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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adhesion of hepatocytes on culture dishes whose surface was coated with a lactose-carrying styrene homopolymer (PVLA) was investigated. Hepatocytes maintained their round shape on PVLA substratum, which is in contrast to the usual spread shape characteristic of those cultured on collagen and fibronectin substrata. Calcium ion was indispensable for hepatocyte adhesion in PVLA substratum, and hence the hepatocytes on PVLA were easily detached when the culture was treated with ethylenediamine tetraacetic acid (EDTA). The recovered hepatocytes readheres to PVLA. The adhesion of hepatocytes to PVLA was not inhibited by cytochalasin B but by colchicine. Hepatocytes recognize the galactose moieties on the surface of asialoglycoproteins and removes these proteins from the blood stream by receptor mediated endocytosis. The mechanism of adhesion of hepatocytes on PVLA substratum which contains a high density of galactose residues was distinct from the attachment on collagen and fibronectin substrata, and showed great similarity to the receptor and ligand interactions which occurs in the clearance of asialoglycoproteins by hepatocytes.
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PMID:Control of adhesion and detachment of parenchymal liver cells using lactose-carrying polystyrene as substratum. 141 77

Initial adhesion of B16 melanoma variants to non-activated endothelial cells is mediated through specific interaction between GM3 (NeuAc alpha 2----3Gal beta 1----4Glc beta 1----Cer) expressed on melanoma cells and lactosylceramide (LacCer, Gal beta 1----4Glc beta 1----Cer) expressed on endothelial cells. This adhesion is predominant over integrin- or lectin-mediated adhesion in a dynamic flow experimental system employing a parallel plate laminar flow chamber (Lawrence, M. B., Smith, C. W., Eskin, S. G., and McIntire, L. V. (1990) Blood 75, 227-237). In this system, a tumor cell suspension flows over a glass plate coated with glycosphingolipid, lectin, or fibronectin, and adhesion is recorded on videotape. These conditions were designed to mimic the microvascular environment in which tumor metastatic deposition takes place. In contrast, lectin- and fibronectin-based mechanisms are predominant in previously used static adhesion systems. Under static conditions, the relative degree of adhesion of the four B16 variants to endothelial cells or to LacCer-coated plates was the same as their relative degree of GM3 expression (i.e. BL6 approximately F10 greater than F1 greater than WA4), and adhesion was inhibited in the presence of methyl-beta-lactoside, or liposomes containing LacCer or GM3. Adhesion was also inhibited by pretreatment of B16 cells with anti-GM3 antibody DH2 or sialidase and by pretreatment of endothelial cells with anti-LacCer antibody T5A7. Under dynamic flow conditions, WA4 cells did not adhere to mouse endothelial cells at high shear stress (greater than 2.5 dynes/cm2) but did adhere at lower shear stress. In contrast, BL6 and F10 cells adhered strongly at both low and high shear stress. BL6 cell adhesion to endothelial cells at both low and high shear stress was inhibited in the presence of antibody DH2, ethyl-beta-lactoside, or lactose, as well as by pretreatment of BL6 cells with sialidase. Thus, some clear differences, as well as similarities, in cell adhesion under static versus dynamic conditions are demonstrated. These findings suggest that melanoma cell adhesion to endothelial cells, based on GM3/LacCer interaction, initiates metastatic deposition, which may trigger a series of "cascade" reactions leading to activation of endothelial cells and expression of Ig family or selectin receptors, thereby promoting adhesion and migration of tumor cells.
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PMID:Cell adhesion in a dynamic flow system as compared to static system. Glycosphingolipid-glycosphingolipid interaction in the dynamic system predominates over lectin- or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells. 151 64

