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)

We examined the value of transferrin concentrations in estimating nutritional status as determined by the subjective global assessment (SGA) score. Fifty-nine hemodialysis patients (37 men and 22 women, aged 59+/-16 years, dialyzed for 3.6+/-3.9 years) were selected by predetermined criteria. All received erythropoietin (EPO) and oral iron therapy. SGA evaluation was conducted twice by both a dietitian and a physician. Serum iron, total iron-binding capacity (TIBC; which is linearly correlated with transferrin), transferrin saturation ratio, ferritin, albumin, total protein, and cholesterol were measured. Twenty-seven (46%) patients were well nourished (group A), 20 (34%) were moderately nourished (group B), and 12 (20%) were poorly nourished (group C) according to the SGA. TIBC values were 276+/-47 mg/dL, 217+/-54 mg/dL, and 176+/-41 mg/dL, respectively (P < 0.00001), and thus directly correlated with the state of nutrition. The relationship between TIBC and nutritional status was independent of age and number of years on hemodialysis. Serum ferritin values were 104+/-93 ng/mL, 161+/-154 ng/mL, and 363+/-305 ng/mL, respectively (P < 0.0003), and thus inversely correlated with the state of nutrition. Transferrin saturation ratios were slightly higher in the severely malnourished patients. The number of years on dialysis were a determinant of nutritional status. These values were 2.4+/-2.4 years for group A, 3.9+/-4.0 years for group B, and 5.7+/-3.9 years for group C (P < 0.05). The average age of the poorly nourished patients was 10 years older than the well-nourished patients. Serum iron values were lower but transferrin saturation ratios were higher in the severely malnourished patients. The required EPO doses were higher in the poorly nourished patients. We suggest that transferrin values are superior to other laboratory tests in assessing nutrition and will supplement SGA criteria. Serum ferritin may be useful as a predictor of illness. Older patients who have been on dialysis longer warrant special concern. Malnutrition may be an indicator of EPO resistance in dialysis patients. Finally, since a decreased TIBC level in poorly nourished patients may erroneously increase the transferrin saturation ratio, our findings may have implications in making the diagnosis and treatment of anemia and iron deficiency in malnourished dialysis patients.
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PMID:Total iron-binding capacity-estimated transferrin correlates with the nutritional subjective global assessment in hemodialysis patients. 946 97

The distribution and development of transferrin-positive cells in the pons and cerebellum of human fetuses to adults were examined immunohistochemically, compared with those of ferritin-positive cells. Transferrin was present in oligodendrocytes, astrocytes, and neurons. Transferrin-positive neurons appeared at 18 weeks of gestation in Purkinje cells and the pontine reticular formation. In the pontine nuclei, transferrin-positive neurons appeared at 22 weeks of gestation. On the other hand, transferrin-positive glia also appeared at 18 weeks of gestation in the reticular formation, and at 24 weeks of gestation in the cerebellar white matter and pontine nuclei. Transferrin-positive glia and cells appeared earlier in the reticular formation of the pons than ferritin, but the order of its appearance was similar to that of ferritin and myelination. Because iron is involved in the syntheses and functions of dopamine, serotonin, and gamma-aminobutyric acid (GABA), transferrin may be carried for various iron uses from an early fetal stage.
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PMID:Immunocytochemical development of transferrin and ferritin immunoreactivity in the human pons and cerebellum. 951 4

The exact mechanisms of iron transport from endosomes to the target iron containing cellular proteins are currently unknown. To investigate this problem, we used the gradient gel electrophoresis and the sensitive detection of 59Fe by autoradiography to detect separate cellular iron compounds and their iron kinetics. Cells of human leukemic line K562 were labeled with [59Fe]transferrin for 30-600 s and cellular iron compounds in cell lysates were analyzed by native electrophoretic separation followed by 59Fe autoradiography. Starting with the first 30 s of iron uptake, iron was detectable in a large membrane bound protein complex (Band I) and in ferritin. Significant amounts of iron were also found in labile iron compound(s) with the molecular weight larger than 5000 as judged by ultrafiltration. Iron kinetics in these compartments was studied. Band I was the only compound with the kinetic properties of an intermediate. Transferrin, transferrin receptor and additional proteins of the approximate molecular weights of 130000, 66000 and 49000 were found to be present in Band I. The labile iron compounds and ferritin behaved kinetically as end products. No evidence for low molecular weight transport intermediates was found. These results suggest that intracellular iron transport is highly compartmentalized, that iron released from endosomal transferrin passes to its cellular targets in a direct contact with the endosomal membrane complex assigned as Band I. The nature of the labile iron pool and its susceptibility to iron chelation is discussed.
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PMID:Iron transport in K562 cells: a kinetic study using native gel electrophoresis and 59Fe autoradiography. 963 Jun 20

