Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cell lines expressing varying levels of ganglioside GM3 at the cell surface show different degrees of adhesion and spreading on solid phase coated with such glycosphingolipids (GSLs) as Gg3 (GalNAc beta 1----4Gal beta 1----4Glc beta 1----1Cer), LacCer (Gal beta 1----4Glc beta 1----1Cer), or Gb4 (GalNAc beta 1----3Gal alpha 1----4Gal beta 1----4Glc beta 1----1Cer) (where Cer is ceramide), which may have structures complementary to GM3, but not on solid phase coated with various other GSLs. The degree of cell adhesion and spreading on Gg3 was correlated with the degree of cell-surface GM3 expression, as defined by reactivity with anti-GM3 monoclonal antibody (mAb) DH2. Only cells with high GM3 expression adhered on solid phase coated with LacCer or Gb4. Adhesion of GM3-expressing cells on Gg3-, LacCer-, and Gb4-coated solid phase is based on interaction of GM3 with Gg3 and, to a lesser extent, with LacCer and Gb4, as demonstrated by: (i) the interaction of the GM3 liposome with solid phase coated with Gg3, LacCer, and Gb4, respectively; (ii) the abolition of cell adhesion on each GSL-coated solid phase by treatment of cells with mAb DH2 or sialidase; and (iii) the inhibition of cell adhesion by treatment of GSL-coated solid phase with mAb specific to each GSL. Sialosyllactosyl-lysyllysine conjugate was bound to Gg3 adsorbed on a C18 silica gel column in the presence of bivalent cation, suggesting that the carbohydrate moiety of GM3 is involved in GM3-Gg3 interaction. Not only the adhesion and spreading of GM3-expressing cells, but also their cell motility was greatly enhanced on Gg3-coated solid phase, as determined by Transwell assay and phagokinetic track assay on a gold sol-coated surface. Spreading and motility of GM3-expressing cells on Gg3-coated solid phase were both inhibited by treatment of cells with mAb DH2 or sialidase. These results provide evidence that not only cell adhesion, but also spreading and motility in these cell lines are controlled by complementary GSL-GSL interaction.
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PMID:Cell adhesion, spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction. 189 38

By hemagglutination tests surface lectins on S. saprophyticus strain S 1 with N-acetylgalactosamine (GalNac) and N-acetylglucosamine (GlcNac) specificity and on P. aeruginosa ATCC strain 27853 with N-acetylneuraminic acid (NANA) specificity could be demonstrated. To elucidate the role of bacterial surface lectins for the specific adhesion, polyether urethane discs were preincubated for 15 h at 4 degrees C in human serum or urine. Adhesion studies with S. saprophyticus S1 and P. aeruginosa ATCC 27853 onto precoated polymers revealed that microbial lectins may play a role in the colonization of prosthetic devices since lectin-blocking with competitive glycoconjugates significantly decreased bacterial adherence to the coated surfaces. Non-specific carbohydrates did not inhibit the adherence demonstrating specificity of this process.
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PMID:Evidence for lectin-mediated adherence of S. saprophyticus and P. aeruginosa to polymers. 211 7

The occurrence and significance of bacterial carbohydrate recognition proteins (bacterial lectins) and endogenous carbohydrate binding proteins (endogenous lectins) of human urothelium as well as kidney tubulus epithelium was analyzed with respect to the adhesion of urotoxogenic Escherichia coli bacteria. Using biotinylated neoglycoproteins, we demonstrated a wide spectrum of endogenous lectins with Galactose-, Mannose-, Fucose-, N-Acetylgalactosamine-, and N-Acetylglucosamine binding activities in the urothelium. In the kidney the distal nephron and especially the medullar collecting ducts exhibited a similar spectrum of endogenous carbohydrate binding activities as detected for the urothelium. Adhesion- as well as inhibition-experiments with selective blocking of either bacterial lectins or endogenous lectins of the target cells by different carbohydrates both reduced the bacterial adhesion. However, maximal inhibition of bacterial adhesion was achieved by simultanous blocking of microbial and target cell lectins with mannose or mannan. From these results it is reasonable to conclude that specific adhesion which may result in an organotropism (urotropism) of E. coli infection is due to a dual recognition mechanism which is accomplished by the combined interaction of the bachterial and host cell lectins with the corresponding carbohydrates of E. coli and that of the target cells respectively. Further studies showed that normal human serum possesses natural antiadhesins which are represented by the glycan parts of the serum-glycoproteins.
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PMID:[Topography and mechanisms of adhesion of uropathogenic Escherichia coli bacteria in the human kidney and renal pelvis]. 248 13

