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

Adhesion of pathogens to proteins and glycoconjugates on the host cell plasma membrane or to components of the extracellular matrix is a critical early step in the initiation of infection. For intracellular pathogens, adhesion to the cell surface is a prerequisite to gaining entry into the cell. In all cases, adhesion to host tissue prevents elimination of the pathogens by normal clearance processes and may help the organism to evade immune surveillance by the host. Many laboratories are investigating the ligand binding specificities of bacterial receptors or adhesions and have described diverse binding specificities for adhesive proteins in the host extracellular matrix including laminin and fibronectin. Many bacteria also have adhesins that bind to carbohydrates occurring on glycolipids and glycoproteins in the apical membranes of epithelia in tissues that are targets for infection. Definition of these binding specificities and identification of the receptors that mediate adhesion may lead to development of a novel class of antibiotics whose mechanism of action is to compete with the endogenous ligands for binding to the pathogen receptors or to otherwise prevent adhesion to host tissues and thereby prevent infection.
Am J Respir Cell Mol Biol 1990 Sep
PMID:Interactions of respiratory pathogens with host cell surface and extracellular matrix components. 220 37

The adhesion of leukocytes to endothelium is a physiological phenomenon which is the first step for leukocyte emigration. The adhesion can be dramatically increased in pathological situations such as inflammation and vascular diseases. The molecular basis of leukocyte-endothelium interaction has been largely investigated in the last ten years. Using monoclonal antibodies it is possible to characterize the leukocyte adhesion molecule (LeuCAM) also named CD11/CD18 complex. These molecules responsible for leukocyte adhesion are heterodimers consisting of a common beta subunit and different subunit CD11a/CD18 corresponding to LFA-1; CD11b/CD18 to Mac1/Mol; CD11c/CD18 to GP150-95. Beside these receptors, other leukocyte structures such as the fibronectin receptors are involved in the adhesive process. On the endothelial cell side specialized structures implicated in leukocyte adhesion have been identified. Structures like Intercellular Adhesion Molecule (ICAM) are expressed on endothelial cells in the absence of stimulation, while other receptors Endothelial Leukocyte Adhesion Molecule (ELAM) are only detectable on activated endothelial cells. Cytokines such as IL-1 induced the expression of ELAM, increased the number of ICAM and Human Leukocyte Antigens (HLA) DR, DP, DQ. In various pathological circumstances, namely extracorporeal circulation, Acute Respiratory Distress Syndrome (ARDS), hypercholesterolemia and diabetes mellitus increased leukocyte adhesion has been reported and is potentially responsible for vascular damage. Therefore, the modulation of leukocyte-endothelial cell interactions is a possible target for antithrombotic and antiatherosclerotic therapy.
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PMID:Leukocyte adhesion to endothelial cells. 226 8

To detect molecules of Entamoeba histolytica involved in the trophozoite-target cell interaction, three different antisera were generated: (a) two rabbit antisera, one against total amebic proteins and another directed specifically to the 112-kDa adhesin; and (b) a mouse antiserum against amebic molecules adhering to the red blood cell (RBC) surface after incubation of RBCs with total soluble protein from trophozoites (anti-adhesion serum). All three antisera recognized the 112-kDa adhesion. Adhesion of this molecule to the RBC surface was temperature-dependent. More of the 112-kDa adhesion was found on the surface of RBCs incubated with trophozoites at 37 degrees C than on RBCs incubated at room temperature or at 0 degree C. Experiments using both anti-adhesin and anti-total ambebic protein sera revealed the presence of 210, 160, 112, 90, 70, 50, and 24-kDa proteins on RBC incubated with trophozoites. Surface proteins obtained from iodinated MDCK cells recognized amebic proteins of 112, 90, and 48-50 kDa. Virulence-deficient mutants presented a similar amount of the 112-kDa adhesin to the wild-type strain. However, in mutants, the adhesion was not functional, since they did not adhere to RBCs. 90- and 24-kDa proteins were also found to be altered in mutants.
Mol Biochem Parasitol 1989 Nov
PMID:Entamoeba histolytica: molecules involved in the target cell-parasite relationship. 255 29

This review of retinal pigment epithelial (RPE) physiology pays tribute to Anthony L. F. Gorman, who introduced the author to the giant neuron of Anisodoris nobilis (the sea lemon) and cellular neurobiology. The RPE is an epithelial monolayer with tight junctions, which controls the environment of the photoreceptor outer segments. The apical and basal membranes have different electrical properties and generate a standing potential across the eye. The RPE helps maintain adhesion between the retina and the wall of the eye. Adhesion is weakened by cyanide, low pH or low calcium, but enhanced by ouabain or acetazolamide. The RPE transports water from the subretinal space toward the choroid. This water movement is inhibited by hypoxia or cyanide but enhanced by ouabain or acetazolamide. The c-wave of the electroretinogram is a composite of a cornea-positive wave produced by hyperpolarization of the apical RPE membrane and a cornea-negative wave produced by the Muller cells, both in response to the fall in extracellular potassium that follows illumination of the photoreceptors. The "light response" of the standing potential is produced by depolarization of the basal membrane of the RPE. These examples illustrate how principles of cellular neurophysiology can be applied to questions of clinical relevance.
Cell Mol Neurobiol 1983 Dec
PMID:From sea lemons to c-waves. 632 7

