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

A very simple, rapid and reproducible method has been developed for studying the interaction of lectins with the cell surface. This involves determining the number of adherent cells after shaking cell suspensions in Petri dishes which have had a lectin coupled to their surface using 1-cyclohexyl-3-(2-morpholinoethyl) carbodiimide metho-p-toluene sulfonate. Using concanavalin A coupled to 60 mm diameter dishes and between 1.5 and 2 x 10(6) tumour cells, this adhesion reached a maximum after 10 min shaking. Maximum cell adhesion also varied according to the particular lectin used. Adhesion was absent or was very low if cells were shaken in untreated dishes, or in dishes coupled to bovine serum albumin, or in the presence of the lectin-specific sugar-competitor. Under conditions of maximum cell adhesion, the binding of two different lymphosarcoma lines to four different lectins was very similar, whereas the binding of a carcinoma line to these lectins was completely different from that observed for the lymphosarcomas.
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PMID:A simple lectin-mediated cell-adhesion method for investigating the cell surface. 58 40

The ability of Escherichia coli K-12(K88ab) to adhere to immobilized porcine small intestine mucus was examined. E. coli K-12(K88ab) but not the isogenic E. coli K-12 strain was found to adhere readily to immobilized crude mucus but not to bovine serum albumin. The adhesion of E. coli K-12(K88ab) was inhibited in a specific fashion by anti-K88 antiserum. Adhesion was also inhibited by pretreatment of receptor-containing crude mucus preparations with sodium metaperiodate or proteolytic enzymes. Removal of glycolipids from crude mucus by chloroform-methanol extraction did not affect the ability of E. coli K-12(K88ab) to bind to mucus preparations. Adsorption of crude mucus preparations with K88ab fimbriae but not type 1 fimbriae resulted in the removal of K88-specific receptors. Analysis of the pelleted fimbriae-receptor complex by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, together with gel filtration chromatography of crude mucus preparations, suggest that the K88-specific receptor present in porcine small intestine mucus is a 40- to 42-kDa glycoprotein.
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PMID:Characterization and identification of a porcine small intestine mucus receptor for the K88ab fimbrial adhesin. 167 Sep 31

In previous studies it was shown that transformation of AKR fibroblasts with 3-methylcholanthrene was associated with a loss of surface fibronectin and that induction of differentiation of the transformed cells with N,N-dimethylformamide (DMF) was associated with reacquisition of surface fibronectin (Chakrabarty et al., J. Cell. Physiol. 133:415, 1987). It is shown in the present study that changes in surface fibronectin reflect altered fibronectin synthesis and altered fibronectin binding. Both the nontransformed cells (AKR-2B) and their transformed counterparts (AKR-MCA) bound 125I-fibronectin in a receptor-like fashion, but the AKR-MCA cells had only 20% of the receptors found on the AKR-2B cells. Whole cell extracts prepared from the AKR-2B cells and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions were examined for 125I-fibronectin binding. Under these conditions, the majority of binding occurred to moieties with molecular weights of 180 kD, 150 kD, and 97 kD. Binding to similar moieties on the AKR-MCA cells was virtually absent but occurred rapidly after treatment with DMF. The appearance of these moieties paralleled the acquisition of 125I-fibronectin binding activity by whole cells. Antibodies to the fibronectin receptor isolated from human placenta reacted with the DMF-sensitive moieties in immunoblot assays. Both the appearance of the fibronectin binding moieties and the acquisition of 125I-fibronectin binding activity by whole cells occurred within 6 hr of DMF treatment and increased over the subsequent 4 day period. The time course of these events paralleled closely the time course for induction of fibronectin biosynthesis by DMF. These changes in fibronectin binding and fibronectin production were associated with alterations in cell-substrate adhesion. The AKR-2B cells rapidly attached and spread on bovine serum albumin-coated dishes and on fibronectin-coated dishes, whereas the AKR-MCA cells were less adhesive on both substrates. Capacity to attach and spread was regained concomitantly with the induction of fibronectin binding and fibronectin production. Adhesion on both substrates was partially inhibited by antibodies to the fibronectin receptor and by RGDS. These studies suggest that fibronectin production and fibronectin binding are coregulated in AKR fibroblasts and that they function together to bring about changes in cell-substrate adhesion.
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PMID:Modulation of fibronectin synthesis and fibronectin binding during transformation and differentiation of mouse AKR fibroblasts. 214 11

