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)

Nonheme iron and ferritin in the bone marrow and serum ferritin was investigated in patients with iron deficiency anaemia or iron overload. As controls served patients without any disturbance of the iron metabolism. There is a precise correlation between the nonheme iron and ferritin in the bone marrow of patients with and without disturbance of iron metabolism. A correlation was also found between the ferritin in the bone marrow and the serum. Nonheme iron and ferritin in the bone marrow and serum ferritin was decreased in patients with iron deficiency anaemia. Conversely, the same parameters were increased in patients with iron overload.
Blut 1978 Sep 15
PMID:Ferritin in bone marrow and serum in iron deficiency and iron overload. 68 38

1. When lead is administered in drinking-water iron-deficient rats retain more Pb than Fe-replete rats (Six & Goyer, 1972; Klauder & Petering, 1975). In the present study the relationship between the absorption of Pb and Fe was investigated. 2. Adult male rats were transfered to a milk-based diet fed with or without supplementary Fe (180 mg Fe/kg as ferrous sulphate). After 7--9 d the absorption of duodenally-administered 203Pb and 59Fe was measured as uptake of radioactivity from the gastrointestinal tract after 90 min. 59Fe absorption was increased in rats given the unsupplemented diet for 7 d and was further increased in rats kept on the diet for up to 7 weeks. 203Pb absorption was not consistently increased by either short- or long-term Fe deprivation. 3. Much of the 203Pb in homogenates of the upper small intestine was bound to soluble protein of which up to 85% was dialysable. In contrast little 59Fe was dialysable. Only a small proportion of the soluble musosal Pb was associated with ferritin during gel-filtration chromatography although 203Pb precipitated together with carrier rat-liver ferritin with an antibody to rat-liver ferritin. 4. There appeared to be no direct relationship between the transfer of Fe and Pb across the small intestine of the adult rat.
Br J Nutr 1978 Sep
PMID:Lead and iron absorption from rat small intestine: the effect of dietary Fe deficiency. 69 63

The inter-relationships between serum ferritin, hemoglobin, serum iron and total body iron stores were studied in 20 patients with chronic renal failure treated conservatively and in 20 patients on regular hemodialysis. There was no relationship between serum iron or transferrin and bone marrow iron deposits, but serum ferritin concentration was a good indicator of increased marrow iron stores. All patients with serum ferritin levels above 300 microgram/l had increased iron stores. Serum ferritin assay is a useful non-invasive technique for detecting iron overload in uremic and hemodialyzed patients.
Clin Nephrol 1978 Sep
PMID:Serum ferritin concentration: a reliable guide to iron overload in uremic and hemodialyzed patients. 69 5

A glycoprotein immunologically related to plasma cold-insoluble globulin (CIG) and fetal skin fibroblast fibronectin has been purified from second-trimester human amniotic fluid. This protein (amniotic fluid fibronectin) migrated more slowly than CIG on sodium dodecyl sulfate gel electrophoresis and showed greater polydispersity which could result, at least in part, from heterogeneity in glycosylation. Cloned human amniotic fluid epithelioid and fibroblastic cells synthesized and secreted a protein with similar properties into the culture medium. Fibronectin was shown to be associated with the pericellular and extracellular matrix of cultured amniotic fluid cells by immunofluorescence, lactoperoxidase-catalyzed iodination, and labeling with ferritin-conjugated antibodies. The kinetics of secretion of the protein were consistent with its role as a matrix protein. We anticipate that amniotic fluid fibronectin will prove to be the same protein which elsewhere in the body is incorporated into connective tissues and basement membranes. Amniotic fluid could, therefore, serve as a convenient source of in vivo synthesized fibronectin for biological and structural studies.
J Cell Biol 1978 Sep
PMID:Amniotic fluid fibronectin. Characterization and synthesis by cells in culture. 70 56

