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)

Previous studies with protein tracers have shown that the luminal surface of the vascular endothelium of the bone marrow is endocytic. The endocytosis occurs through the formation of large bristle-coated vesicles (LCV). The anionic charge distribution in this process was examined at the luminal surface of the endothelial cell, At pH 1.8, colloidal iron (CI), native ferritin, and polycationic ferritin (PCF) are bound by the luminal surface of the endothelial cell, but not at the sites of LCV formation. PCF used over a pH range of 1.8--7.2 (CI is unstable at higher pH levels) revealed LCV binding of this agent in increasing manner from pH 3.5 upwards. PCF binding at low pH (1.8) at the endothelial cell surface was markedly reduced by neuraminidase. Neuraminidase did not reduce PCF binding by the endothelial cell surface nor by the LCV at higher pH levels. It is concluded that the luminal surface of the endothelial cell has exposed sialic acid groups which are absent or significantly diminished at endocytic sites. The free surface of the endothelial cells as well as the sites of endocytosis have, in addition, anionic material with a pKa higher than that of sialic acid (pKa 2.6). These anionic materials may be different at the sites of endocytosis as compared to those present at the free cell surface.
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PMID:Nonrandom distribution of sialic acid over the cell surface of bristle-coated endocytic vesicles of the sinusoidal endothelium cells. 2 50

The lectin receptors of confluently grown hamster BHK, wild type polyoma virus transformed PyBHK, and temperature-sensitive polyoma transformed ts3-PyBHK fibroblasts were investigated using cell agglutination, quantitative (125I)lectin binding, and ferritin-lectin labeling. PyBHK and permissively grown ts3-PyBHK cells agglutinated more strongly with Ricinus communis I agglutinin (RCA-I)compared to BHK and nonpermissively grown ts3-PyBHK, although saturation binding of (125I)RCA-I to these cells at 4 degrees resulted in a twofold difference in lectin-binding sites on BHK and nonpermissively grown ts3-PyBHK cells (1.0-1.3 x 10 7 sites/cell) compared to PyBHK and permissively grown ts3-PyBHK (0.4-0.6 x 10 7 sites/cell). These cells bound equivalent amounts of (125I)concanavalin A (0.8-1 x 10 7 sites/cell) and (125I)wheat germ agglutinin (1-2.2 x 10 7 sites/cell). Under these binding conditions little endocytosis occurred, as judged by the subsequent release of greater than 90% cell-bound (125I)RCA-I by the RCA-I inhibitor lactose and localization of ferritin-RCA-I exclusively to the extracellular plasma membrane surface. However, if the binding is performed at 22 degrees, only 50% of the bound lectin can be removed by lactose, and ferritin-RCA-I is localized inside the cell within endocytotic vesicles. The relative mobility of RCA-I receptors was examined on ts3-PyBHK cells by the ability of ferritin-RCA-I to induce clustering of its receptors at 22 degrees. RCA-I receptors on permissively grown ts3-PyBHK cells appeared to be more mobile than on nonpermissively grown cells. BHK and PyBHK cells were treated with neuraminidase, and the resulting enzyme-treated cells were assayed for lectin agglutinability and quantitative binding of RCA-I, concanavalin A, and wheat germ agglutinin. Neuraminidase treatment resulted in decreased concanavalin A and wheat germ agglutinability and a slight increase in RCA-I agglutinability. The enzyme-treated BHK and PyBHK cells bound less (125I)wheat germ agglutinin (2.8 x 10 6 and 2.2 x 10 6 sites/cell, respectively) and 2.5 and 6.2 times more (125I)RCA-I (2.5-3 x 10 7) and 3.5-4 x 10 7 sites/per cell, respectively). There was no change in the number of concanavalin A binding sites after neuraminidase treatment. The increase in RCA-I binding sites approximated the decrease in wheat germ agglutinin binding sites indicating that the predominant penultimate oligosaccharide residue to sialic acid on these cells is D-Gal.
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PMID:Qualitative and quantitative interactions of lectins with untreated and neuraminidase-treated normal, wild-type, and temperature-sensitive polyoma-transformed fibroblasts. 16 28

