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

Adhesion protein expression by acute myeloid leukaemia (AML) cells may affect bone marrow stromal localization and determine exposure of leukaemic cells to stromal derived myeloid growth factors. We have analysed the surface expression by myeloid leukaemic cells of proteins with known adhesive function and the ability of AML cells to adhere to bone marrow fibroblasts and the extracellular matrix proteins fibronectin and laminin. Cells from all six patients tested adhered to bone marrow fibroblast monolayers (mean binding 28.8 +/- 12.8%) and to purified fibronectin in five cases studied (mean binding 33.8 +/- 15.3%). Cells from four patients with AML also adhered to laminin (mean binding 20.9 +/- 4.0%). AML cells from the majority of patients with leukaemia at diagnosis or relapse expressed the ligand pair LFA-1 and ICAM-1, the CD2 ligand LFA-3, alpha and beta chains of the integrins VLA-4, VLA-5 and VLA-6, and the hyaluronate receptor CD44. Antibodies to CD11a, CD18, VLA-4 alpha, and VLA-5 alpha failed to inhibit binding of AML cells to bone marrow fibroblasts but anti-VLA-5 alpha antibodies inhibited AML cell binding to fibronectin by approximately 50%. The ability of AML cells to adhere to bone marrow fibroblasts and extracellular matrix proteins such as fibronectin and laminin may to help explain the capacity of AML cells to persist in the marrow during periods of apparent complete remission and to subsequently proliferate under the influence of locally secreted myeloid growth factors.
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PMID:Human acute myeloid leukaemia cells express adhesion proteins and bind to bone marrow fibroblast monolayers and extracellular matrix proteins. 835 Jun 18

Adhesion of monocytes to the endothelium is an early event in the development of atherosclerosis. The possibility that low density lipoproteins enhance this process by activating monocytes was investigated using an in vitro adhesion test on endothelial cell monolayer cultures. Preincubation of monocytes with low density lipoprotein (LDL) (100 micrograms LDL protein/l x 10(6) cells/ml) for 15 min induced a 70% increase in adhesion to endothelial cells with a maximal effect at 100 micrograms LDL protein/ml and a short latency of effect (2 min). Anti-LDL receptor antibody, which inhibited LDL binding, blocked this activation. The LDL effect appeared to depend on receptor binding of LDL rather than on receptor-mediated endocytosis, since preincubation of monocytes with LDL at either 4 degrees C or 37 degrees C resulted in the same stimulation of adhesion. A cytofluorimetric study using integrin monoclonal antibodies (MAbs) against CD18 and CD11b did not reveal any increase in expression of the integrins on the surface of LDL-activated monocytes. However, a 30-min preincubation of monocytes with anti-CD18 abolished the LDL-activated adhesion. These results indicate that LDL induces a rapid activation of monocyte adhesiveness to endothelial cells. This effect appears to be mediated by interaction of LDL with its receptor rather than LDL-receptor complex internalization or integrin membrane mobilization from intracellular pools. The integrin system nevertheless appears to be involved.
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PMID:Effect of low density lipoprotein on monocyte adhesiveness to endothelial cells in vitro. 846 Oct 58

Cell-cell adhesion is essential for many immunological functions and is believed to be important in the regulation of hematopoiesis. Adhesive interactions between human endothelial cells and megakaryocytes were characterized in vitro using the CMK megakaryocytic cell line as well as marrow megakaryocytes. Although there was no adhesion between unactivated human umbilical vein endothelial cells (HUVEC) and megakaryocytes, treatment of HUVEC with inflammatory cytokines such as IL-1 beta, tumor necrosis factor alpha, INF-gamma, or the phorbol ester phorbol myristate acetate (PMA) resulted in a time- and dose-dependent increase in adhesion. Stimulation of marrow megakaryocytes or CMK cells with the cytokines IL-1 beta, GM-CSF, IL-6, IL-3, or PMA augmented their adhesion to endothelium. Monoclonal antibodies against the LFA-1 subunit of the leukocyte adherence complex CD18 inhibited the binding of marrow megakaryocytes or CMK cells to HUVEC. Adhesion blocking experiments also demonstrated that the VLA-4/VCAM-1 pathway was important for megakaryocyte attachment to HUVEC. Adhesion promoted maturation of megakaryocytic cells as measured by increased expression of glycoproteins GpIb and GpIIb/IIIa and by increased DNA content. These observations suggest that alterations in megakaryocyte adhesion may occur during inflammatory conditions, mediated by certain cytokines, resulting in augmented megakaryocyte maturation.
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PMID:Characterization of adhesive interactions between human endothelial cells and megakaryocytes. 851 51

