin nor transferrin saturation were completely adequate diagnostic tools. Serum ferritin levels less than 200 ng/dL were 100% specific for the diagnosis but only 41% sensitive. Transferrin saturation of less than 20% was 88% sensitive, but only 63% specific. By excluding patients with hypoproteinemia (transferrin values of < 150 mg/dL), the sensitivity of the test increased to 100% and the specificity to 80%. We conclude that transferrin saturation is an adequate screening tool in anemic chronic renal failure patients, provided that hypoproteinemia is not present. By determining both the serum ferritin concentration and the transferrin saturation, a high sensitivity and specificity can be achieved, even in patients with hypoproteinemia. Furthermore, we believe that on this basis, iron therapy in patients with renal insufficiency can be improved.
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PMID:Diagnosis of iron deficiency anemia in renal failure patients during the post-erythropoietin era. 862 43


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