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)

Tiratricol has been used to suppress pituitary TSH secretion, with reported attenuation of extrapituitary thyromimetic effects. A randomized, double-blind trial was performed to define precisely the tissue-specific thyromimetic actions of tiratricol. Ten athyreotic patients, treated for thyroid carcinoma, were randomly assigned to receive L-T4 sodium 0.7 micrograms/kg daily and either tiratricol 10 micrograms/kg or placebo twice daily. The daily dose of L-T4 was increased by 25-50 micrograms increments until the TRH-stimulated TSH level was less than 0.1 mU/L. After measurement of biochemical and physiological parameters of thyroid hormone actions, patients crossed treatment groups. Patients required 46% less L-T4 to achieve equivalent TSH suppression when taking tiratricol. Hepatic effects were enhanced by tiratricol administration, with significant increases in sex hormone binding globulin and ferritin concentrations, 14% and 37%, respectively. Levels of serum cholesterol, LDL cholesterol, and apolipoprotein B were reduced by 7%, 10%, and 13%, respectively, during tiratricol therapy. Triglyceride levels also declined, but there were no changes of high density lipoprotein cholesterol or apolipoproteins AI and AII. Resting metabolic rate, body weight, urea nitrogen excretion, and symptoms did not differ between the two treatment regimens. Cardiovascular function, as reflected by mean arterial pressure and pulse wave arrival time, was not different during tiratricol therapy. Skeletal metabolic activity was affected by tiratricol, with marked elevation of osteocalcin without significant change in serum calcium, PTH, and urinary calcium and hydroxyproline excretion. Tiratricol has increased hepatic and skeletal actions of potential therapeutic value, but does not have enhanced thyromimetic activity specific to the pituitary gland.
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PMID:Organ-specific effects of tiratricol: a thyroid hormone analog with hepatic, not pituitary, superagonist effects. 151 83

Red cells (RBCs) of individuals with the In(Lu) gene are characterized by suppression of the Lutheran, P1, i, and other blood group antigens, acanthocytosis, and abnormal electrolyte metabolism. To determine the clinical significance of these abnormalities, the survival of autologous RBCs was determined by 51Cr in two siblings with the dominant Lu(a-b-) [In(Lu)] phenotype. Both subjects studied had normal hemoglobin, hematocrit, reticulocyte count, haptoglobin, and ferritin values. RBC indices were mildly hypochromic. Examination of the peripheral smear showed mild acanthocytosis in one individual. Analysis of RBC distribution on discontinuous density gradients showed a shift to lighter fractions than normal control RBCs. Storage of these Lu (a-b-) RBCs at 4 degrees C showed significant hemolysis within a few days; this was confirmed by increased autohemolysis, which was reduced by glucose and ATP. RBC cation content (sodium and potassium) was higher than that in control cells, which indicated increased cell hydration, which explains the lighter density and mild hypochromia of the Lu(a-b-) RBCs. 51Cr survival of autologous Lu(a-b-) RBCs was normal in both subjects studied. The data indicate that the morphologic and cation abnormalities of RBCs of persons with the In(Lu) gene are clinically insignificant, as these cells have normal in vivo survival. Such RBCs, however, are susceptible to increased hemolysis in vitro under standard blood banking storage conditions. Individuals of the Lu(a-b-) phenotype, associated with In(Lu), may not be suitable candidates for routine blood donation.
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PMID:In vitro storage and in vivo survival studies of red cells from persons with the In(Lu) gene. 151 24

Sodium chloride stimulated catalysis of oxidation of phosphatidylcholine liposomes by the soluble fraction of mackerel muscle. Chloride was determined to be the active component of the salt in this system. Sulfate also stimulated lipid oxidation. No difference was observed with either anion among sodium, potassium, or lithium cations. Redox iron was involved in the chloride stimulation of lipid oxidation by the press juice. Part of the chloride stimulation of the press juice was mediated through the high molecular weight (greater than 5 kdalton) fraction. Chloride improved the pro-oxidative effect of ascorbate on rat liver ferritin in vitro. It did not appear that production of chlorine radical by peroxidase was involved in the stimulatory effect of chloride.
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PMID:Effect of NaCl on catalysis of lipid oxidation by the soluble fraction of fish muscle. 153 69