During bacterial peritonitis of patients on continuous ambulatory peritoneal dialysis (CAPD) leukocytes, particularly polymorphonuclear neutrophilic granulocytes (PMNs), migrate into the peritoneal cavity. However, at the site of inflammation PMNs are not sufficiently able to protect the host against micro-organisms. Adhesion molecules, such as ICAM-1 (CD54), are involved in the interaction between endothelial cells and PMNs leading to the accumulation of PMNs at the site of inflammation. As PMNs are the predominant cell type in the peritoneal cavity in peritonitis, the aim of this study was to find out whether PMNs from CAPD peritonitis patients were able to express ICAM-1. Flow cytometric analyses with the anti-CD54 monoclonal antibody demonstrated that normal PMNs constitutively express slight amounts of ICAM-1. In contrast to normal PMNs, peritoneal PMNs from patients with CAPD peritonitis expressed high amounts of ICAM-1 (p = 0.003). Furthermore, ICAM-1 expression on peripheral blood PMNs of these patients significantly differed from PMNs from healthy donor (p = 0.01). Furthermore, Northern blot analysis revealed a weak signal of ICAM-1 mRNA in normal PMNs. However, peritoneal PMNs from CAPD peritonitis patients expressed a strong signal for ICAM-1 mRNA, suggesting that ICAM-1 is newly synthesized when PMNs invade the peritoneal cavity. In summary, this study clearly demonstrates that peritoneal PMNs of CAPD peritonitis express high amounts of ICAM-1 receptor on the level of mRNA and on the surface. Therefore, it is tempting to speculate that peritoneal PMNs interact amongst each other between ICAM-1 and its counter receptors CD11a,b/CD18 receptor.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Synthesis and surface expression of ICAM-1 in polymorphonuclear neutrophilic leukocytes in normal subjects and during inflammatory disease. 852 60

Adhesion of peripheral blood eosinophil and neutrophil granulocytes to the endothelial cell adherence receptors E-selectin, vascular cell adhesion molecule-1, and intercellular adhesion molecule-1 has been measured. The study included patients with allergic rhinitis, patients with mild allergic and nonallergic asthma, and healthy individuals; 10 persons were in each group. In addition, assay of eosinophil and neutrophil cell surface expression of the receptor complex CD11b/CD18 was performed. Increased eosinophil adhesion to vascular cell adhesion molecule-1 (p < 0.05) and intercellular adhesion molecule-1 (p < 0.05) was demonstrated in the patients with a more labile asthma, that is, a peak expiratory flow rate variability of more than 10%, suggesting a relationship to the degree of ongoing inflammation in the airways of the patients. The increased eosinophil adhesion was most probably due to a functional upregulation of the CD11b/CD18 and very late activation antigen-4 receptors, because the number of receptors measured as cell surface expression was unaltered. The increased eosinophil adhesion in the patients with high peak expiratory flow rate variability appeared independent of atopy. The increased adhesion was not entirely specific to the eosinophils, because neutrophils from patients with a peak expiratory flow rate variability of more than 10% also demonstrated increased adhesion to intercellular adhesion molecule-1 (p < 0.05) when compared with neutrophils from the patients with low peak expiratory flow rate variability. In conclusion, the demonstrated priming of eosinophil adhesion to vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 might be one contributing mechanism behind the selective accumulation of eosinophils in the lung tissue of patients with asthma.
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PMID:Increased adhesion to vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 of eosinophils from patients with asthma. 854 53

Inflammation is characterized by the migration of polymorphonuclear leukocytes from the vasculature into the tissue causing profound injury. Adhesion and migration of neutrophils across the vascular bed are governed by a series of complex events including cytokine/chemokine production which in turn orchestrates the temporal expression of a cohort of adhesion molecules mediating the migration. Many of these adhesion molecules and their inducers are under the control of inflammatory response transcriptional factors such as NF kappa B and AP-1. Recently we showed tepoxalin, previously known as a dual cyclooxygenase/lipoxygenase (CO/LO) inhibitor, to be a potent inhibitor of NF kappa B-induced transcription in vitro. In this study, we demonstrated that when administered in vivo, tepoxalin but not naproxen (a nonsteroidal anti-inflammatory drug, NSAID) or zileuton (an LO inhibitor), effectively inhibits neutrophil migration into inflammatory sites in murine skin stimulated by either lipopolysaccharide (LPS) or tumor necrosis factor-alpha. Immunohistochemical analysis indicates that 10-50 mg/kg of tepoxalin inhibits neutrophil migration. It also effectively blocks the upregulation of Mac-1 (CD11b/CD18) on neutrophils. Quantitative polymerase chain reaction Mac-1 analysis shows that LPS-induced transcription of E-selectin mRNA was dramatically suppressed by both 25 and 50 mg/kg of tepoxalin, whereas the level of ICAM-1 was only affected by 50 mg/kg of tepoxalin. Since it has been documented that the expression of E-selectin and Mac-1 is regulated either directly or indirectly by the transcription factor NF kappa B, our studies provide in vivo evidence that tepoxalin is a potent inhibitor of NF kappa B-mediated events in animal models and this novel molecular mechanism clearly defines it as a new class of anti-inflammatory compounds.
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PMID:Tepoxalin blocks neutrophil migration into cutaneous inflammatory sites by inhibiting Mac-1 and E-selectin expression. 856 54