Adhesion molecules like the members of the selectin family participate in the interaction between leukocytes and the endothelium. They are also involved in the pathogenesis of atherosclerotic processes. To contribute to the analysis of the genetic background of atherosclerosis we searched for DNA polymorphisms in the genes encoding adhesion molecules especially E-selectin which seems to be expressed only in activated endothelium. An adenine to cytosine substitution for cDNA position 561 resulting in an amino acid exchange from serine to arginine (position 128) was detected in the epidermal growth factor like domain. A significantly higher mutation frequency (P = 0.02) was observed in 97 patients aged 50 years or less with angiographically proven severe atherosclerosis (allele frequency of arginine 0.155) compared with an unselected population (allele frequency of arginine 0.088) as well as in 40 patients aged 40 years or less (allele frequency of arginine 0.21, P = 0.0025). These data suggest that the 128-serine/arginine polymorphism is associated with a higher risk for early severe atherosclerosis.
Hum Mol Genet 1994 Nov
PMID:E-selectin polymorphism and atherosclerosis: an association study. 753 25

Understanding the molecular mechanisms of pulmonary lymphocyte recruitment is a crucial step toward selective control of immune lung diseases and infections in immunocompromised hosts. To dissect these mechanisms, we are studying the response induced in primed C57BL/6 mice by intratracheal challenge with the T cell-dependent antigen, sheep red blood cells (SRBC). This study used four-parameter flow cytometry to examine expression by CD4+ murine T cells in peripheral blood and lungs of receptors known to be differentially expressed on primed human lymphocytes (CD2, CD11a, CD44, CD45RB, CD49d, and L-selectin). Compared with peripheral blood, more lung CD4+ T cells recovered by bronchoalveolar lavage (BAL) showed a primed phenotype. Judged by low expression of CD45RB or L-selectin, 76 to 90% of BAL CD4+ T cells were primed at all times. Adhesion receptor phenotype of CD4+ T cells in BAL and lung interstitium agreed closely, although BAL contained a greater percentage of primed cells. The percentage of CD4+ T cells with high expression of CD44+ and CD49d increased late in the response. However, when considering only upregulated adhesion receptors which might mediate recruitment, 22 to 52% of CD4+ T cells in BAL did not have increased adhesion receptor expression. Longer duration between priming and challenge did not increase adhesion receptor upregulation. High adhesion receptor expression was least evident during the periods of maximal lymphocyte influx, suggesting that factors other than increased surface density of organ-nonspecific adhesion receptors contribute to lymphocyte recruitment during pulmonary immune responses.
Am J Respir Cell Mol Biol 1995 May
PMID:Adhesion receptor phenotypes of murine lung CD4+ T cells during the pulmonary immune response to sheep erythrocytes. 753 69

Adhesion to extracellular matrix mediates cell cycle progression in mid-late G1; this effect involves an integrin-dependent organization of the cytoskeleton and a consequent change in cell shape. In an effort to identify potential signal-transducing agents that are associated with integrin-dependent shape changes, we looked for kinase activities that were stimulated by long-term adhesion of G0-synchronized NIH-3T3 cells to fibronectin-coated dishes. Several kinase activities were stimulated by this procedure, two of which migrated at 42 and 44 kDa and phosphorylated myelin basic protein in vitro. Blotting with anti-phosphotyrosine and anti-mitogen-activated protein (MAP) kinase antibodies identified these enzymes as ERK 1 and ERK 2. In contrast to the rapid and transient activation of these MAP kinases by platelet-derived growth factor, stimulation of MAP kinase activity by fibronectin was gradual, persistent, and associated with cell spreading rather than cell attachment itself. Cytochalasin D blocked the activation of MAP kinase activity that was induced by the binding of cells to fibronectin. Moreover, MAP kinase was also activated by adhesion of cells to vitronectin and type IV collagen; these effects were also associated with cell spreading. These results distinguish the regulation of G1 phase MAP kinase activity by soluble mitogens and extracellular matrix. They also implicate MAP kinase in shape-dependent cell cycle progression.
Mol Biol Cell 1995 Mar
PMID:Integrin-dependent activation of MAP kinase: a link to shape-dependent cell proliferation. 761 63