Multiple cell types contribute to the pulmonary barrier including Type I and Type II alveolar epithelium. The objective of this research was to establish and characterize an in vitro model of Type II alveolar epithelium using the A549 human lung adenocarcinoma cell line. A549 cells form confluent monolayers with Type II characteristic morphology and tannic acid staining for typical lamellar bodies. A549 cells possess P450 IA1 and P450 IIB6 as determined by Western blots. Both CYPIA1 and CYPIIB6 P450 isozymes were determined to be functional with the fluorescent resorufin assay. Only the IA1 isozyme was observed to be inducible with selected polycyclic hydrocarbons. Uptake and transport experiments were carried out in cluster plates and in Snapwells. Cationized ferritin, a nonspecific absorbtive marker, was found to be taken up by the cells in a concentration-, time-, and temperature-dependent fashion. Lucifer yellow, a fluid-phase marker, was not internalized by the A549 cells. Transferrin, a representative receptor-mediated endocytic marker, was found to be taken up by the cells in a concentration-dependent and competitive fashion. Transport experiments involving fluorescein-transferrin also showed that A549 monolayers were polarized, with a greater amount of intracellular transferrin being transported out of the basolateral side of the cells. The experimental data agree favorably with literature for primary cultures of Type II pulmonary epithelial cells. These results indicated that the A549 cell line may be useful for the studying the metabolic and macromolecule processing contributions of alveolar Type II cells to mechanisms of drug delivery at the pulmonary epithelium.
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PMID:Characterization of the A549 cell line as a type II pulmonary epithelial cell model for drug metabolism. 974 95

Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. As Tf transport through the brain barriers is restricted, Fe is probably released into the brain extracellular compartment as non-Tf-bound iron (NTBI). To evaluate NTBI in the brain and cerebrospinal fluid (CSF), different aged rats (P15, P20, P56) were injected intravenously with [59Fe-125I]Tf followed by sampling of CSF and brain tissue. Between 80 and 93% of 59Fe in CSF was absorbed with anti-Tf and 1 and 5% with anti-ferritin antibodies. The fraction of 59Fe from CSF passing through a 30,000 molecular weight (MW) cutoff filter was approximately 5% (P15), 10% (P20), and 15% (P56). Measurements of Fe and Tf concentrations in CSF of P20 rats revealed that the Fe-binding capacity of Tf was exceeded. In the supernatants of brain homogenates, between 94 and 99% of 59Fe was absorbed with anti-Tf and anti-ferritin antibodies. The respective fractions of 59Fe in the supernatants passing through the 30 kD cutoff filter were 4% (P15), 2% (P20), and 6% (P56). In brain homogenates mixed before filtering with desferroxamine (DFO) or nitrilotriacetic acid (NTA) which complex loosely protein-bound Fe and non-protein-bound Fe, these 59Fe fractions were 2-fold higher. The results indicate that NTBI is present extracellularly in CSF and probably in brain interstitium.
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PMID:Evidence for low molecular weight, non-transferrin-bound iron in rat brain and cerebrospinal fluid. 982 59

