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

Adhesion of cells to extracellular matrix proteins is mediated, in large part, by transmembrane receptors of the integrin family. The identification of specific integrins expressed in early embryos is an important first step to understanding the roles of these receptors in developmental processes. We have used polymerase chain reaction methods and degenerate oligodeoxynucleotide primers to identify and clone Xenopus integrin alpha subunits from neurula-stage (stage 17) cDNA. Partial cDNAs encoding integrin subunits alpha 2, alpha 3, alpha 4, alpha 5, alpha 6 and an alpha IIb-related subunit were cloned and used to investigate integrin mRNA expression in early embryos by RNase protection assay and whole-mount in situ hybridization methods. Considerable integrin diversity is apparent early in development with integrins alpha 2, alpha 3, alpha 4, alpha 5 and alpha 6 each expressed by the end of gastrulation. Both alpha 3 and alpha 5 are expressed as maternal mRNAs. Zygotic expression of alpha 2, alpha 3, alpha 4 and alpha 6 transcripts begins during gastrulation. Integrin alpha 5 is expressed at relatively high levels during cleavage, blastula and gastrula stages suggesting that it may represent the major integrin expressed in the early embryo. We demonstrated previously that integrin beta 1 protein synthesis remains constant following induction of stage 8 animal cap cells with activin (Smith, J. C., Symes, K., Hynes, R. O. and DeSimone, D. W. (1990) Development 108, 289-298.). Here we report that integrin alpha 3, alpha 4 and alpha 6 mRNA levels increase following induction with 10 U/ml activin-A whereas alpha 5, beta 1 and beta 3 mRNA levels remain unchanged. Whole-mount in situ hybridization reveals that alpha 3 mRNAs are expressed by cells of the involuting mesoderm in the dorsal lip region of early gastrulae. As gastrulation proceeds, alpha 3 expression is localized to a stripe of presumptive notochordal cells along the dorsal midline. In neurulae, alpha 3 mRNA is highly expressed in the notochord but becomes progressively more restricted to the caudalmost portion of this tissue as development proceeds from tailbud to tadpole stages. In addition, alpha 3 is expressed in the forebrain region of later stage embryos. These data suggest that integrin-mediated adhesion may be involved in the process of mesoderm involution at gastrulation and the organization of tissues during embryogenesis.
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PMID:Integrin alpha subunit mRNAs are differentially expressed in early Xenopus embryos. 840 28

Adhesion molecules of the integrin family, including very late activation antigens (VLA), have been implicated in various cellular functions. In this study, we investigated the contribution of integrin-mediated interaction with ECM proteins to the cytokine gene expression in human chondrocytes. Human articular chondrocytes expressed VLA-1, -2, -3 and -5 on the cell surface, and could adhere to various ECM proteins, especially to fibronectin (FN). Furthermore, the production of GM-CSF and IL-6 was potently induced by culturing chondrocytes on immobilized FN. This stimulative effect of FN was completely inhibited by an anti-integrin alpha 5 chain mAb, as well as by anti-integrin beta 1 chain mAbs. These results indicate an important role of the VLA-5-mediated interaction with FN in regulating inflammatory cytokine production by human articular chondrocytes.
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PMID:VLA-5-mediated interaction with fibronectin induces cytokine production by human chondrocytes. 861 19