Carbohydrate-containing structures in rat liver rough microsomes (RM) were localized and characterized using iodinated lectins of defined specificity. Binding of [125I]Con A increased six- to sevenfold in the presence of low DOC (0.04--0.05%) which opens the vesicles and allows the penetration of the lectins. On the other hand, binding of [125I]WGA and [125I]RCA increased only slightly when the microsomal vesicles were opened by DOC. Sites available in the intact microsomal fraction had an affinity for [125I]Con A 14 times higher than sites for lectin binding which were exposed by the detergent treatment. Lectin-binding sites in RM were also localized electron microscopically with lectins covalently bound to biotin, which, in turn, were visualized after their reaction with ferritin-avidin (F-Av) markers. Using this method, it was demonstrated that in untreated RM samples, binding sites for lectins are not present on the cytoplasmic face of the microsomal vesicles, even after removal of ribosomes by treatment with high salt buffer and puromycin, but are located on smooth membranes which contaminate the rough microsomal fraction. Combining this technique with procedures which render the interior of the microsomal vesicles accessible to lectins and remove luminal proteins, it was found that RM membranes contain binding sites for Con A and for Lens culinaris agglutinin (LCA) located exclusively on the cisternal face of the membrane. No sites for WGA, RCA, soybean (SBA) and Lotus tetragonobulus (LTA) agglutinins were detected on either the cytoplasmic or the luminal faces of the rough microsomes. These observations demonstrate that: (a) sugar moieties of microsomal glycoproteins are exposed only on the luminal surface of the membranes and (b) microsomal membrane glycoproteins have incomplete carbohydrate chains without the characteristic terminal trisaccharides N-acetylglucosamine comes from galactose comes from sialic acid or fucose present in most glycoproteins secreted by the liver. The orientation and composition of the carbohydrate chains in microsomal glycoproteins indicate that the passage of these glycoproteins through the Golgi apparatus, followed by their return to the endoplasmic reticulum, is not required for their biogenesis and insertion into the endoplasmic reticulum (ER) membrane.
J Cell Biol 1978 Sep
PMID:Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. I. Localization of lectin-binding sites in microsomal membranes. 70 63

1. Human liver ferritin was separated by preparative isoelectric focusing into six fractions. 2. Except for the least acidic fraction the reactivity with antibody against spleen ferritin increased with rising pI, but with antibody against heart ferritin the reactivity decreased. 3. The highest iron content was found in the most acidic isoferritins and progressively decreased with rising pI. 4. Iron uptake was studied in apoferritin prepared from heart and liver ferritin fractions separated by ion-exchange chromatography. There was good correlation between the rate of iron uptake and pI. The most acidic fractions took up iron more rapidly than did the more basic ones. 5. Ferritin was prepared from heart, liver, spleen and kidney. There was little difference on isoelectric focusing between ferritin obtained from normal tissues and the corresponding iron-loaded tissues from patients who had received multiple blood transfusions. The iron-loaked heart ferritin invariably contained relatively more of the basic isoferritins. Normal and iron-overloaded heart ferritins were separated into isoferritin fractions by ion-exchange chromatography, and in each case there was a fall in iron content as the pI increased. The iron content of ferritin from the iron-overloaded heart was higher throughout than that from normal heart. 6. There is a relationship between the rate of iron uptake by apoferritin and pI, and this probably accounts for the variation in iron content of the isoferritins found in human liver and heart.
Biochem J 1978 Sep 01
PMID:Properties of human tissue isoferritins. 70 84

Dihydroflavins reductively release iron rapidly and quantitatively from purified horse spleen or horse heart ferritin. The NAD(P)H:flavin oxidoreductase from Beneckea harveyi is used to generate a constant concentration of dihydroflavin permitting a continuous assay for complete iron release. Sepharose-linked dihydroflavins are not competent to release ferritin iron, demonstrating that the dihydroflavin must pass through the channels of the protein shell prior to iron reduction. Several experiments fail to show any specific flavin binding site, though dihydroflavins do display saturation kinetics with very high apparent Km's. The rates of iron release by a number of dihydroflavin analogues show that the electron transfer is significantly rate determining in iron release by dihydroriboflavin, while diffusion of the dihydroflavin through the protein channel is slow in the release of iron by dihydroFMN. The rate of iron release is also dependent on the initial content of iron, having a maximum at 1200 iron atoms per ferritin.
Biochemistry 1978 Sep 19
PMID:Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues. 70 92