The effects of cell differentiation on cell adhesion to laminin were studied using the human colon tumor cell line, HT29. HT29 cells were induced to differentiate either by glucose deprivation (HT29glc- vs HT29glc+) or by 2 mM butyrate (HT29glc-+B+). Adhesion was assayed after incubating cell suspensions in microtiter wells previously coated with laminin or other substrates. HT29glc+ cells adhered preferentially to laminin over BSA, fibronectin, and ovalbumin. The adhesion to laminin was greater than 50% of maximum within 15 min. HT29glc- cell adhesion to laminin was consistently lower than that for HT29glc+ or HT29glc+B+ cells. alpha-Lactalbumin (ALA), a modifier of galactosyltransferase (GT) substrate specificity, caused a significant reduction (greater than 50%) in HT29glc+ cell adhesion to laminin when ALA was added to the adhesion incubation mixture. Addition of glucose+ALA to the suspension restored adhesion to laminin. Ovalbumin, a GT substrate, increased adhesion of HT29glc+ and HT29glc- cells to laminin, but lactose, a GT product, did not. The data show that undifferentiated HT29 cells adhere preferentially to laminin over fibronectin and collagen IV and that differentiation of HT29 cells reduces adhesion to laminin. In addition, the data imply that cell adhesion to laminin may be mediated by factors that also modify galactosyltransferase activity.
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PMID:Colonic cancer cell (HT29) adhesion to laminin is altered by differentiation: adhesion may involve galactosyltransferase. 163 32

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

S fimbriae purified from recombinant Escherichia coli HB101(pANN801-13) bound strongly to extracellular matrices of cultured endothelial and epithelial cells; only poor binding was seen with the fimbriae purified from the sfaS mutant strain HB101(pANN801-1321). E. coli HB101(pANN801-13) adhered strongly to laminin immobilized on glass; no adhesion was seen to type I, III, IV, or V collagen. Strain HB101(pANN801-1321) failed to adhere to any of the target proteins. Adhesion to laminin of strain HB101(pANN801-13) was inhibited by sialyl-alpha-2,3-lactose as well as by periodate oxidation and neuraminidase treatment of laminin. In Western blotting, the purified S fimbriae recognized more strongly the A chain than the B chains of laminin.
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PMID:Sialyloligosaccharide chains of laminin as an extracellular matrix target for S fimbriae of Escherichia coli. 810 97

Invasive Escherichia coli strains of certain serotypes invade by the same mechanism as the Shigella sp. It has been proposed that invasion of epithelial cells by EPEC strains may also occur; this is a previously overlooked property. In the present study E. coli strains isolated from patients with diarrhoea or ulcerative colitis, lacking the inv plasmid mediating classical invasion, but hybridizing with probes for different adhesins, were analyzed for their ability to invade HeLa and Caco-2 cells. The majority of strains invaded Caco-2 cells to a higher extent than HeLa cells. Adhesion to Caco-2 cells was a prerequisite for subsequent invasion of the cells but EAF, eae, EAgg and other known virulence factors were not sufficient to mediate invasion. In 8/9 E. coli strains invasion was enhanced after growth under iron restriction. Growth during anaerobic conditions did not influence subsequent invasion by E. coli strains whereas 6/9 strains had their invasive ability significantly decreased after growth in the presence of 1% glucose. The invasive process was inhibited by mannose but not by lactose, fucose or galactose. Our data indicate that strains of E. coli may invade Caco-2 cells by novel mechanisms which require adhesion to the cells but which differ from those of Salmonella sp., Yersinia sp., Shigella sp. and classical enteroinvasive E. coli.
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PMID:Invasion of tissue culture cells by diarrhoeagenic strains of Escherichia coli which lack the enteroinvasive inv gene. 880 71

Adhesion and spreading of tumor cells to the films of a galactose-, glucose-, or phosphatidylcholine-bearing lipid was studied. Human adenocarcinoma Hela cells, B16 mouse melanoma cells, and HuH-7 human hepatoma cells selectively adhered and spread on galactose-bearing lipid in serum-containing medium, but not in serum-free medium. The spreading of the tumor cells in serum-containing medium was inhibited in the presence of lactose, but not in the presence of maltose. Cell spreading also occured on the galactose-bearing glycolipid film pre-treated with serum. From quantitative analysis for the the adsorption of serum components by a quartz-crystal microbalance, the surfaces of the lipid films were found to be entirely covered with serum components. These results suggested that serum components pre-adsorbed on the galactose-bearing lipid influence the cell spreading.
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PMID:The influence of serum for spreading of tumor cells on synthetic glycolipid films. 892 25