Adhesion of P. aeruginosa to normal and injured rat tracheas was examined. Rat tracheas were injured by exposure to 0.1N HCl for 10 min, and incubated with P. aeruginosa. Adhesion was quantitated by direct count of the number of bacteria attached to a fixed surface area as viewed by scanning electron microscopy. P. aeruginosa adhered to injured tracheas much more than to normal tracheas. The adhesion of P. aeruginosa, preincubated with mucin and sugars, to acid injured trachea was examined. Mucin, N-acetylneuraminic acid and N-acetyl-D-galactosamine inhibited the adhesion of P. aeruginosa to injured tracheas, but not N-acetylglucosamine, L-fucose, D-mannose and D-galactose. Periodate oxidation and neuraminidase treatment of acid injured tracheas reduced the adhesion of P. aeruginosa. These data suggest that N-acetylneuraminic acid (sialic acid) is the receptor for P. aeruginosa or a part of the receptor in acid injured rat trachea and in tracheobronchial mucin.
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PMID:[Study of the receptor for P. aeruginosa on tracheal cells and in tracheobronchial mucin]. 250 16

We have analyzed the effect of 14 carbohydrates (seven monosaccharides, four disaccharides and three aminosugars) on the adhesion of Entamoeba histolytica HK9 trophozoites to human red blood cells (RBC). Amebal adhesion was significantly inhibited by five of these carbohydrates with the following order of potency: lactose (Lac) greater than N-acetylgalactosamine (GalNac) greater than melibiose (Mel) greater than galactose (Gal) greater than N-acetylglucosamine (GlcNAc). The mean inhibitory concentration of Lac was 2.66 mM. Adhesion increased by 20% in the presence of 5.5 mM glucose (Glc). Inhibition of the adhesion was lower in the absence rather than in the presence of Glc only with Gal-NAc, whereas it was similar with Lac, Mel, Gal, and GlcNAc in both cases. The initial rate of amebal adhesion decreased 27% by RBC fixation, but adhesion to fixed RBC was also inhibited by the same five carbohydrates. Inhibition was higher in mixtures containing Lac, GalNAc, and Mel, than with the same isolated carbohydrates; Lac + Gal-NAc was the most potent mixture. Inhibition decreased when Lac, GalNAc, and Mel were mixed either with Gal or GlcNAc. We conclude that E. histolytica adhesion depends on amebal metabolic energy generated from Glc and on several surface components of RBC, some of which are inactivated with glutaraldehyde whereas others are inhibited by sugars containing Gal, GlcNAc, or Gal-NAc residues.
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PMID:Inhibition of the adhesion of Entamoeba histolytica trophozoites to human erythrocytes by carbohydrates. 289 24

Staphylococcus saprophyticus strains S 1 and S 35 demonstrated lectin like surface receptors specific for N-acetylgalactosamine (S 1) or N-acetylneuraminic acid (S 35). Adhesion assays with human uroepithelial cells together with blocking experiments with competitive carbohydrates suggested that specific attachment of S. saprophyticus to host cells is apparently mediated by lectins. Staphylococcal lipoteichoic acid (LTA) was also shown to interfere with S. saprophyticus adherence to human uroepithelial cells.
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PMID:The role of lectins and lipoteichoic acid in adherence of Staphylococcus saprophyticus. 340 61

The ability of rabbit alveolar macrophages to specifically recognize and adhere to surfaces derivatized with carbohydrates was examined. Otherwise inert polyacrylamide gels were derivatized with aminohexylglycosides as previously described (Guarnaccia, S. P., and Schnaar, R. L. (1982) J. Biol. Chem. 257, 14288-14292). Intact viable rabbit alveolar macrophages, isolated by lung lavage, were placed in contact with surfaces derivatized with different glycosides. Only those surfaces derivatized with alpha-D-mannose residues were capable of supporting rabbit alveolar macrophage adhesion. Adhesion was rapid, obtaining maximal levels within 10 min, and occurred readily at either 0 or 37 degrees C. The carbohydrate specificity of the cell adhesion was investigated by the use of soluble carbohydrate inhibitors. The potency of various saccharides to block the adhesion correlated with that demonstrated for blocking the uptake or binding of radiolabeled soluble glycoproteins (Shepherd, V. L., Lee, Y. C., Schlesinger, P. H., and Stahl, P. D. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 1019-1022). Thus, the order of potency observed was: D-Man congruent to L-Fuc greater than D-GlcNAc congruent to D-Glc much greater than D-Gal congruent to D-GalNAc congruent to L-rhamnose. While soluble monosaccharides were capable of blocking adhesion when added in millimolar concentrations, polymannosylated neoglycoproteins were able to block adhesion in the nanomolar concentration range. Adhesion to the mannose-derivatized surfaces was a dynamic event even at 0 degrees C, since adhesion was less susceptible to monosaccharide inhibition at later incubation times. Surfaces derivatized with aminohexyl S-mannoside ligands were more effective in supporting adhesion than those derivatized with the corresponding O-mannosides. Soluble inhibitor studies suggest that this was due to a more favorable conformation of the S-glycoside for binding to the cell surface receptor. The results reported here demonstrate that the previously reported alveolar macrophage mannose/fucose receptor can mediate carbohydrate-specific cell adhesion.
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PMID:Carbohydrate-specific adhesion of alveolar macrophages to mannose-derivatized surfaces. 669 35