Within the brain, dissemination of glioma cells follows myelinated fiber tracts and extracellular matrix containing structures such as the basement membranes of blood vessels. These patterns represent the two major routes of invasion frequently observed in clinical disease. Previously, we have characterized the substrates for preferential glioma adhesion and migration on purified ECM protein. In this study sections of human brain from different anatomical regions were used as adhesive substrates and also characterized for the presence and distribution of matrix proteins. Adhesion of marker gene transfected glioma cell suspensions to different regions and anatomical structures of human brain was quantified using a computer assisted image analysis system. Monoclonal antibodies against different adhesion molecules were used to inhibit glioma cell attachment ot specific anatomical structures. In addition, glioma cell aggregates were allowed to adhere to brain sections and single cells were observed to migrate out of these aggregates. Scanning electron microscopy was used to morphologically study the preferred routes of glioma dissemination on brain sections. In brain sections different kinetics of cell adhesion to distinct structures were observed. Within 15 minutes cells adhered and spread on blood vessels and arachnoid tissue containing sections. Choroid plexus and the ventricular wall were also adhesive structures. Adhesion to cortex required 1 hour, while adhesion and spreading on myelinated fiber tracts was retarded and required several hours of incubation. The predominant matrix proteins in small vessels were found to be laminin, collagen type IV, and fibronectin. Choroid plexus and the ependyma showed a similar composition of matrix proteins. Arachnoid fibers contained different types of collagens, predominately type I and III, whereas the only matrix protein identified in the subependyma was fibronectin. Antibodies to the alpha 2, alpha 3, and beta 1 integrin subunits completely blocked adhesion to arachnoid tissue, anti-NCAM inhibited attachment to cortex. Adhesion to blood vessels in brain sections could only be inhibited to 50% by anti-integrin beta 1. Antibodies to the av containing integrin av beta 3 also blocked 50% of adhesion to vessels. Our findings indicate that adhesion of glioma cells to brain sections most rapidly takes place on ECM protein containing regions, especially blood vessels which may serve as guiding structures for glioma dissemination.
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PMID:Glioma cell adhesion and migration on human brain sections. 970 90

Laminin-10/11, the laminin isoforms containing the alpha 5 chain, are major components of basement membranes of many fetal and adult tissues. Laminin-10/11 purified from the conditioned medium of human lung carcinoma cells were potent in mediating adhesion of the carcinoma cells in an integrin alpha 3 beta 1-dependent manner. To further define the type(s) of integrins involved in cell adhesion to laminin-10/11, we examined the effects of a panel of function-blocking anti-integrin antibodies on the adhesion of different cell types to laminin-10/11. Although anti-integrin beta 1 antibody inhibited the adhesion of all cell types tested, anti-alpha 3 antibody inhibited the adhesion of carcinoma and glioma cells but not fibroblastic cells. Adhesion of fibroblastic cells was inhibited, however, by a combination of anti-alpha 3 and anti-alpha 6 antibodies, suggesting that both alpha 3 beta 1 and alpha 6 beta 1 integrins function as laminin-10/11 receptors in these cells. To explore this possibility, we examined the adhesion of K562 leukemic cells transfected with integrin alpha 3 or alpha 6 subunit to laminin-10/11 or other laminin isoforms. Laminin-10/11 were potent adhesive ligands for both the alpha 3 beta 11 and alpha 6 beta 1 transfectants, whereas laminin-5 was the preferred ligand for the alpha 3 beta 1 transfectants. Upon stimulation with the activating anti-integrin beta 1 antibody, both transfectants became more adherent to the substratum regardless of the type of laminins coated, although their preference for laminin isoforms remained unaltered. K562 cells transfected with alpha 6 and beta 4 subunits were also capable of adhering to laminin-10/11, indicating that integrin alpha 6 beta 4 is another receptor for laminin-10/11. Even with lung carcinoma cells, the alpha 6-containing integrins partly contributed to adhesion to laminin-10/11 at higher coating concentrations, although non-integrin receptor(s) might also be involved under such conditions. These results indicated that laminin-10/11 are potent and versatile adhesive ligands in basement membranes capable of binding to both alpha 3 beta 1 and alpha 6 beta 1 integrins with high avidity and also to alpha 6 beta 4 integrin.
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PMID:Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. 1067 76

Adhesion molecules are proteins on the cell surface that are involved in the interactions between lymphocytes and antigen-presenting cells, especially in inflammatory skin diseases and autoimmune bullous disorders. Adhesion molecules include cadherins (subgroups E, N, P, M), integrins, selectins, and the immunoglobulin gene family. Cadherins E in the epidermis including desmocollin 1 and 2 and desmoglein 1 and 3 are essential transmembrane components of desmosome glycoproteins, which play a major role in bullous diseases, pemphigus in particular. Also important are integrin beta 1 alpha 1 and other integrins, which connect ligands of the collagen, laminin, and fibronectin. Selectins (E, P) are important for leukocyte migration on endothelial cells. Adhesion molecules from the immunoglobulin superfamily (intercellular adhesion molecule-1, 3 [ICAM-1,3]; vascular adhesion molecule-1 [VCAM-1]) have significant roles in the immune and inflammatory mechanisms.
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PMID:Adhesion molecules in keratinocytes. 2167 70


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