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

We have previously reported that fibrinogen/fibrin can induce the migration of vascular smooth muscle cells in vitro. In this study, we examined the effect of substrate-bound fibrinogen/fibrin and other cell attachment-promoting proteins on the adhesion of vascular smooth muscle cells. The amount of fibrinogen/fibrin adsorbed to plastic wells and the adhesion of smooth muscle cells to the wells were found to depend on the concentration of fibrinogen used for coating the wells. The effect of fibrinogen/fibrin was comparable to that of so-called cell attachment-promoting proteins (fibronectin, vitronectin, and type I collagen). Adhesion of smooth muscle cells to fibrinogen/fibrin-coated wells was inhibited by the synthetic peptide GRGDS, but not by a control peptide, GRGES. Vitronectin, fibronectin, type I collagen, denatured type I collagen and commercial gelatin also induced smooth muscle cell adhesion. The adhesion induced by vitronectin, denatured type I collagen, and commercial gelatin was inhibited by GRGDS. However, the adhesion induced by type I collagen was not influenced and that induced by fibronectin was only slightly inhibited. These observations suggest that fibrinogen/fibrin deposited extracellularly in the arterial intima may act as a scaffold in the process of smooth muscle cell migration.
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PMID:Substrate-bound fibrinogen, fibrin and other cell attachment-promoting proteins as a scaffold for cultured vascular smooth muscle cells. 128 31

The recognition of exposed collagen by circulating platelets is an initial step in the formation of the hemostatic plug or a thrombus after vascular injury. Theoretical calculations of the speed of platelet function required for effective hemostasis have suggested very short reaction times. However, it is not known how fast platelets can adhere to collagen under arterial flow conditions or which membrane proteins are involved. We have used a continuous-flow, microaffinity column linked to a resistive-particle counter to detect platelet adhesion. Adhesion of human platelets to native type I collagen was extremely rapid, with exponential half-times as short as 240 ms, and was nearly complete by 2 s. This RGD-independent process was not associated with platelet aggregation or secretion. The monoclonal antibody 6F1 directed against the glycoprotein Ia/IIa complex inhibited adhesion, suggesting that this complex plays an important role in the initial phases of platelet-collagen interaction under flow conditions. In addition, divalent cations were required for adhesion, as indicated by inhibition with EDTA in plasma and the dependence on Mg2+ for washed platelets.
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PMID:High-speed platelet adhesion under conditions of rapid flow. 163 Oct 56

Altered T cell adherence after human immunodeficiency virus 1 (HIV-1) infection may contribute to viral pathogenesis in the acquired immune deficiency syndrome. To address this hypothesis, we assessed mechanisms of T cell adherence to extracellular matrix proteins in vitro. We found that after HIV-1 infection, both chronically infected H9 CD4+ T cells and acutely infected primary peripheral blood lymphocytes acquired the ability to adhere to the extracellular matrix glycoprotein fibronectin, to a lesser extent to type IV collagen and laminin, but not to type I collagen. H9 cells chronically infected with two of the three HIV-1 strains studied showed approximately a sevenfold increase in attachment to fibronectin, while the same cells infected with the human retrovirus HIV-2 did not. Adhesion was accompanied by changes in morphology, including marked spreading and increased filopodia. These alterations were not blocked by the protein kinase C inhibitor H-7, which did inhibit TPA-induced T cell attachment to fibronectin. Monoclonal antibodies against both the alpha 5 and the beta 1 subunits of the classical fibronectin receptor as well as an Arg-Gly-Asp (RGD) peptide inhibited attachment, whereas anti-alpha 4 monoclonal antibodies and the CS1 peptide did not. Binding to collagen IV was also inhibited by the anti-beta 1 monoclonal antibody, but not the other antibodies. Cells metabolically labeled with [35S]methionine and analyzed by immunoprecipitation with polyclonal anti-beta 1 integrin antibody showed a 2.5-fold increase in integrin synthesis in infected cells compared to uninfected controls. This increase in synthesis was associated with an increase in cell surface expression of both alpha 5 and beta 1 integrins by FACS (registered trademark of Becton Dickinson for a fluorescence-activated cell sorter) analysis. Enhanced expression of integrins such as alpha 5 beta 1 may cause T cell adherence to a variety of tissues, where released viral gene products may induce some of the tissue-specific manifestations of HIV-1 infection.
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PMID:HIV-1 infection of human T lymphocytes results in enhanced alpha 5 beta 1 integrin expression. 183 Dec 4