We investigated the role of mucin-type (O-linked) carbohydrate chains of tumor target cells in the recognition by macrophages through a Gal/GalNAc-specific calcium-dependent lectin. Binding of a soluble form of this lectin to P815 mastocytoma cells was increased by treatment with benzyl-GalNAc, which presumably inhibited the extension of mucin-type carbohydrate chains. The levels of cell surface expression of GalNAc residues were elevated after benzyl-GalNAc treatment, as revealed by the binding of Vicia villosa agglutinin B4 and Dolichos biflorus agglutinin. Adhesion of treated P815 cells to this lectin immobilized on plastic surfaces also increased. Furthermore, the binding of P815 cells to macrophage-like RAW 264.7 cells and to peritoneal macrophages also increased after the same treatment. We concluded that elevated levels of cell surface terminal GalNAc in mucin-type carbohydrate chains increased accessibility of P815 cells to macrophages through Gal/GalNAc-specific calcium-dependent lectins.
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PMID:Enhancement in accessibility to macrophages by modification of mucin-type carbohydrate chains on a tumor cell line: role of a C-type lectin of macrophages. 788 11

Adhesion to target cells represents the first step in infection by Entamoeba histolytica. Binding of axenic amoeba (HMI strain) to human red cells in vitro was employed as a model of the adhesion process. The influence of precontact of trophozoites with suspensions of live Saccharomyces boulardii yeasts, their fractions (membranes and yeast-content supernatant before and after filtration to eliminate the membrane) or yeast culture medium before and after fermentation was investigated. N-Acetylgalactosamine (GalNAC) was employed as the reference inhibitory sugar. The percentage of amoebae bearing red cells after pretreatment of amoebae with the various suspensions and derivates was determined. Adhesion was also evaluated by scanning electron microscopy (SEM). Pretreatment of amoebae with the live yeast suspension led to a significant reduction in the percentage of adhesion [32% vs 70% in the phosphate-buffered saline (PBS) control]. Reduced adhesion was also observed with the filtered and unfiltered supernatant of the yeast suspension homogenate [32% and 34%, respectively, vs 69% in the PBS control], yeast culture medium at the end of fermentation [49% vs 76% in the PBS control] and GalNAC [32% vs 72% in the PBS control]. SEM showed a decrease in the number of amoebae bearing red cells and a reduction in the number of red cells adhering to amoebae. We conclude that substances produced by the yeasts compete with red cells for adhesion sites on amoebae.
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PMID:Inhibitory activity of saccharomyces yeasts on the adhesion of Entamoeba histolytica trophozoites to human erythrocytes in vitro. 815 19

Nerve cells depend on specific interactions with glial cells for proper function. Myelinating glial cells are thought to associate with neuronal axons, in part, via the cell-surface adhesion protein, myelin-associated glycoprotein (MAG). MAG is also thought to be a major inhibitor of neurite outgrowth (axon regeneration) in the adult central nervous system. Primary structure and in vitro function place MAG in an immunoglobulin-related family of sialic acid-binding lactins. We report that a limited set of structurally related gangliosides, known to be expressed on myelinated neurons in vivo, are ligands for MAG. When major brain gangliosides were adsorbed as artificial membranes on plastic microwells, only GT1b and GD1a supported cell adhesion of MAG-transfected COS-1 cells. Furthermore, a quantitatively minor ganglioside expressed on cholinergic neurons, GQ1b alpha (also known as Chol-1 alpha-b), was much more potent than GT1b or GD1a in supporting MAG-mediated cell adhesion. Adhesion to either GT1b or GQ1b alpha was abolished by pretreatment of the adsorbed gangliosides with neuraminidase. On the basis of structure-function studies of 19 test glycosphingolipids, an alpha 2,3-N-acetylneuraminic acid residue on the terminal galactose of a gangliotetraose core is necessary for MAG binding, and additional sialic acid residues linked to the other neutral core saccharides [Gal(II) and GalNAc(III)] contribute significantly to binding affinity. MAG-mediated adhesion to gangliosides was blocked by pretreatment of the MAG-transfected COS-1 cells with anti-MAG monoclonal antibody 513, which is known to inhibit oligodendrocyte-neuron binding. These data are consistent with the conclusion that MAG-mediated cell-cell interactions involve MAG-ganglioside recognition and binding.
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PMID:Gangliosides are neuronal ligands for myelin-associated glycoprotein. 857 Jun 40


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