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)

A glycoprotein coat was demonstrated on the outer surface of both the uterine and trophoblastic cells using ruthenium red, cationized ferritin, concanavalin A-peroxidase and phosphotungstic acid in HCl. No changes were observed on the uterine epithelial surface of cyclic or pregnant animals before or during blastocyst attachment (Day 15). However, the cytochemical reactions were different on the trophoblastic cells of blastocysts at Days 13 and 15, the ruthenium red and cationized ferritin sites of reaction and the concanavalin A receptors being more homogeneously distributed on the outer surface of Day-15 trophoblast. The phosphotungstic acid staining demonstrated a glycoprotein substance between the trophoblast and the uterine epithelium in adhesion areas by Day 18. The results suggest that biochemical changes occur in the composition or distribution of the trophoblastic cell coat during the process of blastocyst attachment in the ewe.
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PMID:Cytochemical studies of uterine and trophoblastic surface coats during blastocyst attachment in the ewe. 704 64

A 20-day-old human conceptus was studied by the indirect immunoperoxidase technique for the presence of a series of plasma proteins: prealbumin (PA), albumin (ALB), alpha-fetoprotein (AFP), alpha 1-antitrypsin (A1AT), carcioembryonic antigen (CEA), immunoglobulin G (IgG), ferritin (FER), transferrin (TR), fetal haemoglobin (HbF), human chorionic gonadotropin (HCG), human placental lactogen (HPL) and pregnancy specific beta 1-glycoprotein (SP1). In the embryo only FER and TR were found. The yolk sac was positively stained for several proteins: PA, ALB, AFP, A1AT, IgG, FER, TR and HbF were demonstrated in the endodermal cells and PA, ALB, IgG and TR in the mesothelial cells. The syncytiotrophoblast of the chorionic villi were heavily stained for all the placental proteins. HCG and HPL were additionally demonstrated in the cytotrophoblast. The Hofbauer cells of the chorionic and villous stroma stained positively for A1AT and FER. TR appeared as a characteristic band on the apical surface of the syncytiotrophoblast. The findings indicate that the yolk sac is the principle source of some of the plasma proteins also in the very early conceptus and the assumption that the yolk sac is the functional antecedent of the liver is supported. The distribution of the various placental proteins is in accordance with the present knowledge that the syncytiotrophoblast is the major site of synthesis of these proteins. Finally correlation of functional aspects of embryonic structures and germ cell tumours is recommended.
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PMID:An immunohistochemical study of a series of plasma proteins in the early human conceptus. 705 Sep 33

The negative charges on the various trophoblast was investigated, in order to cast light on the biological roles, by electron microscopy using cationized ferritin as an ultrastructural marker, in comparison with surface glycoprotein. The following results were obtained: 1. The surface glycoprotein distributed on the trophoblastic plasma membrane forming regularly situated aggregates, 15 to 20 millimicron in diameter separated by 50 to 100 millimicron from neighboring ones. 2. The negative charge on the cell surface was distributed in two different configurations: A strongly negative part and weakly negative one. 3. The placental villi were revealed to carry an extremely high level of negative surface charge. 4. One maternal lymphocyte in a first trimester pregnancy was calculated to carry a 5.9 x 10(-11) Coulomb negative surface charge. 5. In a simplified model, the electronic repulsive force between the lymphocyte and placental villus was calculated as 5.7 x 10(-4) Newton, showing that the electronegative charge on human trophoblast was strong enough to repel the negatively charged lymphocyte against the lymphocyte gradient. 6. For villi from spontaneous abortion with mild degeneration, the surface glycoprotein was observed to make prominent aggregates on the trophoblastic surface in concomitance with the reduced negative surface charge. 7. With the observation by electron microscopy, The complete mole differed essentially from the partial mole in that former resembled normal villi while the later spontaneous abortion.
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PMID:[Negative surface charge of human trophoblast and its biological role (author's transl)]. 706 54