Bacterial adhesion to mammary gland epithelial cells (EC) may play a role in the pathogenesis of mastitis. In vitro adherence systems have been developed to study mastitis in cattle but little has been done in sheep. In this work, a method is described for obtaining mammary gland cell preparations containing greater than or equal to 65% EC from live or dead ewes, using a Ficoll-Hypaque flotation method (cell viability = 70-90%). An in vitro adhesion assay procedure was also developed to study the interaction between EC and ovine mastitis bacterial strains. It was observed that, under the test conditions, adherence increased as the incubation time was prolonged from 30 to 120 min (P less than 0.05). Adhesion was greater at incubation temperature of 37 degrees C than at 22 degrees C (P less than 0.001). An acidic pH (5.9) was associated with an increase in adhesion, when compared with a higher pH (7.2; P less than 0.05). Tween 20, Tween 80 and bovine serum albumin helped to eliminate a background of unbound bacteria from the test slides, but they also inhibited adhesion to some strains. Strain differences in adhesion and in ability to form a background were also observed. Some of these findings may have in vivo implications.
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PMID:Factors influencing the degree of in vitro bacterial adhesion to ovine mammary gland epithelial cells. 221 64

A-B-type block copolymers, consisting of polystyrene (PST) or poly(methyl methacrylate) (PMMA) forming segment (A) and poly(gamma-benzyl L-glutamate) (P[Glu(OBzl)]) segment (B), were synthesized and the thrombus formation on these block copolymer films was investigated in relation to the adsorption of plasma proteins and the activation of platelets. The relative amount of thrombus formation was higher on homopolymers than on block copolymers. The amount of thrombus formation became less, with decreasing content of P[Glu(OBzl)] in the PST block copolymers and with increasing content of P[Glu(OBzl)] in the PMMA block copolymers. Adsorption of bovine serum albumin(BSA), bovine gamma-globulin (B gamma G) and bovine plasma fibrinogen(BPF) onto polymer films was also investigated. More proteins were adsorbed and denatured when adsorbed onto PST and PMMA than onto block copolymers. With increasing content of P[Glu(OBzl)] in the PST block copolymers, the degree of denaturation of adsorbed proteins increased, while the amount of protein adsorption was unaffected. Conversely, with increasing content of P[Glu(OBzl)] in the PMMA block copolymers, the degree of denaturation of adsorbed proteins decreased, while similarly the amount of protein adsorption was unaffected. Adhesion of platelets from platelet suspension (WP) to polymer films coated with one of the plasma proteins showed that the activation of adhered platelets was suppressed when there was a lower degree of denaturation of coated proteins. In the same experiments using platelet-rich plasma(PRP), neither the number of platelets adhered nor the degree of activation of the adhered platelets was correlated with the composition of the polymer films.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Interaction of polystyrene/poly(gamma-benzyl L-glutamate) and poly(methyl methacrylate)/poly(gamma-benzyl L-glutamate) block copolymers with plasma proteins and platelets. 243 Jun 30

