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)

Tissue sections taken from areas of carcinoma, areas of intestinal metaplasia in stomachs bearing carcinoma are areas of intestinal metaplasia in stomachs showing atrophic gastritis only were examined for eight markers: a tumour-derived colon-specific antigen (tCSA), carcinoembryonic antigen (CEA), alpha-fetoprotein (AFP), pregnancy-specific beta-glycoprotein 1 (SP1), human placental lactogen (HPL), human beta chorionic gonadotrophin (beta-HCG), transferrin (TF) and ferritin (FE). In terms of the number of markers demonstrated in each of the three categories, there is a close similarity between the cells of adenocarcinoma and cells of intestinal metaplasia in cases of cancer, but not to similar metaplastic cells in atrophic gastritis cases. In addition, it appears that the presence of tCSA and SP1 is closely linked to carcinoma, though only approximately half of such cases contain these markers. It would also appear that there are two types of morphologically identical intestinal metaplasia, one related to cancer, the other not. No difference was found between so-called intestinal type and diffuse-type carcinomas.
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PMID:Tumor markers in carcinoma and premalignant states of the stomach in humans. 617 91

The biological and antigenic roles of glycosylation were investigated in the influenza hemagglutinin (HA) glycoprotein using the glycosylation inhibitor tunicamycin (TM). Under conditions where only the nonglycosylated form of HA was detected by immunoprecipitation and gel electrophoresis, the migration of glycoproteins to the cell surface was observed by immunofluorescence using either monospecific or monoclonal antibody to the HA polypeptide. Analysis of the surface fluorescence in TM-treated infected cells by a fluorescence-activated cell sorter (FACS) showed that all cells exhibited fluorescence in the complete absence of glycosylation. The relative amount of HA antigen on cell surfaces was found to be reduced by only 30-40% in TM-treated cells, and this reflected a similar reduction in intracellular synthesis. Electron microscopic studies using ferritin labeling also demonstrated that the nonglycosylated HA glycoprotein was present in significant amounts on surfaces of infected cells. Virions with nonglycosylated glycoproteins were purified, and were found to have an approximate 30-fold decrease in both hemagglutinin and neuraminidase specific activities. The possible role of oligosaccharides in antigenic variation among various H1N1 strains was investigated. Immunoprecipitation reactions involving five different monoclonal antibodies and five antigenic variants of A/USSR/90/77 revealed no major antigenic differences between the glycosylated and nonglycosylated forms of HA.
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PMID:Studies on the role of glycosylation in the functions and antigenic properties of influenza virus glycoproteins. 619 89

We submitted 83 consecutive patients with pleural effusion to routine clinical investigation; 57 were diagnosed as malignant, 18 as benign, and 8 were not diagnosed. Pleural fluid and serum were analysed for carcinoembryonic antigen (CEA), acid glycoprotein (AGP), antichymotrypsin (ACT), C-reactive protein (CRP), alpha 2-pregnancy associated glycoprotein (alpha 2-PAG) and ferritin. Multivariate discriminant analysis was performed on the results of the protein measurements. CEA and ACT values in serum and fluid were found to give a good discriminating function between the benign and malignant groups. The use of such an analysis, in a clinical context, is discussed.
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PMID:The diagnosis of pleural effusions--are cancer markers clinically helpful? 619 56

Scanning electron microscopy (SEM) of mouse cornea and conjunctiva fixed with picric acid-paraformaldehyde-glutaraldehyde (PA-P-G) mixture revealed a thin layer of amorphous material covering the microvilli of the corneal surface cells. At the transmission electron microscopic (TEM) level, this layer of material stained positively with dialyzed iron, alcian blue and cationized ferritin, all of which are markers for anionic sulfate or carboxyl groups. The corneal surface was negative for high iron diamine, which specifically stains sulfate groups. These results indicate that the murine ocular surface is rich in carboxyl groups. Treatment with neuraminidase prior to fixation significantly reduced (P less than 0.005) cationic ferritin binding, suggesting that most of the carboxyl groups at the ocular surface are associated with sialic acid residues. The corneal surface also stained positively at the TEM level when a periodic acid-thiocarbohydrazide-silver protein sequence (PA-T-SP) was applied. This result indicated the presence of periodic acid-Schiff (PAS)-positive glycoprotein and glycolipid at the ocular surface.
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PMID:Complex carbohydrates at the ocular surface of the mouse: an ultrastructural and cytochemical analysis. 620 40

