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

The surface saccharide composition of collagenase-dispersed pancreatic cells from adult guinea pig and rat glands was examined by using eight lectins and their ferritin conjugates: Concanavalin A (ConA); Lens culinaris (LCL); Lotus tetragonolobus (LTL); Ricinus communis agglutinins I and II (RCA I, RCA II); Soybean agglutinin (SBA); Ulex europeus lectin (UEL); and wheat germ agglutinin (WGA). Binding studies of iodinated lectins and lectin-ferritin conjugates both revealed one population of saturable, high-affinity receptor sites on the total cell population (approximately 95% acinar cells). Electron microscopy, however, revealed differences in lectin-ferritin binding to the plasmalemma of acinar, centroacinar, and endocrine cells. Whereas acinar cells bound heavily all lectin conjugates, endocrine and centroacinar cells were densely labeled only by ConA, LCL, WGA, and RCA I, and possessed few receptors for LTL, UEL, and SBA. Endocrine and centroacinar cells could be differentiated from each other by using RCA II, which binds to centroacinar cells but not to endocrine cells. Some RCA II receptors appeared to be glycolipids because they were extracted by ethanol and chloroform-methanol in contrast to WGA receptors which resisted solvent treatment but were partly removed by papain digestion. RCA I receptors were affected by neither treatment. The apparent absence of receptors for SBA on endocrine and centroacinar cells, and for RCA II on endocrine cells, was reversed by neuraminidase digestion, which suggested masking of lectin receptors by sialic acid. The absence of LTL and UEL receptors on endocrine and centroacinar cells was not reversed by neuraminidase. We suggest that the differential lectin-binding patterns observed on acinar, centroacinar, and endocrine cells from the adult pancreas surface-carbohydrate-developmental programs expressed during morphogenesis and cytodifferentiation of the gland.
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PMID:Distribution of cell surface saccharides on pancreatic cells. II. Lectin-labeling patterns on mature guinea pig and rat pancreatic cells. 42 54

Anionic sites on the surface of Brucella canis were visualized in the electron microscope by staining with positively charged ferric oxide hydrosols in acetic acid (AI-reagent), or propanoic acid (PI-reagent), and with a polycationic ferritin derivative. With the AI-reagent, single or small aggregates of ferric oxide particles were bound to the cell surface of Br. canis, whereas, with the lipophilic PI-reagent, the microorganisms were heavily stained with focal aggregates of iron granules. The polycationic ferritin label was uniformly distributed over the entire cell surface of Br. canis. The ferritin label was not bound on the surface of the organisms after prior treatment with trichloroacetic acid or methanolic hydrochloric acid. Treatment with aqueous acetone, chloroform/methanol, diethyl ether, sodium deoxycholate, pronase, lysozyme, hyaluronidase, and sodium periodate neither influenced the morphology of the Brucella nor diminished their ionic binding sites. Our results indicate that the anionic sites on the cell surface of Br. canis may be carboxyl and phosphate groups of lipopolysaccharides.
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PMID:[Ultrastructural investigations on anionic surface sites of Brucella canis (author's transl)]. 60 17

Conjugated-Schiff's-base-type fluorescence was measured in iron-depleted samples and chloroform extracts of human spleen haemosiderin. Incubation of ferritin with liposomes and ascorbate led to the formation of compounds with similar fluorescence properties. Analysis of protein subunits by SDS/polyacrylamide-gel electrophoresis confirmed that ferritin was damaged in incubations with ascorbate. Since previous studies have shown that intact ferritin is resistant to proteolytic degradation, it is suggested that haemosiderin may be a product of oxidative reactions involving ferritin and lipid.
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PMID:Haemosiderin-like properties of free-radical-modified ferritin. 382 50

The filamentous bacteriophage f1 can be transformed into a spherical particle (spheroid) or an intermediate shortened filament with a flared end (I-forms) by exposure to a chloroform-water interface at 22 or 4 degrees C, respectively. The protein composition of bacteriophage f1 spheroids and I-forms was examined by separating the proteins from the purified. [35S]cysteine-labeled particles by sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis. Quantitation of the radioactivity on the gels showed that I-forms and spheroids contain the same complement of minor coat proteins as do untreated f1 phage. This composition is unchanged after removal of the DNA, either by digestion with micrococcal nuclease or by centrifugation of the particles through CsCl density gradients, indicating that none of the minor coat proteins is held in the particles solely through an interaction with the DNA. We also examined the location of the A protein in I-forms by decoration with ferritin-conjugated antibodies and examination under the electron microscope and found that the A protein is located specifically at the flared end of the I-form particle, through which the DNA is extruded and at which contraction into spheroids begins. The implications of these results with regard to the orientation of the DNA within the capsid and the process of infection are discussed.
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PMID:Minor coat protein composition and location of the A protein in bacteriophage f1 spheroids and I-forms. 709 58

Cell-size unilamellar vesicles were made by removing solvents from microscopic chloroform spherules containing smaller water droplets within. The average diameter of the vesicles in a typical preparation was 9.2 mum, comparable to that of human erythrocytes (7 mum). The standard deviation of the size distribution was 3.0 mum. The unilamellarity and bilayer unit membrane of vesicles were demonstrated by transmission electron microscopy. Materials so far successfully incorporated into vesicles include glucose, sucrose, Arsenazo III and Ponceau S dyes, thymidine triphosphate, methotrexate, agarose, collagen, ferritin, polyadenylic aid, DNA, and whole bacteria. The captured volume per milligram of lipids (up to 144 microliter/mg) was almost an order of magnitude greater than the highest value reported in the literature to date (up to 15.6 microliter/mg) (Szoka, F.C. and Papahadjopoulos, D. (1978) Proc. Natl. Acad, Sci. U.S.A. 75, 4194-4198).
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PMID:Preparation of cell-size unilamellar liposomes with high captured volume and defined size distribution. 727 96

Gas and tar phases of commercially available filter cigarettes were tested for ferritin-iron-releasing effects and polyunsaturated-fatty-acid oxidant capacity in vitro. A vacuum pump-dependent apparatus with Cambridge filters was used to separate gas and tar; the former was directly smoked into reaction mixtures, while the latter was extracted from Cambridge filters in aqueous medium and freshly used at 40 to 80% final concentrations. Both phases induced ferritin iron release, which was not antagonized by superoxide dismutase (SOD). In specific experiments, we have also shown that gas and tar extracts could cross an organic (i.e., chloroform)-phospholipid layer before mobilizing ferritin iron. Once delocalized from ferritin, iron could trigger lipid peroxidation; however, a marked prooxidant effect (inhibited by 20 microM deferoxamine mesylate and significantly decreased by 40 microM vitamin E) was observed only with gas, whereas tar extracts showed antioxidant effects. Accordingly, tar extracts could also antagonize lipid peroxidation driven by non-chelated iron or by peroxyl radicals. In the absence of ferritin, gas-induced lipid peroxidation was very low, and tar extracts were apparently ineffective. Thus, the intrinsic lipoperoxidative capacity of cigarette smoke is low and is due to gas; however, when smoke interacts with ferritin, a marked iron-driven peroxidation becomes manifest essentially with gas, tar components acting as antioxidants. The present data suggest that cigarette-smoke-mediated iron mobilization from ferritin may represent a specific prooxidant mechanism related to cigarette smoking in vivo.
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PMID:Cigarette smoke, ferritin, and lipid peroxidation. 784 2