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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Trypanosoma lewisi bloodstream and culture forms were agglutinated differentially with low concentrations of the cationic compounds: ruthenium red, ruthenium violet, Alcian blue chloride, 1-hexadecylpyridinium chloride, lanthanum chloride, and cationized ferritin. The bloodstream form trypanosomes gave the highest agglutination levels with each of the compounds tested. Ruthenium red was the most effective inducer of cell agglutination among the several cations used. Trypsin-treated bloodstream forms were agglutinated less in the presence of ruthenium red than untreated controls. Ruthenium red-induced cell agglutination also was lowered with chondroitin sulphate and dextran sulphate, but not with alpha-D-glucose, alpha-D-mannose or with several methyl glycosides. Treatment of the bloodstream trypanosomes with alpha-amylase, dextranase, or neuraminidase had little effect on agglutination levels obtained with ruthenium red. Fine-structure cytochemical staining with ruthenium red, ruthenium violet, and Alcian blue-lanthanum nitrate was used to ascertain the presence and distribution of presumptive carbohydrates in the trypanosome cell surface. The extracellular surface coat of the bloodstream forms stained densely with each of the polycationic dyes. Trypsin treatment removed the surface coat from bloodstream trypanosomes; however, the surface membranes of the organisms were stained densely with the several dyes. Similar surface-membrane staining was obtained with the cationic compounds and the culture forms, which lack a cell surface coat. Cationized ferrin was used at the fine-structure level to visualize the negative surface charge present in the cell surface coat and external membrane of the several trypanosome stages. Results obrained from the agglutination and cytochemistry experiments indicate that complex polysaccharides are present in the surface membranes and cell surface coat of T. lewisi bloodstream forms. Similar conclusions also pertain to the surface membranes of the T. lewisi culture from trypanosomes. The carbohydrates probably represent glycopeptide and glycoprotein structural components of the surface membrane of this organism.
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PMID:Cell surface saccharides of Trypanosoma lewisi. I. Polycation-induced cell agglutination and fine-structure cytochemistry. 5 63

A carbohydrate-containing fraction was extracted from the trypanosomatid Crithidia fasciculata by a phenol-water procedure. Ion-exchange chromatography separated this fraction into three components: a polysaccharide which was not retained on the column; RNA which eluted upon addition of salt; and, another polysaccharide which eluted upon addition of detergent. The unretained fraction was shown to be composed solely of D-mannose. The mannan, which was heterodisperse on Sephadex G-100, had an average molecular weight of approx. 14 000 as based on analysis of reducing groups. The detergent-eluted material yielded arabinose and galactose upon acid hydrolysis. The arabinogalactan was excluded from Sephadex G-100 and Sephacryl S-200 molecular sieve columns, suggesting a molecular weight greater than or equal to 200 000. Cell fractionation studies showed the bulk of extractable polysaccharide was associated with a particulate fraction. Further determination of the cellular localization of the polysaccharide was accomplished by employing a specific antiserum prepared from rabbits immunized with the polysaccharide extract. The cell surface localization of the arabinogalactan was demonstrated by cell agglutination studies as well as immunocytochemical techniques using fluorescein and ferritin conjugated antibodies.
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PMID:Polysaccharides of crithidia fasciculata. Identification and partial characterization of a cell surface constituent. 9 71

The use of Lens culinaris lectin for electron microscopic detection of D-mannose,- D-glucose and N-acetyl-D-glucosamine like sites on tumor cells, erythrocytes, erythrocyte ghosts, cultured rat liver cells and various tissues of mice is demonstrated. In addition to Lens culinaris lectin-peroxidase reaction (LeL-po reaction) the preparation of active Lens culinaris lectin-ferritin conjugate are described and the specificity of cytochemical reactions are demonstrated. Furthermore experiments by immuno freeze-etching are reported for topological analysis of the lectin receptors.
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PMID:Electron microscopic demonstration of cell surface carbohydrates by means of peroxidase and ferritin complexes of the Lens culinaris lection. 115 Apr 86