Microvascular endothelial cells from human omental samples were isolated and grown. Adhesion to polytetrafluoroethylene vascular graft material was then studied using scanning electron microscopy and adhesion of cells labelled with indium-111. Grafts coated with fibronectin and type I collagen were found to promote the best adhesion of cells at times up to 90 min. A coating of blood clot matrix was less effective but still resulted in a threefold increase in cell adhesion compared with controls.
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PMID:Seeding of human microvascular endothelial cells onto polytetrafluoroethylene graft material. 146 24

Strains of Streptococcus cricetus and Streptococcus rattus exhibited striking differences in their ability to bind to different types of collagen. For example, S. cricetus AHT bound in highest numbers to hydroxyapatite (HA) treated with human type V collagen, while rat type I collagen was ineffective. In contrast, human type V collagen was least effective in promoting attachment of S. rattus LB-1, while treatment with rat or human type I collagen was effective. Adsorption of both species to human type I collagen-treated HA showed a high correlation with a Langmuir model. Estimates of adsorption parameters indicated there were greater numbers of binding sites with higher affinity for S. rattus LB-1 than for S. cricetus AHT. Treatment of HA with either the alpha 1 (1) or alpha 2 (1) polypeptide chains of collagen was effective in promoting adhesion of S. rattus LB-1 cells. In contrast, the alpha 2 (1) chain was more effective than the alpha 1 (1), chain for S. cricetus AHT. These observations indicate that S. cricetus AHT and S. rattus LB-1 cells bind to different segments of collagen molecules. Adhesion of both species was also promoted by collagen-rich fractions of human dentin.
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PMID:Streptococcus cricetus and Streptococcus rattus bind to different segments of collagen molecules. 196 4

We recently described specific binding sites for Clq on human blood platelets that cross-react with antibodies against Clq receptors (ClqR) on lymphoblastoid cells. Inasmuch as Clq inhibits collagen-induced platelet aggregation, we compared the effects of ClqR occupancy by purified Clq, monoclonal (IIl/B5) and polyclonal anti-ClqR antibodies on collagen-induced platelet adhesion, release, and aggregation. Washed platelets in buffered Tyrode's solution containing 2 mM magnesium were preincubated (30 min, 22 degrees C) with antibodies, Clq, or appropriate control buffers and antiserum. Platelet aggregation and release measurements were made using 14C-serotonin-labeled platelets stimulated with type I collagen. Adhesion assays were performed in the presence of magnesium under static conditions at 22 degrees C with 51Cr-labeled platelets and collagen-coated microtiter wells. Concentrations of IIl/B5, polyclonal anti-Clq R antiserum, or Clq causing 82 to 92% (n = 7) inhibition of collagen-induced release and 67 to 98% inhibition of aggregation, failed to inhibit magnesium-dependent platelet adhesion to collagen. Inasmuch as divalent cation-independent platelet-collagen interactions have also been described, further studies were performed to compare the divalent cation requirement of ClqR occupancy by Clq and inhibition of platelet-collagen interactions. Whereas, Clq binding to platelets was divalent cation independent, neither Clq nor anti-ClqR antibodies prevented platelet adhesion to collagen in the presence of EDTA. These data suggest that under defined in vitro conditions, ClqR modulate collagen-induced platelet aggregation and secretion, but not platelet adhesion.
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PMID:Modulation of platelet responses to collagen by Clq receptors. 240 63

Platelet membrane components adhering with high affinity to collagen fibers were studied by means of an affinity column in which fibrillar type I collagen was physically immobilized. Intact rabbit platelets in 1 mM EGTA adhered to the column but did not aggregate. Adhesion was dependent on the collagen concentration and on the number of platelets applied. Passage through the column without adhesion did not affect the potential for subsequent platelet binding. Surface-labelled whole platelets were passaged through this column, lysed in Triton and in SDS and labelled components adhering to the collagen were analysed on SDS-polyacrylamide gels. It was found that Triton lysis removed most of the major surface glycoproteins but left the cytoskeleton on the column. Subsequent SDS elution removed the cytoskeletal proteins along with the remaining major surface glycoproteins. The label left on the column could not be eluted with 8 M urea or up to 4 M NaCl. Collagenase digestion of the column collagen released a single surface glycoprotein of Mr 80,000. Limited chymotryptic digestion of the labelled platelets prior to their application to the column did not affect their binding. A radiolabelled band of the same molecular weight (MW) became bound to the collagen following passage of the chymotrypsin-treated platelets. This band was trypsin-sensitive following SDS-polyacrylamide gel electrophoresis (SDS-PAGE). These results, along with other published evidence, suggest that at least one platelet membrane component, expressed on the surface of the unstimulated platelet, binds with high affinity to fibrillar type I collagen and is probably involved in platelet collagen recognition.
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PMID:Identification of a surface protein of the rabbit blood platelet with high affinity for collagen. 302 23

