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http://purl.uniprot.org/citations/15220135http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15220135http://www.w3.org/2000/01/rdf-schema#comment"Vascular cell adhesion molecule (VCAM)-1 supports specific eosinophil adhesion via alpha4beta1 integrin. We tested the hypothesis that adhesive contacts formed by eosinophils on VCAM-1 are different from focal adhesions formed by adherent fibroblasts. Eosinophils adherent on VCAM-1 formed punctate adhesions that fit the criteria for podosomes, highly dynamic structures found in adherent transformed fibroblasts, osteoclasts, and macrophages. The structures contained beta1 integrin subunit, phosphotyrosine-containing proteins, punctate filamentous actin, and gelsolin, a podosome marker. In contrast, nontransformed fibroblasts on VCAM-1 formed peripheral focal adhesions that were positive for alpha4, beta1, phosphotyrosine, vinculin, talin, and paxillin; negative for gelsolin; and associated with microfilaments. Phorbol myristate acetate or tumor necrosis factor-alpha and interleukin-5 stimulated podosome formation in adherent eosinophils. Because podosomes in tumor cells are associated with extracellular matrix degradation, we analyzed the VCAM-1 layer. VCAM-1 was lost under adherent eosinophils but not under adherent fibroblasts. This loss was inhibited by the metalloproteinase inhibitor ortho-phenanthroline and correlated with expression and podosome localization of a membrane-tethered metalloproteinase, a disintegrin and metalloproteinase domain 8. Podosome-mediated VCAM-1 clearance may be a mechanism to regulate eosinophil arrest and extravasation in allergic conditions such as asthma."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.org/dc/terms/identifier"doi:10.1165/rcmb.2004-0099oc"xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Mosher D.F."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Annis D.S."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Barthel S.R."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Johansson M.W."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Duffy A.K."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/author"Lye M.H."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/name"Am J Respir Cell Mol Biol"xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/pages"413-422"xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/title"Eosinophils adhere to vascular cell adhesion molecule-1 via podosomes."xsd:string
http://purl.uniprot.org/citations/15220135http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/15220135http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15220135
http://purl.uniprot.org/citations/15220135http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15220135
http://purl.uniprot.org/uniprot/P78325#attribution-D6854C9ADF8FF5CE043641A8F98BC821http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15220135
http://purl.uniprot.org/uniprot/P04141#attribution-D6854C9ADF8FF5CE043641A8F98BC821http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15220135
http://purl.uniprot.org/uniprot/P05113#attribution-D6854C9ADF8FF5CE043641A8F98BC821http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15220135
http://purl.uniprot.org/uniprot/P01375#attribution-D6854C9ADF8FF5CE043641A8F98BC821http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15220135
http://purl.uniprot.org/uniprot/P19320#attribution-D6854C9ADF8FF5CE043641A8F98BC821http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15220135