Adhesion of cells to components of the extracellular matrix has been shown to be critical in normal lung development, particularly during the pseudoglandular stage, when conducting airways are forming through a process of branching morphogenesis. Expression of factors that inhibit cellular adhesion might also modulate branching morphogenesis. SPARC is a secreted glycoprotein that exhibits antiadhesive effects on cultured cells and is widely expressed in embryonic tissues. In this report, we examine the distribution of SPARC in fetal rat lung during development and its effect on the process of branching morphogenesis. Immunohistochemistry and in situ hybridization studies revealed that SPARC was present in the airway epithelial cells during the pseudoglandular stage of lung development, and in blood vessels and smooth muscle cells associated with airways during the canalicular and saccular stages of development. We used an in vitro model of rat lung branching morphogenesis to examine airway branching in the presence of: a) a neutralizing anti-SPARC antibody; or b) a synthetic peptide from a region of SPARC that, like the native protein, perturbs cell adhesion and diminishes the synthesis of fibronectin and thrombospondin 1. Lungs cultured in the presence of either reagent exhibited diminished branching and an abnormal morphology that was characterized in part by dilated airways. These findings implicate SPARC in the development of the airways.
Am J Respir Cell Mol Biol 1995 Sep
PMID:SPARC participates in the branching morphogenesis of developing fetal rat lung. 765 84

Early experience with recombinant adenoviruses for gene transfer to airway epithelium suggests that these vectors are associated with the development of inflammation. The mechanisms for this are unclear, but previous work has shown that respiratory viruses can cause increased expression of intercellular adhesion molecule-1 (ICAM-1) on airway epithelial cells. We therefore hypothesized that recombinant adenoviruses may induce ICAM-1 expression and thereby facilitate the development of airway inflammation. To address this, primary cultures of human bronchial epithelial cells were examined for ICAM-1 expression by flow cytometry after infection with a serotype 5, E1/E3-deleted recombinant adenovirus containing the Escherichia coli LacZ reporter gene driven by the cytomegalovirus promoter (Ad.CMVlacZ). Compared with control cells, ICAM-1 expression was unchanged after infection with Ad.CMVlacZ, but increased after infection with wild-type adenovirus. Treatment of Ad.CMVlacZ-infected cells with interferon-gamma (IFN) resulted in increased ICAM-1 expression, but to a lower level than that seen in cells treated with IFN alone, indicating that recombinant adenovirus infection blunted IFN-induced up-regulation of ICAM-1. Adhesion of human leukocytes to human bronchial epithelial cells was not increased after Ad.CMVlacZ infection, thereby excluding an ICAM-1-independent increase in leukocyte-epithelial adhesion. The results for ICAM-1 expression were confirmed in vivo, as immunostaining of human bronchial xenografts infected with Ad.CMVlacZ revealed basilar epithelial staining with ICAM-1, but no increased expression on cells expressing beta-galactosidase. This study demonstrates that unlike other respiratory viruses, recombinant E1/E3-deleted adenovirus does not cause increased ICAM-1 expression on human bronchial epithelium in vitro or in vivo nor increased leukocyte adhesion in vitro.
Am J Respir Cell Mol Biol 1995 Feb
PMID:ICAM-1 expression on bronchial epithelium after recombinant adenovirus infection. 786 13

The ligand specificity of the alpha 3A beta 1 integrin was analyzed using K562 cells transfected with full-length alpha 3A cDNA and was compared with that of alpha 6A beta 1 in similarly transfected K562 cells. Clones were obtained that showed comparable surface expression of either alpha 3A beta 1 or alpha 6A beta 1 integrins. Those expressing alpha 3A beta 1 attached to and spread on immunopurified human kalinin and cellular matrices containing human kalinin, which is a particular isoform of laminin. In addition, alpha 3A transfectants adhered to bovine kidney laminins possessing a novel A chain variant. Binding to kalinin was blocked by a monoclonal antibody against the A chain constituent of kalinin and adhesion to both kalinin and kidney laminins by anti-alpha 3 and beta 1 monoclonal antibodies. The alpha 3A transfected cells bound more strongly to kalinin and bovine kidney laminins after treatment with the beta 1 stimulatory antibody TS2/16. A distinctly weaker and activation-dependent adhesion of alpha 3A transfectants was observed on human placental laminins possessing the Am chain variant (merosin), and no adhesion occurred on bovine heart laminins and murine EHS tumor laminin. Further inactive substrates were fibronectin, nidogen, and collagen types IV and VI, indicating that the alpha 3A beta 1 integrin is a much less promiscuous receptor than thought before. By contrast, alpha 6A transfected cells adhered to all laminin isoforms when stimulated with TS2/16. Adhesion also occurred only on bovine kidney laminins in the absence of TS2/16. These results demonstrate that both alpha 3A beta 1 and alpha 6A beta 1 integrins are typical laminin receptors but that their affinity and activation dependence for binding to various laminin isoforms differ considerably.
Mol Biol Cell 1994 Feb
PMID:Distinct and overlapping ligand specificities of the alpha 3A beta 1 and alpha 6A beta 1 integrins: recognition of laminin isoforms. 801 6


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