In 95 patients with inoperable squamous cell carcinoma of the bronchus, nine potential serum "markers" were analysed for their prognostic significance. Lactate dehydrogenase, alpha 1 HS-glycoprotein, ferritin, carcino-embryonic antigen and immunoglobulin E did not prove to be useful as prognostic indices. The erythrocyte sedimentation rate and the acute phase proteins alpha 1 acid glycoprotein, C-reactive protein and prealbumin were correlated with survival. After taking the performance status and tumour stage into account, C-reactive protein still proved to be a strong prognosticator. The clinical relevance of the acute phase proteins signifying a so-called "biochemical status" next to the "clinical status" is discussed.
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PMID:The prognostic significance of acute phase proteins in patients with inoperable squamous cell carcinoma of the bronchus. 620 52

Enveloped viruses are excellent tools for the study of the biogenesis of epithelial polarity, because they bud asymmetrically from confluent monolayers of epithelial cells and because polarized budding is preceded by the accumulation of envelope proteins exclusively in the plasma membrane regions from which the viruses bud. In this work, three different experimental approaches showed that the carbohydrate moieties do not determine the final surface localization of either influenza (WSN strain) or vesicular stomatitis virus (VSV) envelope proteins in infected Madin-Darby Canine Kidney (MDCK) cells, as determined by immunofluorescence and immunoelectron microscopy, using ferritin as a marker. Infected concanavalin A- and ricin 1-resistant mutants of MDCK cells, with alterations in glycosylation, exhibited surface distributions of viral glycoproteins identical to those of the parental cell line, i.e., influenza envelope proteins were exclusively found in the apical surface, whereas VSV G protein was localized only in the basolateral region. MDCK cells treated with tunicamycin, which abolishes the glycosylation of viral glycoproteins, exhibited the same distribution of envelope proteins as control cells, after infection with VSF or influenza. A temperature-sensitive mutant of influenza WSN, ts3, which, when grown at the nonpermissive temperature of 39.5 degrees C, retains the sialic acid residues in the envelope glycoproteins, showed, at both 32 degrees C (permissive temperature) and 39.5 degrees C, budding polarity and viral glycoprotein distribution identical to those of the parental WSN strain, when grown in MDCK cells. These results demonstrate that carbohydrate moieties are not components of the addressing signals that determine the polarized distribution of viral envelope proteins, and possibly of the intrinsic cellular plasma membrane proteins, in the surface of epithelial cells.
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PMID:Glycosylation does not determine segregation of viral envelope proteins in the plasma membrane of epithelial cells. 626 61

The early interactions of LLC-MK2 cell-grown noninfectious Sendai virus and a murine cell line, P815 mastocytoma ascitic cells, were studied by electron microscopy, using the ferritin-conjugated antibody technique with anti-virus glycoprotein serum. For comparison, the interactions of egg-grown infectious Sendai virus with the same cells were also examined. When noninfectious virus was adsorbed to the cells in the cold, the cell membranes become partially invaginated at the site of contact of adsorbed virions, but ferritin-conjugated antibodies did not penetrate into the areas of envelope-cell membrane association. This pattern of virus attachment was similar to that of infectious virus attachment. Upon subsequent incubation at 37 degrees C, most of the adsorbed noninfectious virions were taken into cytoplasmic vesicles and then degraded, although a few virions remained attached to the cell membrane. No evidence of fusion of envelopes of noninfectious virions was obtained. On the other hand, envelopes of infectious virions fused with the cell membrane, and the transferred viral antigens diffused on the cell surfaces and then decreased in number.
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PMID:Immunoelectron microscopic study on interactions of noninfectious sendai virus and murine cells. 626 15

