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http://purl.uniprot.org/citations/12208882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12208882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12208882http://www.w3.org/2000/01/rdf-schema#comment"The recently described junctional adhesion molecules (JAMs) in man and mice are involved in homotypic and heterotypic intercellular interactions. Here, a third member of this family, human JAM-3, was identified and described as a novel counterreceptor on platelets for the leukocyte beta2-integrin Mac-1 (alphaMbeta2, CD11b/CD18). With the help of two monoclonal antibodies, Gi11 and Gi13, against a 43-kD surface glycoprotein on human platelets, a full-length cDNA encoding JAM-3 was identified. JAM-3 is a type I transmembrane glycoprotein containing two Ig-like domains. Although JAM-3 did not undergo homophilic interactions, myelo-monocytic cells adhered to immobilized JAM-3 or to JAM-3-transfected cells. This heterophilic interaction was specifically attributed to a direct interaction of JAM-3 with the beta2-integrin Mac-1 and to a lower extent with p150.95 (alphaXbeta2, CD11c/CD18) but not with LFA-1 (alphaLbeta2, CD11a/CD18) or with beta1-integrins. These results were corroborated by analysis of K562 erythroleukemic cells transfected with different heterodimeric beta2-integrins and by using purified proteins. Moreover, purified JAM-3 or antibodies against JAM-3 blocked the platelet-neutrophil interaction, indicating that platelet JAM-3 serves as a counterreceptor for Mac-1 mediating leukocyte-platelet interactions. JAM-3 thereby provides a novel molecular target for antagonizing interactions between vascular cells that promote inflammatory vascular pathologies such as in atherothrombosis."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.org/dc/terms/identifier"doi:10.1084/jem.20020267"xsd:string
http://purl.uniprot.org/citations/12208882http://purl.org/dc/terms/identifier"doi:10.1084/jem.20020267"xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Linder M."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Linder M."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Preissner K.T."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Preissner K.T."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Chavakis T."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Chavakis T."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Ruf A."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Ruf A."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Santoso S."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Santoso S."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Kroll H."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Kroll H."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Sachs U.J.H."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/author"Sachs U.J.H."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/name"J. Exp. Med."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/name"J. Exp. Med."xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/pages"679-691"xsd:string
http://purl.uniprot.org/citations/12208882http://purl.uniprot.org/core/pages"679-691"xsd:string