Antibodies raised against the Sarkosyl-insoluble, major flagellar glycoprotein fraction, mastigonemes, were used to determine the source of flagellar surface glycoproteins and to define the general properties of flagellar surface assembly in Euglena. After suitable absorption, mastigoneme antiserum reacts with several specific mastigoneme glycoproteins but does not bind either to the other major flagellar glycoprotein, xyloglycorien, or to other Sarkosyl-soluble flagellar components. When Fab' fragments of this mastigoneme-specific antiserum were used in combination with a biotin-avidin secondary label, antigen was localized not only on the flagellum as previously described but also in the contiguous reservoir region. If deflagellated cells are reservoir pulse-labeled with Fab' antibody, this antibody appears subsequently on the newly regenerated flagellum. This chased antibody is uniformly distributed throughout the length of the flagellum and shows no preferred growth zone after visualization with either fluorescein or ferritin-conjugated secondary label. From these and tunicamycin inhibition experiments it is concluded that (a) a surface pool of at least some flagellar surface antigens is present in the reservoir membrane adjacent to the flagellum and that (b) the reservoir antigen pool is transferred to the flagellar surface during regeneration.
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PMID:Flagellar surface antigens in Euglena: immunological evidence for an external glycoprotein pool and its transfer to the regenerating flagellum. 711 1

This study examines the distribution of glycoconjugates on the surface of cultured chick myotubes with a battery of lectins labeled with ferritin or horseradish peroxidase. In addition, the distribution of a specific glycoprotein, fibronectin, is investigated by immunocytochemistry. Particular attention is paid to the localization of these substances in specialized patches on the cell surface previously shown to contain a high density of acetylcholine receptors as demonstrated with horseradish peroxidase labeled alpha-bungarotoxin. The specialized patches are found to bind a greater amount of concanavalin A, ricin agglutinin I, and soy bean agglutinin and a lesser amount of wheat germ agglutinin than the general myotube surface. Limulus lectin is distributed over the entire cell surface while other lectins do not bind to any sites. The surface patches contain a high density of acetylcholine receptors as shown by double labeling with ferritin-labeled lectins and peroxidase labeled alpha-bungarotoxin. Fibronectin occurs in high concentration at the surface patches and is present over other regions of the cell surface as well. These results reveal differential patterns of distribution of glycoconjugates and fibronectin over the myotube surface. These regional differences may be related to the distribution of acetylcholine receptors or to recognition and attachment by the innervating nerve.
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PMID:Distribution of cell surface saccharides and fibronectin on cultured chick myotubes: relationship to acetylcholine receptor clusters. 716 Mar 17

The cellular sites of the glycoproteins Group 1 allergen (glycoprotein 1) and Antigen A (glycoprotein 2) in mature ryegrass pollen have been investigated by immunoelectron microscopy. Radioimmunoassays confirm previous findings of cross-reactivity between the purified glycoprotein antigens at the high immunoglobulin G (IgG) concentrations used for localization. Freeze-drying of anthers followed by anhydrous processing has been employed because of the water solubility and mobility of the glycoproteins. A double-embedding technique has been developed. This involves, first, embedding anthers in the water-soluble plastic resin JB-4, sectioning and incubating in ferritin-labelled antisera by the indirect method. The sections are then embedded in Spurr's resin for ultra-thin sectioning. Both glycoproteins are found in the following sites: (1) exine and intine wall layers; (2) pollen cytoplasm; (3) the orbicules and anther loculus; and (4) the anther cuticle. In the exine arcades and surface and in the anther loculus, the ferritin label is bound to pollenkitt. The finding that the glycoproteins are in similar sites is predictable in view of the cross-specificity of the antisera. The extent of antibody penetration of the plastic sections has been examined; labelling is confined to cut grains and absent from intact grains.
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PMID:Immunocytochemical localization of water-soluble glycoproteins, including group 1 allergen, in pollen of ryegrass, Lolium perenne, using ferritin-labelled antibody. 717 55

The various histologic components of 39 germ cell tumors of the testis were studied with indirect labeled immunoperoxidase technique for the presence of the following tumor-associated antigens: alpha-fetoprotein (AFP), alpha 1-antitrypsin (A1AT), chorionic gonadotropin (HCG), specific pregnancy beta 1-glycoprotein (SP1), human placental lactogen (HPL), carcinoembryonic antigen (CEA), and ferritin (Fe). Embryonal carcinoma components were positive for AFP in 9/16, for A1AT in 6/16, for CEA in 2/16, and for Fe in 14/16. All yolk-sac tumor components were positive for AFP and Fe, and 8/13 contained A1AT and 2/13 CEA. Epithelium in teratoid components was positive for AFP in 5/14 cases, for A1AT in 8/14, for CEA in 7/14, and for Fe in 8/14. Syncytial trophoblast in choriocarcinoma components and syncytial giant cells were all positive for HCG, SP1 and HPL. In addition, tumor giant cells in two nonseminomatous tumors and in one seminoma contained HCG. Otherwise, all pure seminomas were negative for all antigens, except for Fe, which was positive in 12/16 cases. Demonstration of this functional aspect of germ cell tumors of the testis may clarify problems of classification and elucidate histogenesis. Furthermore, immunohistochemical demonstration of tumor-associated antigens is of value in the management of the patient as an indicator of which tumor markers should be used for monitoring the treatment. In addition, the presence of tumor-associated antigens may be used in prognostic evaluation.
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PMID:Distribution of tumor-associated antigens in the various histologic components of germ cell tumors of the testis. 719 54