Adhesion of polymorphonuclear granulocytes (PMNs) in microvessels occurs in the presence of shear forces exerted by the blood flow. To model this in vitro, phorbol myristate acetate (PMA)-activated PMN were exposed to shear stress on cultured human umbilical vein endothelial cells (HUVECs) and on plastic dishes coated with bovine serum albumin (BSA). PMN adhesion to HUVECs averaged 36% of the total PMNs added and was reduced to 21% by shear stress of approximately 1.5 dynes.cm-2. On BSA, adhesion was reduced from 59% to 35%. Dextran sulfate (molecular weight 500,000) inhibited PMN adhesion in a dose-dependent manner when shear stress was applied. At a concentration of 1 mg.ml-1, inhibition was 72% on HUVECs and 76% on BSA. Half-maximal inhibition was reached at approximately 1 microgram.mL-1 dextran sulfate, corresponding to 2 nmol/L. Without shear stress, dextran sulfate had no effect on HUVECs and only a moderate effect on BSA. The murine monoclonal antibody (MoAb) 60.3, recognizing an epitope on the leukocyte adhesion glycoprotein CD18, inhibited PMN adhesion equally well with and without shear. A low dose of MoAb 60.3 enhanced the effect of dextran sulfate without shear stress. Flow cytometry (FACS) did not show inhibition of MoAb 60.3 binding to PMNs by dextran sulfate. These results indicate that a dextran sulfate-inhibitable adhesion process is important for PMN adhesion in the presence of shear stress.
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PMID:Shear-dependent inhibition of granulocyte adhesion to cultured endothelium by dextran sulfate. 246 7

We have prepared protein-peptide conjugates composed of bovine serum albumin (BSA) derivatized with short peptides containing the Arg-Gly-Asp (RGD) sequence derived from the adhesion site of fibronectin. The RGD-BSA conjugates were used to coat tissue culture plastic surfaces which then served as substrata in cell adhesion experiments. Our results indicate that the efficiency of adhesion to RGD-BSA-coated surfaces is highly dependent on the valency of the (RGD)n-BSA conjugates. For example, on surfaces with approximately equal amounts of RGD ligand, CHO cells adhered virtually 100% to the (RGD)n-BSA (n = 20.8) conjugate and not at all to the (RGD)n-BSA (n = 3.5) conjugate. Adhesion on (RGD)n-BSA-coated substrata and on fibronectin- or vitronectin-coated substrata was also examined in terms of the relationship between cell adhesion and the intermolecular distances of adsorbed proteins. It was observed that for substrata coated with relatively compact, symmetric molecules, such as RGD-BSA or vitronectin, adhesion dropped off sharply as intermolecular distances increased; by contrast, for fibronectin, a large asymmetric molecule, adhesion declined more gradually as intermolecular distances increased. Finally, we have examined the role of different cell-surface receptors in the process of adhesion to RGD-BSA substrata. Interestingly, competition and blocking experiments with antibodies and with soluble competing proteins suggest that it is the vitronectin receptor rather than the fibronectin receptor which mediates adhesion to RGD-BSA.
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PMID:(Arg-Gly-Asp)n-albumin conjugates as a model substratum for integrin-mediated cell adhesion. 246 96

We have demonstrated previously that chick embryo fibroblasts synthesize and secrete a large chondroitin sulfate proteoglycan (designated PG-M) that binds to fibronectin. We now report the possibility that PG-M interactions with cell surfaces can modulate cell-substrate adhesion. When PG-M was added to the medium, various types of trypsinized cells failed to adhere not only to fibronectin-coated substrates but also to collagen- or vitronectin-coated substrates. Adhesion of the cells to laminin or glycyl-arginyl-glycyl-aspartyl-serine derivatized serum albumin (arginyl-glycyl-aspartic acid-containing molecules with no capacity to bind PG-M) was also inhibited by PG-M. Treatment of the proteoglycan with either proteolytic enzymes or chondroitinase abolished its inhibitory effects on the cell adhesion. These results suggest that direct binding between PG-M and fibronectin, if any, is not a cause of the inhibition by PG-M and that only the proteoglycan form is responsible for the activity. When the immobilization of added PG-M to available plastic surfaces of coated dishes was blocked by pretreating the dishes with serum albumin, the inhibitory effect of PG-M was abolished, suggesting that the immobilized fraction of PG-M can act as a cell adhesion inhibitor. In immobilized form, both cartilage chondroitin sulfate proteoglycan (designated PG-H) and chondroitin sulfate-derivatized serum albumin also inhibited cell adhesion. In contrast, heparan sulfate proteoglycan form LD and heparan sulfate-derivatized serum albumin had far lower inhibitory activities, indicating that the active site for the interaction between cells and PG-M is on the chondroitin sulfate chains.
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PMID:Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates. 247 Jul 39

