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

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

The effect of Tamm Horsfall protein (THP) of 18 healthy subjects and 14 diabetics on adherence of Escherichia coli (06:K13) 2699 strain to human kidney cells (HUK) was studied. Adhesion of bacteria (without additions: 100 bacteria per cell) was reduced dose-dependently by THP, half maximal inhibition occurring with 250 micrograms THP ml-1. Maximal inhibition (-84% at 1000 micrograms ml-1) exceeded inhibition by alpha-methyl-mannoside (36% at 50 mM), was specific (not reproduced by other glycoproteins, e.g. ovalbumin, mucin or thyroglobulin) and reversible (abolished by washing THP off HUK cells). Anti-adherence property of THP was not abolished by neuraminidase treatment. No significant difference of anti-adherence activity of THP was found between controls and diabetics, despite altered carbohydrate composition of THP in diabetes.
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PMID:Tamm Horsfall glycoprotein interferes with bacterial adherence to human kidney cells. 313 Feb 65

Single viable muscle fibers isolated from adult rats by collagenase digestion rapidly bind dissociated spinal neurons or PC-12 cells but not a variety of other cells tested. The adhesion process is calcium-independent, temperature-sensitive, and is not blocked by pretreating cells with inhibitors of energy metabolism or actin polymerization. Adhesion is mediated by a carbohydrate-binding protein and can be inhibited by N-acetylneuraminic acid or mucin, a glycoprotein with high sialic acids content. The hapten inhibitors do not dissociate cells if added after aggregation has occurred. Experiments to block adhesion by pretreatment of cells with either neuraminidase or mucin show that the sialic acids-rich moiety is on the nerve cells, while its receptor is on the muscle fibers.
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PMID:Rapid adhesion of nerve cells to muscle fibers from adult rats is mediated by a sialic acid-binding receptor. 371 Nov 46

An overview is presented of our studies on the interaction between blood-borne tumor cells and the tissues where metastases are formed, in particular the liver. Using blocking antibodies and tumor cell mutants, we have identified the adhesion molecules involved, which so far are all integrins. Strikingly, tumor cell lines that are quite similar, and invade in a comparable fashion, use distinct integrins. Lymphomas that invade the liver massively and diffusely use LFA-1 or fibronectin receptors to adhere to hepatocytes. We have obtained evidence that LFA-1 is activated during the interaction by factors that act through G-protein-coupled receptors, and preliminary results suggest that the same may be true for the fibronectin receptors. Whereas TA3/Ha murine mammary carcinoma cells adhere to hepatocytes via alpha 6 beta 4, TA3/St variant cells of the same tumor bind via the fibronectin receptor alpha 5 beta 1. Adhesion of the TA3/Ha cells appears to be impaired by the mucin epiglycanin that is abundantly present on the surface of these cells.
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PMID:The role of integrins and integrin activation in liver metastasis. 765 36

We recently described the molecular cloning of a murine cDNA encoding an endothelial cell surface ligand for the leukocyte adhesion molecule, L Selectin (Lasky, L. A., Singer, M., Dowbenko, D., Ima, Y., Henzel, W., Grimley, C., Gennie, C., Gillett, N., Watson, S., and Rosen, S. D (1992) Cell 69, 927-938). This glycoprotein ligand was found to resemble mucins in that it contained a large percentage of serine and threonine residues that were apparently O-glycosylated. At least one of the O-linked carbohydrates found on this endothelial ligand interacts with the lectin domain of L Selectin. These data suggest that this endothelial ligand is an adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L Selectin, and the name GLYCAM 1 (GLY-cosylation-dependent Cell Adhesion Molecule 1) has been proposed. In this paper we describe the genomic structure and chromosomal localization of this unique Selectin ligand. The gene has been found to be encoded on four separate exons, and it thus differs from the cell surface mucin leukosialin, whose coding region is contained on one exon, but is similar to glycophorin and CD34, other cell surface mucins whose genes are divided into multiple coding exons. While there is some correlation between exon division and protein domain structure, these relationships are not as clear as they are in other genes. The gene encoding GLYCAM 1 was found to map to murine chromosome 15.
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PMID:Structure and chromosomal localization of the murine gene encoding GLYCAM 1. A mucin-like endothelial ligand for L selectin. 768 41

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

Helicobacter pylori shows in vivo a specific affinity for epithelial surface mucus cells (SMC) of the human stomach. We studied the in vitro adhesion of five different H. pylori strains and one non-pathogenic Escherichia coli-strain to (a) human antral SMC, obtained during gastroscopy; (b) human tumour SMC, from a carcinoma cell line (CRL 1739 AGS); and (c) bovine SMC, obtained from the abomasum. SMC of different origin were characterized by means of electron microscopy and immunohistochemistry, and showed similar main features: all cells showed intra-cellular structures like zymogens and PAS-positive mucin granules. HSMC were antibody-positive against epithelial cell markers. All five H. pylori strains adhered to human SMC (HSMC) and tumour SMC (TSMC). Only one strain additionally adhered to bovine SMC (BSMC). No adhesion to any of these cells was observed with E. coli. Adhesion in vitro is characterized by a close membrane-to-membrane association between H. pylori and the target cells. This phenomenon suggests a specific receptor-ligand interaction.
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PMID:Adhesion of Helicobacter pylori and Escherichia coli to human and bovine surface mucus cells in vitro. 795 1