Freshly isolated bone cells from embryonic chick calvariae were found to attach to films of native monomeric type I or II collagen, to gels of native type I collagen and, to a lesser extent, to air-dried films of these collagens, in a fibronectin-independent manner, and with no requirement for collagen synthesis. Adhesion to type III collagen was relatively poor. Films of native monomeric type I or II collagen were preferred to the corresponding air-dried films as substrata for proliferation. Cis-hydroxyproline inhibited growth upon both plastic and type I and type II collagenous substrata, but this effect could largely be overcome by providing bone cell-conditioned medium, suggesting the possibility of a requirement in the growth process for synthesis of a collagen other than type I, the major form in bone matrix.
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PMID:Interaction of embryonic chick calvarial bone cells with collagen substrata; attachment characteristics and growth behaviour. 338 71

In the present study we show that adhesion of normal rat liver epithelial cells (RL34) to substratum coated with type I collagen (collagen substratum) is promoted by a factor involved in 80% ammonium sulfate precipitated proteins from serum-free conditioned medium (PCM) of rat embryo fibroblasts. Adhesion of RL34 cells to collagen substratum was promoted dose dependently by whole PCM and the maximum effects on adhesion could be achieved by 200 micrograms/ml whole PCM. Kinetics studies with 100 micrograms/ml whole PCM showed that adhesion proceeded very slowly, taking 16 h to reach a plateau. Adhesion-promoting activity in whole PCM was sensitive to treatments with trypsin, acid, and heat but stable to dithiothreitol treatment. Further purification of whole PCM was performed using a combination of chromatography on blue Sepharose column, gel filtration column and heparin Sepharose column. The partially purified proteins, referred to as heparin PCM, are not bound or only weakly bound to heparin under physiological ion strength and pH, and the apparent molecular weight (Mr) range is estimated to be 40,000 to 60,000 from gel filtration chromatography and SDS-polyacrylamide gel electrophoresis. When whole PCM or heparin PCM was used for coating on plastic or collagen substratum, they no longer exerted the promoting activity.
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PMID:Adhesion-promoting factor from embryonic fibroblasts for normal liver epithelial cells. 359 33

Adhesion of human platelets to type I collagen under arterial flow conditions is extremely fast, being mediated primarily by the alpha 2 beta 1 integrin (glycoprotein Ia/IIa). We have investigated the involvement of cyclic nucleotides in platelet adhesion to soluble native collagen immobilized on Sepharose beads using a new microadhesion assay under arterial flow conditions. To prevent platelet stimulation by thromboxanes and adenosine diphosphate (ADP), experiments were performed with aspirin-treated platelets in the presence of ADP-removing enzyme systems such as creatine phosphate/creatine phosphokinase or apyrase. Rapid reciprocal changes in platelet adenosine 3'5'-cyclic monophosphate (cAMP) and guanosine 3'5'-cyclic monophosphate (cGMP) occurred during adhesion. cAMP levels in adherent platelets were 2.4-fold lower than in effluent platelets or in static controls, whereas cGMP levels were increased 2.4-fold. These results suggest that contact between platelets and collagen stimulates guanylate cyclase and inhibits adenylate cyclase. This occurs in the absence of the platelet release reaction. We also studied short-term effects of agents that regulate cyclic nucleotide synthesis, prostaglandin E1 (PGE1) and sodium nitroprusside (SNP). After only 3.8 seconds at 10 to 30 dyne/cm2, PGE1 (10 mumol/L) increased cAMP 16.4-fold, whereas SNP (50 mumol/L) increased cGMP ninefold and caused a 3.2-fold increase in cAMP. Both PGE1 and SNP rapidly (< 5 seconds) inhibited platelet adhesion in a dose-dependent manner that was correlated with the increase in cyclic nucleotides. Our data suggest that cAMP and cGMP play a regulatory role in the initial phases of platelet adhesion to collagen mediated by the alpha 2 beta 1 integrin receptor.
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PMID:Role of cyclic nucleotides in rapid platelet adhesion to collagen. 751 2


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