The occurrence of endocytotic mechanisms in human small-intestinal absorptive cells was investigated by culturing biopsy specimens in the presence of horseradish peroxidase (HRP), lactoperoxidase (LPO), and ferritin. The results indicate that both HRP and LPO entered the cells by apical endocytosis, after which they were transported via apical vesicles and tubules to the lysosome-like bodies. Ferritin, which showed a distinct affinity for the cell-coat glycoproteins, was not interiorized by the absorptive cells. These findings suggest that although human absorptive cells have an endocytotic mechanism, possibly fluid-phase endocytosis, cell-coat glycoproteins are not taken up by the cells, as indicated by the absence of ferritin in the apical vesicles and tubules, as well as the lysosome-like bodies. These findings provide indirect support for our hypothesis that the lysosome-like bodies have a function in the regulation of cell-coat glycoprotein transport via a crinophagic mechanism (fusion of apical vesicles and tubules with lysosome-like bodies) rather than via an exocytotic-endocytotic mechanism.
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PMID:Endocytosis in absorptive cells of cultured human small-intestinal tissue: horseradish peroxidase, lactoperoxidase, and ferritin as markers. 722 1

Several studies suggest biological functions of the iron-binding neutrophilic glycoprotein lactoferrin that imply an initial interaction with cells from the monocyte/macrophage family. Among these, an important role of lactoferrin as responsible for the inflammatory-induced blood hyposideremia and accumulation of iron in the monocyte/macrophage system has been suggested mainly based on experiments in rodents. In a series of experiments we have examined the binding of human lactoferrin to human monocytes. We have demonstrated the presence of a receptor binding including a high-affinity component and a low-affinity component. The affinity of the binding is compatible with a biological significance of this receptor (KD is about 10(-8) M, and the number of receptors about 10(6) per cell). More than 90% of the lactoferrin will dissociate from the cell. The binding is not truly reversible since lactoferrin will lose its receptor-binding property after dissociation from the cell. The only observed change in the molecule is a small decrease in isoelectric point from 8.9 to 8.8. Lactoferrin is able to translocate at least 50% of its bound iron to intracellular ferritin in monocytes. These findings are compatible with the idea that lactoferrin might be involved in the pathogenesis of the disturbances in iron metabolism observed during inflammation.
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PMID:The monocytic receptor for lactoferrin and its involvement in lactoferrin-mediated iron transport. 776 50

Interleukin-1 beta (Il-1 beta), a key cytokine in the acute phase response, elevates hepatic expression of both the heavy (H) and light (L) ferritin subunits without influencing the steady-state levels of either ferritin transcript. Transfection experiments with human hepatoma cells reveal that sequences within the 5' untranslated region (5'UTR) of H-ferritin mRNA confer translational regulation to chimaeric chloramphenicol acetyl transferase (CAT) mRNAs in response to Il-1 beta in the absence of marked changes in CAT mRNA levels. Il-1 beta dependent translational enhancement is mediated by a distinct G + C rich RNA sequence within 70 nucleotides (nt) of the start codon. The upstream Iron Responsive Element RNA stemloop does not confer increased expression to CAT mRNA in Il-1 beta stimulated hepatoma transfectants. A 38 nucleotide consensus sequence within the 5'UTRs of the mRNAs encoding the hepatic acute phase proteins alpha 1-antitrypsin (alpha 1AT), alpha 1-acid glycoprotein (AGP) and haptoglobin (Dente et al., 1985) is similar to sequences in the G + C rich H-ferritin mRNA translational regulatory element. Deletion of three nucleotides from this region of the 61 nt G + C rich element in the H-ferritin mRNA 5' leader eliminates Il-1 beta translational enhancement of the CAT reporter transcripts.
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PMID:Translational enhancement of H-ferritin mRNA by interleukin-1 beta acts through 5' leader sequences distinct from the iron responsive element. 804 31


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