Recently we described the isolation of a mouse cDNA clone encoding a mucin-like endothelial glycoprotein that appears to function as an adhesive ligand for L selectin. This ligand has been named GlyCAM 1 (Gly-cosylation-dependent Cell Adhesion Molecule 1) because its adhesive interactions with the L selectin lectin domain require that the GlyCAM 1 polypeptide chain be appropriately modified with carbohydrates. These carbohydrate modifications include the addition of sialic acid as well as sulfate residues to O-linked carbohydrate side chains that are clustered in two serine/threonine-rich domains of the mucin. An additional interesting structure that may have relevance to the association of GlyCAM 1 with the lumenal surface of the endothelium was a potential amphipathic helix at the C terminus of the glycoprotein. In order to examine the importance of the postulated O-linked domains as well as the potential amphipathic helix, we have cloned the rat homologue of GlyCAM 1. The sequence of this clone reveals a serine/threonine-rich protein that is highly homologous with the mouse GlyCAM 1. As was found for the mouse GlyCAM 1, the rat homologue shows a clustering of these potential O-linked carbohydrate acceptors in two domains of the protein. Interestingly, many of the serines and threonines are found to be spaced identically in the two homologues, consistent with the possibility that both density and position of the O-linked side chains may be important for appropriate L selectin-mediated adhesion. In support of its postulated functional importance, the C-terminal potential amphipathic helix is conserved in the rat homologue. Finally, immunoprecipitation analysis of [35S]sulfate-labeled rat lymph nodes with either a mouse L selectin IgG chimera or a peptide antiserum directed against a relatively conserved portion of mouse GlyCAM 1 demonstrates a approximately 45-kDa sulfated ligand in rat lymph nodes that is analogous to that previously described for mouse lymph nodes.
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PMID:Cloning of a rat homologue of mouse GlyCAM 1 reveals conservation of structural domains. 810 Feb 29

The purpose of this study was to identify components of saliva that interact with Candida albicans in solution and that may modulate adhesion to dental acrylic (polymethylmethacrylate [PMMA]) surfaces. Saliva-derived pellicles extracted from C. albicans blastoconidia and hyphal-form cells mixed with fresh human submandibular-sublingual saliva (HSMSL) contained predominantly high- and low-molecular-weight mucins (MG1 and MG2, respectively). In contrast, few components from fresh human parotid saliva were adsorbed to yeast cells. Coating PMMA beads with HSMSL significantly enhanced (10-fold) adhesion of both growth forms of C. albicans compared with human parotid saliva (2-fold), suggesting a role for mucins in adhesion. HSMSL-enhanced adhesion was completely abolished by preadsorbing HSMSL with either blastoconidia or hyphal-form cells prior to coating PMMA. However, coating PMMA with purified salivary mucins or the addition of mucin to preadsorbed saliva did not enhance or restore adhesion to levels found with fresh HSMSL. Adhesion assays employing guanidine-treated fresh HSMSL showed a complete lack of Candida binding, suggesting that subjecting HSMSL to dissociating conditions may alter a property of salivary mucins crucial for C. albicans adhesion. Protease and glycosidase treatment of yeast cells significantly reduced adhesion to HSMSL-coated PMMA. In addition, preincubation of C. albicans with mannose and galactose inhibited adhesion to HSMSL-coated PMMA. These results suggest that mucins may play a role in C. albicans adhesion to saliva-coated PMMA and that a glycoprotein on the yeast surface may be involved in these events.
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PMID:Human submandibular-sublingual saliva promotes adhesion of Candida albicans to polymethylmethacrylate. 850 Sep 3

The goal of this study was to characterize salivary components of titanium pellicles and to determine how experimental pellicles affect adhesion of several strains of streptococci to titanium surfaces. Titanium experimental pellicles were formed by incubation of fresh human parotid or human submandibular-sublingual saliva on pure titanium beads. Pellicle was recovered from the beads using sodium dodecyl sulfate buffer and was subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting to identify adsorbed salivary components. Streptococcus anginosus, S. oralis, and S. salivarius recovered from in vivo titanium plaque and five reference strains of streptococci were used in adhesion assays to titanium beads with and without experimental salivary pellicles. The experimental pellicle formed on titanium was found to be composed of selected proteins from human parotid and human submandibular-sublingual saliva. Salivary alpha-amylase and proline-rich proteins were found in all experimental pellicles, while sIgA, high-molecular weight mucin, and proline-rich glycoproteins were detected in one of the experimental pellicles examined. Adhesion of fresh isolates and reference stains of S. anginosus, S. oralis, and S. salivarius to saliva-coated titanium was reduced compared to that of titanium without saliva coating. However, adhesion of laboratory strains of S. gordonii and S. sanguis was found to be significantly greater to experimental pellicles of human submandibular-sublingual saliva than was the adhesion of the fresh isolates, suggesting that streptococci-colonizing implant surfaces may be inherently less adhesive than other bacterial strains. This study found that salivary pellicles are selectively formed on titanium and mediate in vitro adhesion of streptococci.
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PMID:Experimental salivary pellicles formed on titanium surfaces mediate adhesion of streptococci. 880 39


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