The carbohydrate composition of horse spleen ferritin was studied. 1 mol of the apoferritin, the protein moiety of ferritin, contains 25 mol of hexose, 3 mol of hexosamine and 10 mol of fucose. Same carbohydrate composition was detected in the apoferritin from iron rich ferritins. These results indicate that horse spleen ferritin is composed of non-identical subunits as regards its carbohydrate composition.
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PMID:Carbohydrate composition of horse spleen ferritin. 118 1

The surface charge of Crithidia fasciculata and Crithidia luciliae was analysed by measurement of the zeta-potential and labelling of the protozoan surface with cationized ferritin particles. Both trypanosomatids have a net negative surface charge, with a zeta-potential of -10.39 mV and -11.12 mV for C. luciliae and C. fasciculata, respectively. Enzyme treatment showed that phosphate groups, but not sialic acid, significantly contributed to the negative surface charge. Lectin-induced agglutination was used to analyse the presence of surface-exposed carbohydrates in C. fasciculata and C. luciliae. The cells did not agglutinate when incubated in the presence of lectins which recognized L-fucose, N-acetyl-D-glucosamine and sialic acid. However, lectins which bind to N-acetyl-D-galactosamine, D-galactose and D-mannose agglutinated both protozoa.
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PMID:Cell surface charge and sugar residues of Crithidia fasciculata and Crithidia luciliae. 178 53

In addition to maintaining corneal transparency via a pump-leak mechanism, the corneal endothelium plays an active role in the transport of certain proteins to supply nutrients for the stroma and to remove metabolites. In order to investigate transcellular transport mechanisms across the endothelium, we exposed cultured rabbit corneal endothelial cells to tracers that are commonly used to describe various forms of endocytosis. The cells were incubated on their apical surfaces in solutions containing different HRP conjugated lectins (concanavalin A and lens culinaris = alpha-D-mannose, alpha-D-glucose; peanut agglutinin = alpha-D-galactose), cationized ferritin (CF), native ferritin (NF), and HRP alone for 5-60 min and processed for EM cytochemistry. At early times, the lectins and CF were seen bound to the apical plasma membrane, thus indicating adsorptive endocytosis. The NF and the lectins in the presence of their competing sugar as well as HRP showed little or no surface binding, thus being markers for fluid phase endocytosis. At later times, large amounts of lectins and CF were located in round, tubular, or U-shaped vesicles of various sizes, large vacuoles, multivesicular bodies, and in other cytoplasmic compartments. Very little or no uptake was observed with NF, or when the lectins were used in presence of their competing sugars. HRP was seen in moderate amounts only in round or oval shaped vesicles. This study suggests that adsorptive endocytic pathways play a major role in transcellular transport through the corneal endothelium, whereas the transport of macro-molecules via fluid phase endocytosis is more limited. In addition, our observations suggest that adsorptive endocytic tracers undergo various intracellular fates and also appear to be transported through the cells at different rates.
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PMID:Adsorptive and fluid phase endocytosis by cultured rabbit corneal endothelium. 218 89

Distribution of alpha-D-mannose and alpha-D-glucose residues of glycoconjugates in axons of sciatic nerves of 24-month old rats of Wistar strains was studied by concanavalin-A-ferritin conjugate. In some of axons there were cumulations of ferritin molecules in agglomerates of various size with polarization of the phenomenon at preserved integrity of myelin sheath. In other cases the concentration of a large number of lectin binding sites was established in the region of the degenerating part of myelin sheath, engrossed in the axon cylinder. The changes in the distribution of carbohydrate residues in the axoplasm of some of the fibers are discussed in connection with the occurring axonal atrophy in fibers of peripheral nerves of old rats.
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PMID:[Cytochemical localization of concanavalin A binding sites in the peripheral nerve axons of old rats]. 239 17