This study demonstrates that the glycoprotein of vesicular stomatitis virus clusters in the plasma membrane of infected Chinese hamster lung cells during morphogenesis and suggests that viral nucleocapsids are required for this clustering. A mutant virus (ts E-1) which is temperature sensitive for the synthesis of viral nucleocapsids but not viral membrane proteins was used. The surface distribution of the viral glycoprotein in cells infected by this virus was determined by a specific indirect immunoferritin stain. Early in infection at permissive temperatures, the glycoprotein was randomly distributed on membrane ghosts. Later, clusters of ferritin the size and shape of virus particles were seen. In contrast, ghosts prepared from virus-infected cells maintained at a restrictive temperature always had a random distribution of viral glycoprotein.
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PMID:Assembly of vesicular stomatitis virus: distribution of the glycoprotein on the surface of infected cells. 629 21

Successful invasion of mammalian cells by pathogenic parasites is generally considered, from circumstantial evidence, to be a consequence of specific mechanisms of recognition of cell surface components--this has stimulated investigations of the biochemical characterization of such molecules. Several studied of trypanosomiasis have examined the ability of parasites to interact with mammalian cells. However, knowledge of the mammalian cell surface 'receptors' which interact with the parasite is limited. We now report that fibronectin, which is a high molecular weight glycoprotein present in blood, connective tissue and at cell surfaces, binds specifically to Trypanosoma cruzi trypomastigotes. The reaction is specific, reversible (in the presence of a 100-fold molar excess of unlabelled ligand) and of moderate affinity (Kd = 11.36 nM). Various other proteins (for example, thyroglobulin, ferritin, catalase, aldolase, human IgG and bovine serum albumin) had no significant effect on the binding of labelled ligand to the parasite surface. Addition of anti-fibronectin antibodies to the culture medium significantly inhibited the infection of rat fibroblasts (3T3 FR) by T. cruzi trypomastigotes, suggesting that cell surface fibronectin may act as a recognition site for attachment of the parasites.
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PMID:Fibronectin receptors on Trypanosoma cruzi trypomastigotes and their biological function. 632 89

The subcellular location of the major malarial glycoprotein in erythrocytes infected with schizonts of Plasmodium falciparum has been studied by two methods. In the first, glycoproteins were labelled with [3H]glucosamine or [3H]isoleucine during in vitro culture. Trypsin treatment of intact infected erythrocytes caused no major qualitative or quantitative changes in [3H]glucosamine labelled glycoproteins or [3H]isoleucine labelled proteins separated by sodium dodecylsulfate polyacrylamide gel electrophoresis. However, in the presence of Triton X-100 the labelled glycoproteins and proteins were completely cleaved by trypsin. In the second method, two monoclonal antibodies which specifically immunoprecipitate the major 195 kDa glycoprotein failed to react on indirect immunofluorescence with intact non-fixed schizont-infected erythrocytes, but reacted strongly with saponin released schizonts indicating specificity for the surface of mature intracellular parasites. Immunoelectronmicroscopy using ferritin-conjugated secondary antibody confirmed the location of the epitope(s) recognized by these monoclonals on the surface of intracellular parasites. Ferritin particles were not associated with knob-bearing erythrocyte membranes. The results indicate that only a small proportion or none of the 195 kDa glycoprotein is on the surface of the infected erythrocyte and that the largest proportion is expressed on the surface of mature intraerythrocytic parasites.
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PMID:Localization of the major Plasmodium falciparum glycoprotein on the surface of mature intraerythrocytic trophozoites and schizonts. 637 50


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