Iron is essential for oxidation-reduction catalysis and bioenergetics, but unless appropriately shielded, iron plays a key role in the formation of toxic oxygen radicals that can attack all biological molecules. Hence, specialized molecules for the acquisition, transport (transferrin), and storage (ferritin) of iron in a soluble nontoxic form have evolved. Delivery of iron to most cells, probably including those of the kidney, occurs following the binding of transferrin to transferrin receptors on the cell membrane. The transferrin-receptor complexes are then internalized by endocytosis, and iron is released from transferrin by a process involving endosomal acidification. Cellular iron storage and uptake are coordinately regulated post-transcriptionally by cytoplasmic factors, iron-regulatory proteins 1 and 2 (IRP-1 and IRP-2). Under conditions of limited iron supply, IRP binding to iron-responsive elements (present in 5' untranslated region of ferritin mRNA and 3' untranslated region of transferrin receptor mRNA) blocks ferritin mRNA translation and stabilizes transferrin receptor mRNA. The opposite scenario develops when iron in the transit pool is plentiful. Moreover, IRP activities/levels can be affected by various forms of "oxidative stress" and nitric oxide. The kidney also requires iron for metabolic processes, and it is likely that iron deficiency or excess can cause disturbed function of kidney cells. Transferrin receptors are not evenly distributed throughout the kidney, and there is a cortical-to-medullary gradient in heme biosynthesis, with greatest activity in the cortex and least in the medulla. This suggests that there are unique iron/heme metabolism features in some kidney cells, but the specific aspects of iron and heme metabolism in the kidney are yet to be explained.
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PMID:Cellular iron metabolism. 1008 80

Transferrin and ferritin cDNAs have been isolated and characterised from the common brushtail possum (Trichosurus vulpecula), the first marsupial examples of these genes. The transferrin cDNA encodes a 711 amino acid pre-protein which shows high levels of amino acid identity with eutherian transferrins (58-60%) and lactoferrins (54-56%). Phylogenetic analysis suggests that the possum transferrin has evolved independently along a pathway distinct from that of the eutherian transferrins and lactoferrins. Possum H-ferritin is a 182 residue protein which shares 86-94% amino acid identity with mammalian, avian and amphibian sequences. Ferritin mRNA was detected in all tissues tested, whereas transferrin was highly expressed in possum liver and mammary gland, and at lower levels in heart, testis and lung. In the possum mammary gland, ferritin mRNA was expressed throughout lactation with higher levels during the first 30 days which coincides with the high iron concentration of milk at this time. The transferrin gene was differentially expressed during lactation with peak mRNA levels detected during the first 6 days of lactation and after day 106 throughout late lactation. The pattern of transferrin mRNA expression in the mammary gland was identical to that of another whey protein, the late lactation protein, suggesting that the transcription of these genes may be regulated by a similar mechanism in this tissue.
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PMID:Cloning and expression of the transferrin and ferritin genes in a marsupial, the brushtail possum (Trichosurus vulpecula). 1020 59

Genetic predisposition to haemochromatosis may be an important aetiological factor in some cases of Type 2 diabetes. Our aim was therefore to test the hypothesis that the haemochromatosis gene mutations Cys282Tyr and His63Asp are more prevalent in Type 2 diabetic patients compared with the Canterbury, New Zealand general population. We studied 230 consecutive patients referred to the Diabetes Services with age > or = 30 years and considered to have Type 2 diabetes. DNA was extracted from whole blood and amplified by polymerase chain reaction prior to restriction fragment length polymorphism analysis. The frequency of the mutations was compared with that observed previously in 1064 subjects from the Canterbury general population by chi2 testing. Iron was measured by a colorimetric method, transferrin by rate nephelometry and ferritin by immunoassay. There were 2/230 (0.8%) Cys282Tyr homozygous subjects in the diabetic group compared with 5/1064 (0.5%) NS in the general population. Although there was a trend to lower incidence of Cys282Tyr heterozygosity in the diabetic group, there was no significant difference for any of the six genotype frequencies between the two groups. Haemochromatosis gene mutations Cys282Tyr and His63Asp are therefore not increased in Type 2 diabetics compared with the general population. Transferrin saturation was a sensitive marker (100%) of genetic haemochromatosis, although ferritin had low specificity (77.8%). Genetic susceptibility to haemochromatosis is not an important aetiological factor for diabetes, and targeted screening of diabetic patients for haemochromatosis is not indicated.
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PMID:Haemochromatosis gene mutations Cys282Tyr and His63Asp are not increased in Type 2 diabetic patients compared with the Canterbury (New Zealand) general population. 1036 30