Transfer factor activities have been studied in both clinical and basic science settings for several decades. Until now, highly purified transfer factors that are suitable for molecular analysis have not been available. This has impeded progress towards understanding the molecular and cellular basis of the activities of these important inducers of cell-mediated immune responses. Murine transfer factors with specificities for chicken egg albumin or horse spleen ferritin were purified to virtual homogeneity using a combination of affinity chromatography and reversed-phase and polytypic high performance liquid chromatography (hplc). Transfer factors prepared by this methodology were recovered in high yield and in biologically-active, antigen-specific forms. The purified materials were further analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis, chromatographic methods and an in vivo assay for immunological activity. For the first time definitions for unit transfer factor activity and specific activity are introduced. The results of these experiments indicate that transfer factors are a family of highly polar, hydrophilic molecules of low molecular weight (approximately 5,000) which are produced in small quantities by lymphoid cells and which have potent biological activity. The availability of purified transfer factors should facilitate definitive studies into the nature and mechanisms of production and action of these molecules.
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PMID:Purification of transfer factors. 154 96

After fractionation of mitochondrion-free extracts of Xenopus laevis and Rana temporaria oocytes in sucrose gradients, a distinct peak of adenosine triphosphate (ATP)/guanosine triphosphate (GTP)-binding activity in the 50-70 S range has been detected. This substance has a boyant density in Cs2SO4 of 1.45 g/cm3. The nucleotide-binding substance has been purified to apparent homogenety. By means of electron microscopy, sodium dodecyl sulfate-electrophoresis and other methods it has been identified as ferritin.
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PMID:The main adenosine triphosphate-binding component of amphibian oocytes is ferritin. 156 27

The virulence of three avian strains of Pasteurella multocida was evaluated in mice. Strains P-1059I (serotype A:3) and its uncapsulated variant P-1059B and strain 2723 (serotype A:16) were compared. Capsular material thickness after polycationic ferritin labelling of dextrose starch agar (DSA)-grown P. multocida was shown to vary with the strain and was not always related to virulence. Addition of alpha,alpha' bipyridyl (BIP) (160 microM) to the culture medium did not affect capsule production but increased virulence of strains P-1059B and 2723. None of the strains tested showed dermonecrotic activity. Using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), outer membrane protein (OMP) profiles indicated for strains P-1059I and P-1059B three proteins of 30, 35, and 38 KDa with the 30 KDa protein being the major one. Strain 2723 showed the same OMP profile but the 38 KDa protein was the major one. DSA + BIP-grown strains showed the same OMP profiles. Whole cell profiles were similar for all strains tested. However, addition of BIP to the culture media increased the virulence of strains P-1059B and 2723 and for all strains a 39 KDa protein was induced by the iron chelator. The results indicate that encapsulation may be important for virulence, but other surface components such as OMPs may be required as well.
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PMID:Cell surface characteristics and virulence in mice of Pasteurella multocida. 157 5

The uptake and intracellular metabolism of radiolabeled ferritin in rat hepatocytes were investigated. A receptor assay performed by incubating isolated hepatocytes with 125I-labeled ferritin at 37 degrees C for 1 h revealed 37,000 ferritin binding sites/cell with an affinity constant (Ka) of 1.8 X 10(9) M-1. The hepatocytes preincubated with 125I-labeled ferritin at 37 degrees C for 1 h were further incubated in a ligand-free medium at 37 degrees C for 4 h, and then the distribution of the label in the subcellular fractionations of hepatocytes was analyzed by 30% Percoll density gradient centrifugation. The label was transported from the plasma membrane fraction to the lysosome/mitochondria fraction and the cytosol fraction. Meanwhile, both of trichloroacetic acid (TCA)-soluble and TCA-precipitable 125I in the incubation medium increased with the incubation time. In order to study the intracellular metabolism of endocytosed ferritin, the hepatocytes preloaded with 59Fe-125I-double labeled ferritin were incubated at 37 degrees C for 4 h in the ligand-free medium containing 100 mumol/l chloroquine (a lysosomal metabolic inhibitor) or 10 mmol/l sodium cyanide (a mitochondrial metabolic inhibitor). Chloroquine increased TCA-precipitable 125I in the medium with a corresponding decrease in TCA-soluble 125I. However, no effect with sodium cyanide was observed. Radioactivities in the incubation medium were then divided into two components by HPLC gel filtration. One had a molecular weight similar to intact ferritin, 98% of which reacted to an anti-rat liver ferritin antiserum, while the other had a molecular weight of less than 1,000, 25% of which reacted to the antiserum. Chloroquine increased the amounts of intact ferritin released into the medium and decreased the degraded fragments. These results suggest two pathways of the endocytosed ferritin in hepatocytes; one is a degradation of ferritin in lysosome, which results in a storage of iron in the cells and an excretion of degraded peptides outside the cells, and the other is exocytosis of intact ferritin from the cells by a similar mechanism to "diacytosis" proposed for asialoglycoprotein.
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PMID:[Uptake and intracellular metabolism of ferritin by primary cultured rat hepatocytes]. 165 94

