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

Escherichia coli F-18, a normal fecal isolate, was previously shown to be an excellent colonizer of the streptomycin-treated CD-1 mouse large intestine, whereas E. coli F-18col-, a derivative of E. coli F-18 that no longer makes the E. coli F-18 colicin, was shown to be a poor mouse colonizer. It was also shown that E. coli F-18 bound two to three times more soluble colonic mucus protein than did E. coli F-18col- and that a major receptor in CD-1 mouse colonic mucus was a 50.5-kilodalton glycoprotein. In the present investigation, an additional E. coli F-18 colonic mucus glycoprotein receptor (66 kilodaltons) and three cecal mucus glycoprotein receptors (94, 73, and 66 kilodaltons) were identified. Numerous colonic and cecal brush border protein receptors specific for E. coli F-18 were also identified. Furthermore, E. coli F-18col- was found to bind to the same mucus and brush border receptors as E. coli F-18, although to a far lesser extent. Adhesion of both E. coli F-18 and F-18col- was inhibited by D-mannose and alpha-methyl-D-mannoside, and both strains were shown to bind specifically to the mannose moiety of a mannose-bovine serum albumin glycoconjugate, although again E. coli F-18col- bound to a lesser extent. Finally, both E. coli F-18 and F-18col- were shown to be piliated. The possible role of pilus mediated adhesion in E. coli F-18 colonization of the streptomycin-treated mouse large intestine is discussed.
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PMID:Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: role of adhesion to mucosal receptors. 283 41

Adhesion of 3H-labeled Escherichia coli K-12(K88ab) to CD-1 mouse small intestine mucus and brush border preparations, immobilized on polystyrene, was studied. E. coli K12(K88ab) was shown to adhere readily to either crude mucus or brush border preparations, but not to bovine serum albumin. In contrast, the nearly isogenic E. coli K-12 strain, i.e., lacking the K88ab plasmid, did not bind well to either mucus, brush borders, or bovine serum albumin. The adhesion of E. coli K-12(K88ab) to both mucus and brush borders required pilus expression (i.e., growth at temperatures greater than 18 degrees C) and was inhibited by pretreatment of either mucus or brush borders with trypsin, pronase, or sodium metaperiodate and by the presence of D-galactosamine. Crude mucus was fractionated by gel filtration, and the proteins in receptor-containing fractions were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Separated proteins were Western blotted to nitrocellulose. Adhesion of 35SO4-labeled E. coli K-12(K88ab) and 35SO4-labeled E. coli K-12 to Western blots followed by autoradiography revealed two E. coli K-12(K88ab)-specific mucus receptor proteins (57 and 64 kilodaltons). Brush borders contained the same two receptor proteins present in mucus and an additional 91-kilodalton receptor protein.
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PMID:Identification and characterization of mouse small intestine mucosal receptors for Escherichia coli K-12(K88ab). 300 59

Lewis lung carcinoma cells are able to bind sugar residues, mainly alpha-D-glucosyl and alpha-D-mannosyl derivatives as assessed by fluorescent neoglycoproteins binding assay. We have investigated the binding efficiency and shown that: 3LL tumor cells are heterogeneous with regards to their capability to recognize neoglycoproteins, as shown by fluorescence microscopy and flow cytofluorometry analyses; basically two distinct subpopulations could be evidenced which were called glucose-receptor-rich (or glucose-specific lectin-rich, GLR 3LL) and glucose-receptor-poor (or glucose-specific lectin-poor, GLP 3LL) cells; those two subpopulations could be separated on the basis of their binding properties to neoglycoprotein-substituted microcarriers onto which GLR 3LL cells were able to rapidly adhere (2 h) while GLP 3LL cells were not. Some aspects of the biological behavior of these two selected populations were investigated in order to determine the possible involvement of 3LL cell membrane sugar receptors in cell-cell recognition and adhesion to other cells: namely C57 B1/6 mouse pulmonary cells maintained in primary culture. The two 3LL sublines bind to pulmonary cells but their adhesion kinetics were markedly different. Adhesion inhibition studies showed the adhesion process to be dependent upon the specificity of membrane lectins present on both the tumor cell surface (alpha-D-glucose-specific) and on the pulmonary cells (alpha-L-fucose-specific). Surface sugar-specific receptors on mouse pulmonary cells were shown to bind beta-D-galactose-, alpha-L-fucose and alpha-L-rhamnose substituted serum albumin. A neoglycoprotein bearing alpha-L-rhamnose residues was an efficient binder under the conditions of cell adhesion experiments and a potent cell adhesion inhibitor. A fucose-containing neoglycoprotein was shown to have a high inhibitory activity when used concomitantly to alpha-D-glucose-containing neoglycoproteins. Adhesion inhibition experiments, performed with cells the sugar specific receptors of which have been selectively inactivated, showed that the alpha-L-fucose specific receptors on pulmonary cell surface are partly responsible for the specificity of this cell-cell recognition process.
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PMID:Involvement of membrane sugar receptors and membrane glycoconjugates in the adhesion of 3LL cell subpopulations to cultured pulmonary cells. 380 41

