http://purl.uniprot.org/citations/12392763 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12392763 | http://www.w3.org/2000/01/rdf-schema#comment | "E-cadherin is a 120-kDa transmembrane glycoprotein expressed mainly on the surface of epithelial cells. The best characterised function of E-cadherin is homotypic, calcium-dependent cell-cell adhesion; however, the observation that E-cadherin is also capable of interacting with the alphaEbeta7 integrin to mediate leukocyte cell-cell adhesion [Nature 372 (1994) 190] suggests that it also participates in heterotypic interactions. To investigate the possibility that E-cadherin may interact with integrins expressed on non-leukocytic cells, cell adhesion and solid-phase receptor-ligand binding experiments were performed using a pentameric E-cadherin construct designed to detect low affinity, high avidity interactions. HT1080 human fibrosarcoma cells specifically adhered to pentameric E-cadherin, and this adhesion was inhibited by anti-functional monoclonal antibodies directed against the integrin alpha2 and beta1 subunits, but not by a series of antibodies recognising other subunits. This suggested that the E-cadherin receptor was alpha2beta1, a previously characterised collagen/laminin receptor. Pentameric E-cadherin, but not monomeric E-cadherin, specifically bound, in a divalent cation-dependent manner, to both purified alpha2beta1 and to a recombinant form of the A-domain of the alpha2 subunit, which has been shown to be a major ligand-binding site within this and other integrins. These findings demonstrate that E-cadherin can interact with alpha2beta1 and suggest that heterotypic interactions between E-cadherin and integrins may be more common than originally thought."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0945-053x(02)00037-9"xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Engel J."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Koch A."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Mould A.P."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Pertz O."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Humphries M.J."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Craig S.E."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/author | "Whittard J.D."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/name | "Matrix Biol"xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/pages | "525-532"xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/title | "E-cadherin is a ligand for integrin alpha2beta1."xsd:string |
http://purl.uniprot.org/citations/12392763 | http://purl.uniprot.org/core/volume | "21"xsd:string |
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