While endothelial oxidant generation and subsequent leukocyte chemotaxis and activation are important mechanisms of tissue damage in ischemic organs, it is not known if oxidant generation may be involved in triggering the subsequent leukocyte-mediated injury which occurs. Questions remain whether particular oxidants and oxygen-free radicals are capable of modulating the expression of leukocyte adhesion molecules and effecting leukocyte endothelial adhesion. Studies were performed to determine the effect of different biologically occurring oxidant molecules and oxygen free radicals including: .O2-, .OH, and H2O2 on the expression of integrin and selectin adhesion molecules on the surface of human PMNs and to determine the effect of these alterations on PMN adhesion to the endothelium. Adhesion molecule expression on the surface of human PMNs was measured by immunofluorescence flow cytometry. Electron paramagnetic resonance spectroscopy was applied to characterize the presence of exogenous free radical generation as well as that from activated PMNs. It was observed that these oxidants can cause up-regulation of CD11b and CD18 expression with shedding of L-selectin. The kinetics and dose-response of these effects were analyzed and their functional significance determined by measuring PMN adhesion to cultured human aortic endothelial monolayers. These studies demonstrate that oxygen free radicals and non-radical oxidants can directly trigger PMN activation and adhesion to vascular endothelium.
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PMID:Hydrogen peroxide and superoxide modulate leukocyte adhesion molecule expression and leukocyte endothelial adhesion. 859 2

Megakaryocytes generate cytoplasmic processes (CP) that penetrate endothelial cells in the bone marrow sinus, and these processes may release platelets into the circulation at their terminal stage. Adhesion between the CP and endothelial cells may be important during the extension of CP. We examined the expression of adhesion molecules of the integrin family (CDw49b, CDw49d, CDw49e, CDw49f, CD18, CD11a CD11c, and CD11b), the immunoglobulin superfamily (CD54, CD56, CD58, and CD31), the selectin family (ELAM-1, LECAM-1, and CD62), and CD44, CD41b, and CD42b on platelets, megakaryocytes, and megakaryocytes with CP. No specific adhesion molecules were observed on the megakaryocytes with CP. Three staining patterns of adhesion molecules-homogeneous, speckled, and accumulated-were observed on the megakaryocytes with CP, but not on those without CP. Platelet integrins (i.e., CD41a, CDw49b, CDw49e and CDw49f) and GPIb (CD42b) were strongly and homogeneously stained on the CP. GMP-140 CD62) was weakly stained, in a speckled pattern. CD31 (PECAM-1) was also weakly stained but accumulated selectively on the tip of the CP. ANTI-CD31 suppressed CP formation of megakaryocytes. We speculate that the homodimerization of CD31 expressed on the tips of CP and endothelial cells is important for the extension of the processes and for the migration of megakaryocytes.
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PMID:Expression of adhesion molecules on cytoplasmic processes of human megakaryocytes. 863 24