Lectins, plant proteins that bind specific saccharide determinants, have been utilized to examine the effect of neuraminidase digestion on the structure and/or expression of oligosaccharide moieties present at the periphery of Novikoff ascites hepatoma cells. Five lectins were utilized: concanavalin A (Con A), specific for alpha-D-manno- or alpha-D-glucopyranosyl residues; wheat germ agglutinin, specific for 2-acetamido-2-deoxy-D-glucopyranosyl residues; Ricinus communis agglutinin I (RCAI), specific for D-glucopyranosyl residues; R. communis agglutinin II (RCAII), specific for D-galacto- or 2-acetamido-2-deoxy-D-galactopyranosyl residues; and soybean agglutinin, specific for 2-acetamido-2-deoxy-D-galactopyranosyl residues. Neuraminidase treatment of Novikoff cells did not alter their agglutination by Con A or wheat germ agglutinin. Similar treatment produced only a 2-fold increase in their agglutination by RCAI but a 12-fold increase in their agglutination by RCAII, indicating that 2-acetamido-2-deoxy-D-galactopyranosyl residues become expressed upon neuraminidase treatment. This conclusion was confirmed by the observation that neuraminidase-treated Novikoff cells acquired agglutinability by soybean agglutinin. Binding studies using ferritin-conjugated RCAII indicated that neuraminidase treatment exposed cryptic cell surface receptors for RCAII. To ascertain the role of cell surface glycoproteins in lectin-induced agglutination of Novikoff cells, glycopeptides cleaved from the cell surface by papain were assayed for lectin receptor activity. The cell surface glycopeptides exhibited receptor activity for Con A, wheat germ agglutinin and RCAI but not for RCAII and soybean agglutinin. A cell surface macrosialoglycopeptide fraction, resolved by gel filtration and ion-exchange chromatography, possessed a major portion of the Con A and RCAI receptor activity.
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PMID:Effect of neuraminidase and papain treatment on lectin-induced agglutination of Novikoff tumor cells and assay of lectin receptor activity of the glycopeptides released from the cell surface by papain. 17 11

Surface charge of wild-type Crithidia fasciculata and three drug-resistant mutants (TR3, TFRR1, and FUR11) was studied by direct zeta-potential determination and ultrastructural cytochemistry. Surface tension was also investigated by measurements of the advancing contact angle formed by the protozoa monolayers with drops of liquids of different polarities. The individual zeta potential varies markedly among the C. fasciculata cells. The wild and FUR11 mutant strains displayed lower negative surface charge (-12.5 and -9.5 mV, respectively) as compared with the TR3 (-14.8 mV) and TFRR1 (-14.7 mV) mutant strains. Binding of cationized ferritin (CF) was observed at the cell surface of wild and mutant strains of C. fasciculata. Neuraminidase treatment reduced the negative surface charge in the TFRR1 and TR3 mutants in about 37 and 29%, respectively, whereas no significant change was observed with the wild and FUR11 mutant strains. These findings suggest that sialic acid residues are the major anionogenic groups on the surface of C. fasciculata. The density of sialic acid residues per cell in wild and mutant strains of C. fasciculata falls in a range of 1.4 x 10(4) to 3.6 x 10(4). Marked differences of hydrophobicity were also observed. For example, the TFRR1, FUR11, and TR3 drug-resistant mutant strains showed higher contact angle values (55.4, 54.2, and 49.3, respectively) than the wild-type (35.6), as assessed by alpha-bromonaphtalene.
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PMID:Surface charge and hydrophobicity of wild and mutant Crithidia fasciculata. 128 83