Complex carbohydrates in secretory granules and at the apical cell surface of mouse gastric mucoid cells were studied during embryogenesis and in the early postnatal period by various cytochemical methods; the periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) and tannic acid-uranyl acetate (TA-UA) procedures made neutral mucosubstances (NMS) visible, whereas the hexose residues of glycoconjugates were identified using WGA-, RCA II- and ConA-ferritin. The glycocalyx was stained with ruthenium red (RR). During differentiation of the embryonic mucoid cells the number of secretory granules increased in parallel to the increase in their carbohydrate component. NMS-stainable parts in secretory granules also had binding sites for the conjugates RCA II- and WGA-ferritin, but the binding of ConA could not be identified. The increasing quantity of NMS in secretory granules was correlated with the increased amount of PA-TCH-SP and TA-UA positive substances in the apical glycocalyx only in 14- and 18-day-old embryos. The observed uniform affinity for RR and lectin conjugates in all analysed developmental stages remains to be explained.
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PMID:The carbohydrates of secretory granules and the glycocalyx in developing mucoid cells. 241 10

The localization of complex carbohydrates in the Golgi apparatus, secretory granules and plasmalemma of mouse parotid acinar cells was studied using the fracture-labelling method. The hexose residues of glycoconjugates were identified using ferritin conjugated with Wheat Germ Agglutinin (WGA-), Ricinnus Communis Agglutinin II (RCA-II-), Phaseolus Vulgaris Agglutinin (PHA-) and Limulus Polyphemus Agglutinin (LPA-). We found that the fracture-labelling method allows not only the labelling of membrane faces but also analysis of the compartment's content that is exposed during the fracturing of the tissue. Our results revealed differences in the hexose residues located in the Golgi apparatus, secretory granules and the apical and lateral plasmalemma. Numerous binding sites for WGA-, PHA- and RCA-II-ferritin were demonstrable in the Golgi apparatus. In secretory granules, the WGA- and RCA-II-ferritin binding sites were most numerous, while LPA-ferritin binding sites were very rare. The density of the binding sites for PHA-ferritin showed considerable variation in secretory granules. The apical plasmalemma exhibited a high density of binding sites for all of the lectins used. In the lateral plasmalemma, LPA-ferritin was not bound, and there were fewer binding sites for WGA-, RCA-II- and PHA-ferritin.
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PMID:Lectin-binding pattern in parotid acinar cells. The fracture-labelling method and post-embedding staining. 243 Sep 21

The nature of the adhesive capacity of three hemagglutinating Escherichia coli strains that had earlier been described as nonfimbriated was studied. The strains that were isolated from human disease adhered to human buccal and urinary tract epithelial cells, an adhesion that was not inhibited by D-mannose. By crossed immunoelectrophoresis it was shown that the three strains produced a common antigen, Z1, developed after growth at 37 degrees C but not 18 degrees C. One of the strains produced an additional antigen, Z2, of almost the same electrophoretic mobility in crossed immunoelectrophoresis. A mutant of this strain deficient of its polysaccharide K antigen had maintained the adhesive capacity, indicating that the K antigen was not responsible for adhesion. A further mutant of the acapsular mutant produced a strongly reduced amount of the Z antigens and had lost the ability to adhere. The Z1 (and Z2?) antigens were therefore deemed to be responsible for adhesion. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of extracts of cells of the three strains, a heavy Coomassie-blue stained line was seen, indicating the presence of a protein subunit of molecular weight slightly above 14,400. By immunoblotting with absorbed antiserum, it was shown that this protein was the same as that detected by crossed immunoelectrophoresis. Protease from Streptomyces griseus, but not trypsin, digested the protein. Heating to 100 degrees C did not affect it. By immunoelectron microscopy of embedded and sectioned bacteria that had first been treated with specific antisera and ferritin-labeled antirabbit immunoglobulin, the protein adhesin-antibody complex was found to surround the bacteria as a heavy capsule. After negative staining with uranylacetate (pH approximately 4), the capsule appeared as a mesh of very fine filaments. The possible role of this capsule in the pathogenesis of disease is discussed.
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PMID:An adhesive protein capsule of Escherichia coli. 285 13


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