A monoclonal immunoglobulin G1 (IgG1) antibody (mAb), designated mNI-11, was produced by immunizing mice with the lipopolysaccharide (LPS)-stimulated monocyte-like cell line U937. The reactivity of mNI-11 was tested by the indirect immunofluorescence method. The antigen defined by mNI-11 was found to be expressed on U937 cells, LPS-stimulated U937 cells, normal CD14+ cells (monocytes/macrophages), and human umbilical vein endothelial cells (HUVECs). Expression of the antigen defined by mNI-11 on HUVECs slightly increased in response to exposure to tumor necrosis factor-alpha (TNF-alpha) and phorbol myristate acetate (PMA). When the reactivity of mNI-11 and mAbs binding human differentiation antigens such as CD11a, CD11b, CD11c, CD14, CD16, CD18, CD23, CD28, CD29, CD31, CD43, CD44, CD45RA, CD49d, CD50, CD54, CD58, CD80, CD102, CD106, HLA-class I, or HLA-class II antigen was compared, no mNI-11 reactivity resembling that of these mAbs was found. mNI-11 markedly induced homotypic cell aggregation of U937 cells when they were stimulated with LPS. The mNI-11-induced aggregation of LPS-stimulated U937 cells, referred to as LPS-U937 cells, required neither Fc receptor engagement nor cross-linking of the antigen defined by mNI-11 because aggregation was induced by both F(ab')2 fragments and monovalent F(ab') fragments of mNI-11. The mNI-11-induced aggregation was blocked by the addition of ethylenediaminetetraacetate, and also when incubated at 4 degrees C. mAbs to CD11a/CD18 (lymphocyte-function associated antigen-1; LFA-1) and CD54 (intercellular adhesion molecule-1; ICAM-1) completely blocked the LPS-U937 cell aggregation induced by mNI-11. The LPS-U937 cell aggregation induced by mNI-11 was partially but not completely blocked by the protein kinase C inhibitors sphingosine and H-7, and was completely blocked by the protein-tyrosine kinase inhibitor genistein. Interestingly, mNI-11 markedly promoted LPS-U937 cell adhesion to HUVECs. The mNI-11-induced LPS-U937 cell adhesion to HUVECs was not reduced in the presence of LFA-1 (CD11a/CD18) or ICAM-1 (CD54) mAbs. On the other hand, LPS-U937 cells, whether treated with mNI-11 or not, sufficiently adhered to the extracellular matrix protein fibronectin, but not to laminin or collagen type I. However, mNI-11 did not markedly promote LPS-U937 cell adhesion to fibronectin. Adhesion of LPS-U937 cells treated with mNI-11 to fibronectin was completely blocked by CD29 (beta chain of very late antigens) mAb. The surface antigen recognized by mNI-11 had a molecular size of approximately 97 kDa under non-reducing conditions and approximately 117 kDa under reducing conditions, as determined by immunoblotting analysis. We found that mNI-11 recognizes an adhesion-associated molecule distinct from any previously reported in terms of its pattern of cellular distribution and molecular weight, and also found that mNI-11 has activity which induces cell adhesion/aggregation of U937 cells when stimulated with LPS.
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PMID:Development and characterization of a novel monoclonal antibody (mNI-11) that induces cell adhesion of the LPS-stimulated human monocyte-like cell line U937. 865 55

L-Plastin is a calcium-regulated actin bundling protein expressed in leukocytes and some transformed cells, which is phosphorylated on serine in response to several different leukocyte-activating stimuli. Adhesion to immune complexes induced L-plastin phosphorylation in neutrophils, as did phagocytosis of IgG-opsonized particles, but insoluble immune complexes in suspension were very inefficient activators of L-plastin phosphorylation. Neutrophils express two IgG Fc receptors, the transmembrane FcgammaRII and the glycan phosphoinositol-linked FcgammaRIIIB. Use of monoclonal antibodies that distinguished the two Fc receptors demonstrated that FcgammaRII ligation was 100-fold more potent at signaling L-plastin phosphorylation than occupancy of FcgammaRIIIB. Depletion of intracellular calcium did not affect FcgammaRII-activated L-plastin phosphorylation, demonstrating that any potential regulation of plastin function by calcium did not affect its phosphorylation. Adhesion to immune complexes caused L-plastin to localize to podosomes, since it colocalized with actin to discrete, punctate Triton X-100-insoluble sites on the adherent neutrophil surface in a pattern indistinguishable from vinculin and alpha-actinin. Nonetheless, localization to podosomes was not required for L-plastin phosphorylation, since both neutrophils from a patient with leukocyte adhesion deficiency (CD18 deficiency) and neutrophils treated with anti-CD18 F(ab')2, which do not form podosomes upon adhesion to immune complexes, phosphorylated L-plastin normally. Indeed, L-plastin was normally phosphorylated in response to adhesion to immune complexes even when the actin cytoskeleton was disrupted with cytochalasin D. We conclude that efficient FcgammaRII-mediated phosphorylation of L-plastin requires cell adhesion but does not require IgG-induced rearrangements of the actin cytoskeleton. These data suggest a model in which plastin phosphorylation and localization to the actin cytoskeleton can act as two distinct mechanisms regulating L-plastin functions in neutrophils adherent to immune complexes.
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PMID:FcgammaRII-mediated adhesion and phagocytosis induce L-plastin phosphorylation in human neutrophils. 866 66


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