The efficiency of semi-dry electrophoretic transfer after sodium dodecyl sulfate (SDS)-electrophoresis using PhastGel media was investigated in a model system using three isotope labelled proteins. To give a full picture of the blotting process the amount of protein present in the gel, membranes, and filter papers was determined after different transfer times. The influence of the transfer buffer, commonly used additives such as methanol and SDS, and several different immobilizing matrices was investigated. Soybean trypsin inhibitor, bovine serum albumin, and ferritin were used as model proteins to study the effect of size on transfer efficiency. Basically, all three stages of the blotting process decide the result; the elution of protein from the gel, the immobilization of protein to the membrane, and the loss of material from the membrane during transfer. A theoretical explanation for the observed poor binding to a second membrane is discussed. Our results show that the buffer composition has little influence on the efficiency of transfer from the gel, but can be significant to the binding capacity of the membrane. In all experiments performed, there was never one moment during the transfer when all protein was eluted from the gel and simultaneously still bound to the membrane. The highest recovery in the membrane was obtained at different time intervals for different proteins. This indicates that quantitative transfer procedures cannot be generalized. However, obtaining an optimal method for reliable quantification of a specific protein or group of proteins is possible. For general protein staining of nitrocellulose and polyvinylidene difluoride membranes, a highly sensitive silver staining method requiring only 15 min has been used.
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PMID:Important parameters in semi-dry electrophoretic transfer. 169 Jun 43

Iron absorption by intestinal epithelial cells, passage onto plasmatic apotransferrin, and regulation of the process remain largely misunderstood. To investigate this problem, we have set up an in vitro model, consisting in CaCo2 cells (a human colon adenocarcinoma line, which upon cultivation displays numerous differentiation criteria of small intestine epithelial cells). Cells are cultivated in a serum-free medium, containing 1 microgram/ml insulin, 1 ng/ml epidermal growth factor, 10 micrograms/ml albumin-linoleic acid, 100 nM hydrocortisone, and 2 nM T3 on new, transparent, Cyclopore polyethyleneterephthalate microporous membranes coated with type I collagen. Cells rapidly adhere, grow, and form confluent monolayers; after 15 days, scanning electron microscopy reveals numerous uniform microvilli. Domes, which develop on nonporous substrata, are absent on high porosity membranes. Culture medium from upper and lower compartments of microplate inserts and cell lysates were immunoprecipitated after labeling with [3H]glucosamine and leucine; analysis was done by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by autoradiography. [3H]transferrin is found mainly in the lower compartment and in cells; [3H]apolipoprotein B is released in both compartments, and fibronectin almost entirely recovered in the lower compartment; [3H]transferrin receptors and ferritin are only present in cell lysates. Binding experiments also show that transferrin receptors are accessible from the lower compartment. These results suggest that CaCo2 cells, cultivated in synthetic medium on membranes of appropriate porosity, could provide an in vitro model of the intestinal barrier, with the upper compartment of the culture insert corresponding to the apical pole facing the intestinal lumen and the lower one to the basal pole in contact with blood.
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PMID:Iron absorption by intestinal epithelial cells: 1. CaCo2 cells cultivated in serum-free medium, on polyethyleneterephthalate microporous membranes, as an in vitro model. 183 Mar 3

Medical examinations related to iron nutrition (hemoglobin concentration, serum ferritin concentration and transferrin saturation) and measurements of daily nutriment intakes based on three day dietary records were carried out for 440 female subjects from adolescence to menopause, and the relationships between both parameters were compared. The subjects could be reasonably divided into 3 age groups of menstruating I (17-29 years), II (30-53 years) women and menopausal (48-69 years) women by the one-way analysis of variance. The occurrence of iron deficiency including iron deficient anemia was above 45% both in menstruating I and menstruating II women. In addition, the average amounts of iron intake were 8.7 and 10.2 mg/day in these groups, respectively. These values were below the recommended intake of iron (12 mg/day) for females of these ages in Japan. In menopausal women, the occurrence of iron deficiency decreased to 11.3%, which corresponded to the increase of average iron intake to 11.2 mg/day. Irrespective of age groups, there were almost no significant correlations between the results of medical examinations and the amounts of daily iron intake. Although no improvement in hemoglobin concentration and transferrin saturation was observed in 62 menstruating women, who received 10 mg iron daily as sodium ferrous citrate for 2 months, the average serum ferritin concentrations were significantly increased at 1 and 2 months after the supplement and 2 weeks after they stopped. These therapeutic trials indicate the relationship between iron deficiency and low iron intake in menstruating women.
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PMID:[Relationship between iron nutrition and nutriment intakes in the menstruating and menopausal women]. 188 Jan 99


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