Sucralfate, which binds to the matrix of the ulcer bed, is theoretically advantageous for duodenal ulcer therapy, but has not fulfilled its promise clinically. We examined the effects of sucralfate and related compounds in a human intestinal epithelial (Caco-2) cell culture model of restitution on sheet migration across and adhesion to collagen I. Migration was quantitated across a collagen I matrix treated with sucralfate or related compounds and correlated with cell adhesion. Caco-2 motility was significantly and dose-responsively inhibited by sucralfate at therapeutic luminal concentrations. Sucrose octaacetate, the sucralfate backbone, and lactose octaacetate exhibited similar effects while the beta-bonded disaccharide maltose octaacetate had little effect. Sucrose itself slightly stimulated motility. Adhesion effects paralleled motility. Thus, sucralfate may inhibit intestinal epithelial motility by sterically interfering with adhesion to collagen I. A sucralfate analog with a lactose octaacetate backbone might retain growth factor binding without inhibiting enterocyte motility, perhaps improving its clinical efficacy.
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PMID:Sucralfate impedes intestinal epithelial sheet migration in a Caco-2 cell culture model. 901 8

Adhesion and friction forces are the main physical factors determining the re-suspension of a micronized drug from carrier particles during inhalation. Hence, it appears useful to link adhesion and friction force measurements to the in vitro testing of dry powder inhalations, namely the assessment of the mass median aerodynamic diameter (MMAD) using an eight-stage Andersen cascade impactor. Interactive mixtures of micronized Salmeterol Xinafoate adhered to irrespirable lactose monohydrate carrier particles were used as model dosage forms. The adhesion force between the drug and carrier particles was assessed using a centrifuge technique, and the MMAD was determined under standardized working conditions using the Andersen-Cascade impactor (Mark II). A cascade impactor simulator (CIS), which is a computer program containing a re-suspension model to assess the amount of drug detached from the carrier particles during inhalation, was developed and validated using the experimental data. It could be shown, that the CIS provided a good estimate of the loss of drug due to adhesion to the carrier particles and the loss of drug on the cascade impactor walls. Small deviations between the theoretical and experimental mass median aerodynamic particle diameters however were found. These deviations were shown to be mainly due to the experimental error introduced by the cascade impactor, and that the error due to the experimental adhesion measurements is negligibly small. Hence, the CIS developed could be a useful tool in early development stages of dry powder inhalations to predict the in vitro aerodynamic performance of drug particles.
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PMID:The development of a cascade impactor simulator based on adhesion force measurements to aid the development of dry powder inhalations. 917 25

Human Mac-2 binding protein (M2BP) was prepared in recombinant form from the culture medium of 293 kidney cells and consisted of a 92 kDa subunit. The protein was obtained in a native state as indicated by CD spectroscopy, demonstrating alpha-helical and beta-type structure, and by protease resistance and immunological analysis. It was highly modified by N- and O-glycosylation but not by glycosaminoglycans. Ultracentrifugation showed non-covalent association into oligomers with molar masses of 1000-1500 kDa. Electron microscopy showed ring-like shapes with diameters of 30-40 nm. M2BP bound in solid-phase assays to collagens IV, V and VI, fibronectin and nidogen, but not to fibrillar collagens I and III or other basement membrane proteins. The protein also mediated adhesion of cell lines at comparable strength with laminin. Adhesion to M2BP was inhibited by antibodies to integrin beta1 subunits but not to alpha2 and alpha6 subunits, RGD peptide or lactose. This distinguishes cell adhesion of M2BP from that of laminin and excludes involvement of lactose-binding galectin-3. Immunological assays demonstrated variable secretion by cultured human cells of M2BP, which was detected in the extracellular matrix of several mouse tissues.
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PMID:Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. 950 Oct 82


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