The surface charge of different isolates of Phytomonas from Euphorbia hyssopifolia, Euphorbia pinea, Euphorbia characias and Manihot esculenta was analysed by the binding of cationic particles (colloidal iron hydroxide at pH 1.8 and cationized ferritin at pH 7.2) to the protozoan surface and by determination of the cell electrophoretic mobility (EPM). All the isolates had a net negative surface charge, and the isolate from E. hyssopifolia manifested the greatest negative charge. A good relationship between the electrophoretic mobility data and the density of the cationic particles on the parasite's surface, as seen in ultrathin sections, was observed. Neuraminidase treatment did not significantly reduce the mean EPM of the parasites analysed.
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PMID:Comparative study of the surface charge of some isolates of trypanosomatids of the genus Phytomonas. 251 59

The anionic macromolecules at the glomerular endothelial cell surface are visualized only when stained with cationic stains. We investigated the arrangement and composition of this anionic matrix at the luminal surface. Rat kidneys were perfused with anionic ferritin (pI 4.5), ferritin (pI 7.4), or cationized ferritin (CF, pI 8.3). Anionic ferritin (pI 4.5) did not bind to the capillary wall, ferritin (pI 7.4) bound discontinuously only to the laminae rarae of the basement membrane, but cationized ferritin (CF, pI 8.3) bound as a thick continuous layer to the cell plasmalemma and bound to the anionic matrix in the fenestral spaces. These observations show that an anionic matrix lines the entire capillary lumen surface, fills the fenestrae, and is interposed between the blood and the basement membrane at the fenestrae. The anionic constituents at the capillary luminal surface were identified by in vivo digestion with specific enzymes. Absence of CF binding following digestion with specific enzymes was taken to indicate the presence of the particular glycoprotein known to be susceptible to the enzyme used. Neuraminidase digestion revealed that anionic sites over the surface plasmalemma are mainly from sialoproteins. In contrast, the matrix in fenestral channels contains heparan sulfate, hyaluronic acid, and sialoproteins. Papain digestion showed no glycolipids at the luminal surface. The functions of this continuous anionic layer located at the luminal surface of glomerular capillaries have not yet been established.
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PMID:The anionic matrix at the rat glomerular endothelial surface. 296 99

Polycationic derivatives of ferritin containing primary amino groups (CFah) or tertiary amino groups (CFdmp) were potent platelet agonists inducing shape change, aggregation and secretion, but also agglutination in the presence of EDTA. Pretreatment of platelets with neuraminidase, PGE1, indomethacin, or creatine kinase/creatine phosphate inhibited CF-induced activation. In contrast, neuraminidase and PGE1 increased the agglutination by CF, indicating an inverse relationship between activation and CF-induced agglutination. At pH 7.4, the cationic charges of CFdmp exceeded those of CFah by a factor of 1.5 and the platelets bound approximately 1.5 times more CFah than CFdmp, suggesting the same number of anionic surface sites for both CF preparations. The capacity of the platelets to bind CF was diminished by 55% at 0 degree C or by 62% after aldehyde fixation and by 13% with PGE1. This suggests that the binding capacity depends on the mobility of the binding sites in the plane of the membrane but is only slightly increased by platelet activation. Binding to fixed or cold platelets approached equilibrium within a few seconds whereas saturation required several minutes at 37 degrees C. Neuraminidase preferentially reduced the slow binding and much less the rapid binding. Since activation by CF developed during seconds, suppressible by a brief treatment with neuraminidase 25 mU/ml, a small portion of neuraminidase-sensitive sites appears to be necessary for CF-induced platelet activation. Full activation and agglutination occurred at CF concentrations far below saturating concentrations. The results show that neither CF-induced activation nor agglutination depend on a simple neutralization of the negative surface charge.
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PMID:Cationized ferritin as a platelet-stimulating surface probe. Binding to platelets and effects on platelet function. 308 60