Escherichia coli F-18 isolated from the feces of a healthy human is an excellent colonizer of the CD-1 mouse colon. In the present investigation, adhesion of E. coli F-18 to CD-1 mouse colonic mucus and bovine serum albumin (BSA), immobilized on polystyrene, was studied. Adhesion of E. coli F-18 to mucus was two- to sixfold greater than to either BSA or polystyrene. E. coli F-18 lipopolysaccharide specifically blocked adhesion of E. coli F-18 to mucus and mimicked adhesion of E. coli F-18 to mucus, BSA, and polystyrene. Purified capsule also blocked adhesion of E. coli F-18 to mucus, but this inhibition was found to be entirely nonspecific. The specific E. coli F-18 receptor in mucus appeared to be a glycoprotein, containing sugars normally found in mucins and having a maximum molecular weight of between 1.25 X 10(5) and 2.5 X 10(5).
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PMID:Adhesion of a human fecal Escherichia coli strain to mouse colonic mucus. 392 Jan 46

We have measured separation distances between live human red blood cells and simple or modified glass surfaces, using the finite aperture technique of microscope interferometry. In general, separation increases as the ionic strength falls, in isotonic solutions. Restriction on movement parallel to the glass in all except the most dilute salt solutions, coupled with the absence of Brownian motion, indicates direct molecular contact with the substratum. Thus increased separation must be due to swelling of the glycocalyx under electrostatic forces. However, at approximately less than to 2mM adherent cells show a separation greater than 100 nm, execute Brownian motion and the restriction on lateral motion is less evident. This suggests that secondary minimum adhesion by long-range forces with little or no direct molecular connection occurs at extreme dilution only. Treatment of cells with trypsin reduces separation by up to 40 nm, but the extent to which this reflects reduced double-layer repulsion due to loss of surface charge, as opposed to the reduced opportunity for swelling in a trimmed-down glycocalyx, is unclear. Adhesion at a separation approximately 100 nm in 1 mM buffer after trypsinization supports the view that adhesion can occur without very long glycoprotein connections, but does not prove it. Adhesion to unwettable methylated glass and completely wettable unmethylated glass, with an identical ionic strength dependence of the separation, shows that hydrophilicity is not an absolute requirement. Red cells interact closely at all ionic strengths with glass made polycationic with poly-L-lysine, owing to electrostatic attraction. The interference technique also shows that adherent cells can be spaced from the glass by an intervening layer of previously absorbed serum albumin.
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PMID:Conformational response of the glycocalyx to ionic strength and interaction with modified glass surfaces: study of live red cells by interferometry. 663 Mar 5

A simple turbidimetric method is described that permits quantitation of both the number and the rate at which human fixed washed platelets adhere to fibrillar collagen in suspension. Fixed washed platelets were mixed with buffer or test sample in an aggregometer cuvette. Collagen was added, and the change in light transmission was recorded at 37 degrees C. Percent adhesion was obtained from the maximum change in light transmission within 5 minutes, and the adhesion rate was calculated from the initial slope of the adhesion curve. In this system, the percent adhesion was optimal at ionic strengths of 0.1 to 0.15 in a pH range of 7.0 to 8.0. Percent adhesion could be increased either by lowering the platelet number or by increasing the collagen concentration. No adherence of fixed washed platelets to heat-denatured collagen or Cytodex 3 beads was observed. Adhesion rate increased with greater stirring speed, but decreased with increasing concentrations of bovine serum albumin or normal human plasma, but the percent adhesion remained relatively constant. The rate of adhesion in 20% normal human plasma was greater than that in 1% to 4% bovine serum albumin buffer. This suggests that normal plasma contains some factor(s) that can overcome the inhibitory effect of protein on the rate of adhesion of fixed washed platelets to fibrillar collagen.
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PMID:A quantitative method for studying platelet adhesion to collagen. 671 55

We have shown previously that rat liver macrophages (Kupffer cells) express a membrane-bound form of C-reactive protein (mCRP) on their surface which is identical to a galactose-specific particle receptor activity. We now establish the presence of mCRP on human monocyte-macrophages using immunocytochemistry with an anti-neoCRP specific monoclonal antibody and RNA-RNA in situ hybridization to demonstrate the presence of CRP-specific mRNA. Concomitant with mCRP expression, cells exhibit galactose-dependent uptake of particles coated with lactosylated bovine serum albumin. Adhesion experiments on fibronectin-coated surfaces that mCRP on human blood monocytes may act as a selectin-like adhesion molecule, mediating initial carbohydrate-specific contacts which are followed by peptide-specific recognition via integrin receptors.
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PMID:Expression of membrane-associated C-reactive protein by human monocytes: indications for a selectin-like activity participating in adhesion. 762 Mar 28