The cause of anemia in chronic renal failure is multifactorial. Decreased erythropoietin (EPO) production is the main pathogenetic factor, but iron deficiency is the primary cause of unresponsiveness to EPO therapy. The diagnosis of iron deficiency in patients with chronic renal failure is difficult. We assessed the sensitivity and specificity of serum ferritin, total iron-binding capacity, transferrin saturation index, erythrocyte ferritin, and serum transferrin receptor in 63 patients with chronic renal failure undergoing dialysis (47 men, 16 women) with iron deficiency anemia. They were selected on the basis of clinical stability and absence of factors that may interfere with iron metabolism. None of the patients had received intravenous iron therapy or recombinant human erythropoietin (rHuEPO). Bone marrow biopsy with iron staining was the reference standard for iron stores. The receiver operating characteristic (ROC) curve and the area under the curve were calculated to assess the sensitivity and specificity of iron metabolism parameters. The parameter with the largest area under the ROC curve was serum ferritin (0.83). A cut point of 121 microgram/L showed a sensitivity and a specificity of 75%. The areas under the ROC curves of serum transferrin receptor and erythrocyte ferritin were 0.69 and 0.68, respectively. The remaining parameters showed areas under the ROC curve less than 0.65. Although serum transferrin receptor and erythrocyte ferritin may be acceptable markers for iron deficiency in stable chronic renal failure patients, serum ferritin level continues to be the most reliable diagnostic parameter. Transferrin saturation index is not a reliable parameter for the diagnosis of iron deficiency in stable patients not treated with rHuEPO.
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PMID:Diagnosis of iron deficiency in chronic renal failure. 1046 62

Reactive oxygen species may contribute to airway injury in patients with cystic fibrosis (CF) and iron catalyzes oxidant injury by promoting generation of highly reactive hydroxyl radicals. Iron in the lower respiratory tract may be free, ferritin bound (from which iron can be reductively mobilized), or transferrin bound (which generally prevents iron mobilization). Ferritin is composed of subunits that are heavy (H) or light (L), and H-rich ferritins have additional biologic effects including inhibition of lymphocyte proliferation and cell growth. To assess concentrations of iron and iron-binding proteins in the lower respiratory tract of patients with CF, we measured iron (ferrozine), L-ferritin, H-ferritin, and transferrin (enzyme-linked immunosorbent assay [ELISA]) in bronchoalveolar lavage (BAL) fluid recovered from stable patients with CF (n = 8), healthy nonsmokers (NS; n = 8), or heavy cigarette smokers (HS; n = 8). Iron was detected in BAL fluid from patients with CF and HS, but not NS, with higher iron concentrations in patients with CF (42.0 +/- 11.6 microgram/dl) than in HS (9.9 +/- 2.6 microgram/dl, p < 0.05). Ferritin was present in all BAL fluids, with higher total ferritin (L + H) in patients with CF (647 +/- 84 ng/ml) than in HS (181 +/- 25 ng/ml, p < 0.005) or NS (9 +/- 3 ng/ml, p < 0.0005). Ferritin recovered from HS and NS lungs was < 2% H type, whereas ferritin in CF lungs was > 40% H-type ferritin. Transferrin concentrations in BAL fluid were not different in any group. Tumor necrosis factor (TNF)-alpha was present only in BAL samples from patients with CF. To assess whether TNF-alpha contributed to H-ferritin accumulation in CF lungs, we treated lung epithelial cells (A549) with iron alone (FeSO(4), 10-40 microM) or with iron and TNF-alpha (5-20 ng/ml). Iron-treated A549 cells synthesized almost entirely L-ferritin whereas exposure to TNF-alpha with iron caused a dose-dependent increase in accumulation of H-type ferritin. These findings suggest that oxidant injury could be promoted in lungs of patients with cystic fibrosis by iron mobilized from extracellular ferritin and, in addition, that TNF-alpha-promoted accumulation of H-type ferritin may impair local immune function and cell growth.
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PMID:Increased concentrations of iron and isoferritins in the lower respiratory tract of patients with stable cystic fibrosis. 1047 99


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