We have prepared fluorescein isothiocyanate (FITC) conjugates of cationised ferritin (CF) and have investigated the usefulness of this CF-FITC to measure the negative cell surface charge of mouse bone marrow cells by flow cytometry. CF-FITC conjugates of low fluorochrome to protein ratios (F/P ratio) gave insufficient fluorescence and/or formed large aggregates when stored. CF-FITC conjugates of high F/P ratios (above 25) bound specifically to bone marrow cells, giving sufficient fluorescence, the intensity of which differed for the different cell types. When stored at -20 degrees C the CF-FITC was stable and could be used over prolonged periods. CF-FITC could be used to selectively enrich for pluripotent stem cells (CFU-S) and granulocyte/macrophage progenitors (CFU-C) by fluorescence activated cell sorting (FACS), although the CF-FITC binding to CFU-S and CFU-C was unexpectedly low. No correlation between CF-FITC fluorescence, cell size and electrophoretic mobility (EPM) was observed of bone marrow cells fractionated by free flow electrophoresis. Neuraminidase treatment to remove negatively charged sialic acid groups from the cell surface resulted in an increased binding of CF-FITC, although the EPM was decreased. The biotin conjugate of CF bound to bone marrow cells and could be visualised by avidin-FITC. The relative fluorescence intensity for the individual cell types showed a good correlation with the cell surface charge as determined by the EPM of the different cell types. The mechanism of binding CF-FITC to the cell surface was not by electrostatic interaction of the negative cell surface and positively charged CF because CF-FITC of F/P ratios of above 20 was negatively charged.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The use of cationized ferritin to measure cell surface charge of mouse bone marrow cells by flow cytometry. 308 17

In retinal photoreceptors the connecting cilium constitutes a boundary between the inner and outer segments. In previous studies we demonstrated that, while opsin could be localized in abundance in the distal ciliary membrane, very little opsin was detected in the proximal ciliary plasma membrane. In the present study we extended our view of molecular specialization on the ciliary membrane with respect to glycoconjugates. Saccharide moieties of ciliary glycoconjugates were studied in immature and mature rat photoreceptors. Surface saccharides were detected and localized by means of ferritin-labeled lectins and electron microscopy. Dense labeling of the ciliary membrane surface with wheat germ agglutinin (WGA) was observed. In immature photoreceptors the labeling was restricted to the proximal ciliary membrane, in a region where opsin molecules could not be detected. Neuraminidase digestion abolished WGA binding to the proximal ciliary membrane surface, indicating that sialic acids mediate WGA binding to this domain. Peanut agglutinin (PNA) did not label the ciliary surface, nor did it bind to the surface of other photoreceptor domains. Neuraminidase digestion exposed numerous PNA binding sites on the ciliary membrane surface. In view of the carbohydrate specificity of PNA, we suggest that a terminal trisaccharide sequence, sialic acid-galactose-(beta 1----3)-N-acetyl galactosamine, is present in high density on the proximal ciliary membrane surface.
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PMID:Surface glycoconjugates on rat photoreceptor cilium. Effect of neuraminidase digestion. 329 28

Terminal saccharide sequences in rat photoreceptor cell surface glycoconjugates were characterized. Lectin cytochemistry and electron microscopy were used for preembedding cytochemical localization of surface carbohydrates. Neuraminidase digestion was employed for the exposure of penultimate saccharides in sialoglycoconjugates. Isolated rat retinas were incubated with ferritin-labeled wheat germ agglutinin (WGA), peanut agglutinin (PNA), and soybean agglutinin (SBA) prior to and after neuraminidase digestion. PNA and SBA did not label untreated photoreceptors. WGA densely labeled the photoreceptor surface and interphotoreceptor matrix (IPM) components. Following neuraminidase treatment, PNA, but not SBA, labeled the photoreceptor surface and the IPM. WGA labeling of the IPM was abolished, and the labeling of the photoreceptor surface was reduced. Based on the lectin specificity, it was concluded that photoreceptor surface glycoconjugates in the rat retina contain a terminal trisaccharide: sialic acid-D-galactose-(beta 1----3)-N-acetyl-D-galactosamine.
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PMID:Cytochemical characterization of sialoglycoconjugates on rat photoreceptor cell surface. 355 69


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