Lymphocyte migration from blood into tissue depends on integrin-mediated adhesion to endothelium. Adhesion requires not only integrin ligands on the endothelium, but also activation signals because T-cell integrins cannot bind well until they are activated. The physiological 'triggers' for T-cell adhesion are unknown, but cytokines may be good candidates as they are released during inflammation and trigger adhesion in neutrophils and monocytes. We have identified a cytokine, macrophage inflammatory protein-1 beta (MIP-1 beta), that induces both chemotaxis and adhesion of T cells; MIP-1 beta is most effective at augmenting adhesion of CD8+ T cells to the vascular cell adhesion molecule VCAM-1. We reasoned that, as cytokines in vivo will be rapidly washed away, MIP-1 beta might be bound to endothelial surfaces and so induce adhesion in its immobilized form. Here we show that: (1) MIP-1 beta is present on lymph node endothelium; (2) immobilized MIP-1 beta induces binding of T cells to VCAM-1 in vitro. MIP-1 beta was immobilized by binding to proteoglycan: a conjugate of heparin with bovine serum albumin and cellular proteoglycan CD44 were both effective. We propose that MIP-1 beta and other cytokines with glycosaminoglycan-binding sites will bind to and be presented by endothelial proteoglycans to trigger adhesion selectively not only of lymphocyte subsets, but also of other cell types.
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PMID:T-cell adhesion induced by proteoglycan-immobilized cytokine MIP-1 beta. 842 88

Neutrophils showed a rapid and transient adhesion to immunoglobulin G (IgG)-coated plates compared with their adhesion to bovine serum albumin (BSA)-coated plates: the adhesion reached a peak after 15 min of incubation and then gradually returned to almost the basal state in 60 min. The addition of monomeric IgG or anti-Fc gamma RII monoclonal antibody (mAb) (IV.3) suppressed the increase in adhesion, whereas anti-Fc gamma RIII mAb (3G8) was hardly effective, indicating that the interaction of Fc gamma R, especially Fc gamma RII, with coated IgG is involved in the process. Adhesion was also blocked by cytochalasin B, suggesting that functional actin filament structures are crucial. Protein kinase inhibitors, erbstatin and genistein, inhibited the adhesion in a dose-dependent manner. The adhesion was inhibited by anti-CD11b (M1/70) and anti-CD18 (MHM23, TS1/18) mAbs. Moreover, neutrophils from a patient with complete leukocyte adhesion deficiency syndrome did not show increased adhesion to IgG-coated plates. The adhesion of neutrophils to fibrinogen- and BSA-coated plates was also increased when Fc gamma R was stimulated in the fluid phase with soluble aggregated IgG, which was also inhibited by anti-CD11b mAb. Stimulation of neutrophil Fc gamma R with soluble aggregated IgG enhanced the expression of CD11b in concert with the enhanced adhesion. These data collectively suggest that stimulation via Fc gamma R evokes a tyrosine kinase-dependent and actin filament-dependent intracellular signal that enhances the specific and nonspecific adhesive activity of neutrophils, presumably through the activation of CD11b/CD18.
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PMID:Involvement of CD11b/CD18 in enhanced neutrophil adhesion by Fc gamma receptor stimulation. 791 Aug 40

Human peripheral blood eosinophils adhered specifically to microtitre plates coated with plasma fibronectin (Fn) in a dose- and time-dependent fashion. Adhesion was optimal at 60 min at a concentration of 100 micrograms/ml. Adherence to Fn was up-regulated by platelet-activating factor (PAF; optimum concentration of 10(-6) M) and was significantly inhibited by a polyclonal anti-Fn antibody (P < 0.05). The following evidence suggested that eosinophil adhesion to Fn was mediated by alpha 4 beta 1: (1) eosinophil adherence to Fn was not inhibited by an Arg-Gly-Asp-Ser (RGDS) synthetic peptide; (2) there was a dose-dependent adherence of eosinophils to microtitre plates coated with the 40,000 MW proteolytic fragment of Fn that contains the CS-1 alpha 4 beta 1 binding region, whereas adherence to the 120,000 MW chymotryptic fragment of Fn, which contains the RGD-dependent binding site, was weak and only observed at high concentrations (> 250 micrograms/ml); (3) significant inhibition of eosinophil adherence to Fn was achieved by monoclonal antibodies (mAb) against the alpha chain of VLA-4 but not by a mAb against CD45 or a mouse myeloma antibody as negative controls. After adhesion to Fn, eosinophils were investigated for their capacity to release leukotriene C4 in response to stimulation with a suboptimal concentration of calcium ionophore (2 x 10(-6) M). Significant enhancement of release was detected with Fn-coated plates but not with the control bovine serum albumin (BSA) (P < 0.01). Furthermore, this enhancement was significantly inhibited by the alpha 4 beta 1 mAb HP2/1 (P < 0.05) but not by an anti-CD45 mAb. From these studies we conclude that (1) alpha 4 beta 1 (VLA-4) integrin is a major receptor for Fn on human eosinophils and (2) adhesion to Fn may prime eosinophils for mediator release during allergic inflammation.
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PMID:Adhesion to fibronectin primes eosinophils via alpha 4 beta 1 (VLA-4). 792 93


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