Escherichia coli F-18, an excellent colonizer of the streptomycin-treated mouse large intestine, produces type 1 pili. E. coli F-18 FimA-, type 1 pilus negative, and E. coli F-18 FimH-, type 1 pilus positive but adhesin negative, were constructed by bacteriophage P1 transduction of defective fimA and fimH genes from the E. coli K-12 strains ORN151 and ORN133, respectively, into E. coli F-18. Adhesion of E. coli F-18 to an immobilized mannose-bovine serum albumin glycoconjugate was about sixfold greater than that of either E. coli F-18 FimA- or E. coli F-18 FimH-, and adhesion of E. coli F-18 to immobilized cecal epithelial cell brush border membranes was between two- and threefold greater than that of E. coli F-18 FimA- or E. coli F-18 FimH-. When either E. coli F-18 FimA- or E. coli FimH- was fed to streptomycin-treated mice together with E. coli F-18, the pilus-negative and adhesin-negative strains colonized as well as their type 1-piliated parent. Essentially the same result was observed when the type 1-piliated E. coli K-12 strain ORN152 was fed to streptomycin-treated mice together with a nearly isogenic K-12 FimA- strain, ORN151. Furthermore, when streptomycin-treated mice were fed E. coli F-18 FimA- or E. coli F-18 FimH- together with E. coli F-18 Col-, which also makes type 1 pili but is a poor colonizer relative to E. coli F-18 because it grows poorly in mucus in the presence of E. coli F-18, the F-18 FimA- and F-18 FimH- strains colonized well (10(6) to 10(7) CFU/g of feces), whereas the number of E. coli F-18 Col- in feces decreased rapidly to 10(2) CFU/g of feces. These data show that in streptomycin-treated mice, the inability to produce functional type 1 pili has no effect on the ability of E. coli F-18 and E. coli K-12 to colonize the large intestine.
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PMID:Type 1 pili are not necessary for colonization of the streptomycin-treated mouse large intestine by type 1-piliated Escherichia coli F-18 and E. coli K-12. 257 Jul 52

In this paper, interfacial aspects of spreading and adhesion of human skin fibroblasts on solid substrata after protein precoating have been studied. Three solid substrata were used with different surface free energy (gamma s): Tissue Culture Polystyrene (TCPS) with gamma s = 70 erg.cm-2, Polyvinylfluoride (PVF) with gamma s = 56 erg.cm-2 and Fluoroethylenepropylene (FEP) copolymer with gamma s = 18 erg.cm-2. The substrata were precoated with fetal calf serum, bovine fibronectin or bovine serum albumin. Cell spreading was evaluated by means of light microscopy and scanning electron microscopy (SEM). Adhesion sites were studied by transmission electron microscopy (TEM). In general, spreading was lowest on FEP and highest on TCPS. Although protein precoating markedly increased cell spreading, the relative order in which the cells spread on the protein precoated substrata remained identical to that on the bare substrata. Analysis of the kinetics of spreading demonstrated that spreading was fastest on the high-energy substratum and slowest on the low-energy substratum. In the presence of all three types of protein precoating, the average distance between a cell and a substratum after spreading was smaller (20-50 nm) than without a coating (greater than 100 nm).
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PMID:Kinetics of cell spreading on protein precoated substrata: a study of interfacial aspects. 271 33


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