Liver depot iron can be divided into two fractions: ferritin iron and non-ferritin depot iron. Three methods intended to measure the non-ferritin depot iron in the rat liver were compared using livers of normal rats and livers of rats loaded with iron by transfusion of erythrocytes. Liver depot iron varied between 75 and 850 microgram Fe/g liver. Non-ferritin depot iron, measured as the iron fraction sedimentable at 10 000 x g, was in the range 4--22 microgram Fe/g liver. This fraction did contain ferritin. When measured as the difference between total liver depot iron and heat-stable iron (ferritin iron), the range was 10--270 microgram Fe/g liver but this fraction also includes some ferritin iron. The values derived with both methods were linearly proportional to the total liver depot iron values. Non-ferritin depot iron, when measured as the difference between total liver depot iron and total ferritin iron, ranged from 0 to 190 microgram Fe/g liver. In this last method no ferritin iron is included. This method provides the best estimate of the non-ferritin depot iron fraction. The concentrations obtained with this method were not always linearly proportional to the total liver depot iron concentration. Intravenous injection of rat liver ferritin resulted in a rapid accumulation of ferritin iron in the liver, together with an increase of the non-ferritin depot iron fraction from 18 microgram Fe/g liver to 55 microgram Fe/g liver. This confirms a relationship between ferritin catabolism and the non-ferritin depot iron fraction.
Biochim Biophys Acta 1978 Sep 21
PMID:On the non-ferritin depot iron fraction in the rat liver. 70 85

ZGM was purified from both primary and metastatic colonic carcinomas demonstrably positive for ZGM by immunofluorescence microscopy. ZGM purification included preparative Pevikon electrophoresis, Sepharose 4B molecular exclusion chromatography and Con A-Sepharose affinity chromatography. ZGM had an alpha2 electrophoretic mobility, an estimated molecular weight by Sepharose 4B equal to or greater than 2 x 10(6), and did not bind to Con A-Sepharose, although having determinants with CEA-like activity. Its immunologic activity was resistant to trypsin or phospholipase A but not to neuraminidase. Antisera prepared to ZGM and absorbed with saliva, when tested by double immunodiffusion, formed a single precipitation line with saline extracts of colon tumors and did not cross-react with CEA, AFP, normal tissue extracts, ferritin, NCA, NCA-2, CSAp, blood groups A, B, H, Lewis antigen, or buffy coat, alpha-2 macroglobulin, saliva or ovarian cyst fluid. Immunofluorescence microscopy confirmed the presence of ZGM in 40 out of 45 adenocarcinomas of the GI tract staining primarily in tumors, the apical cytoplasm, and in grossly nonmalignant tissues, the deep crypts of the villi, while all of 22 non-GI tumors in the study were ZGM negative.
Cancer 1978 Sep
PMID:Present status of the zinc glycinate marker (ZGM). 70 28

Purified human spleen ferritin was labelled with 125I. On Sepharose 6-B gel filtration four species of labelled products were separated: a component with a higher molecular weight than ferritin; a component which is eluted in the same volume as unlabelled ferritin; and two labelled compounds with molecular weights lower than ferritin. When these labelled materials were used in a double antibody radioimmunoassay, the high molecular weight fraction showed variable and high non-specific binding and was poorly displaced by unlabelled ferritin; the fraction behaving like true ferritin gave good standard curves and showed non-specific binding of less than 1%. The remaining two components showed poor binding to rabbit antiferritin. Using labelled material from the second fraction, a double antibody radioimmunoassay capable of measuring 2 microgram ferritin protein/litre of serum was developed. Inter- and intra-assay variation was between 3% and 8% over a concentration range of 0 to 250 microgram ferritin protein/litre. Good agreement between serum ferritin levels assayed by the present method and by an immunoradiometric method was obtained. Labelled ferritin was stable for at least six weeks. The simplicity of the methodology makes it possible to assay serum ferritin in large batches.
J Clin Pathol 1978 Sep
PMID:Radioimmunoassay of serum ferritin. 71 18


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