| http://purl.uniprot.org/citations/12941957 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12941957 | http://www.w3.org/2000/01/rdf-schema#comment | "Functional interactions between Fcgamma-receptors (FcgammaR) and the beta2 integrin Mac-1 (CD11b/CD18) have been described, but the molecular basis of this relationship remains unclear. Although the glycosylphosphatidylinositol-linked receptor FcgammaRIIIB of human neutrophils is constitutively associated with Mac-1, we found no evidence for direct physical association between Mac-1 and the FcgammaR of mouse macrophages, which are transmembrane proteins. Nevertheless, Mac-1 accumulated in the phagocytic cup following engagement of FcgammaR by IgG-opsonized particles. Blocking the CD18 chains of beta2 integrins by using specific antibodies reduced Mac-1 accumulation in the cup. These antibodies or the addition of the recombinant CD11b I-domain inhibited the ingestion of IgG-opsonized particles. FcgammaR cross-linking stimulated cell adhesion to surfaces coated with Mac-1 ligands and in addition enabled macrophages to bind C3bi-opsonized particles, indicating that FcgammaR-derived signals induce activation of Mac-1. Measurements of fluorescence recovery after photobleaching revealed that whereas most (>80%) of Mac-1 is immobile in resting cells, stimulation of FcgammaR markedly increases the mobile fraction of the integrin. Activation of Mac-1 by FcgammaR required the activity of Src family tyrosine kinases, phosphatidylinositol 3-kinase and phospholipase C, with the release of diacylglycerol and stimulation of protein kinase C. Because elevated cytosolic Ca2+ was not required, we suggest that novel protein kinase C isoforms are involved in Mac-1 activation. These results suggest that FcgammaR stimulation promotes Mac-1 clustering into high avidity complexes in phagocytic cups by releasing the integrin from cytoskeletal constraints and enhancing its lateral diffusion. FcgammaR can enhance host defense by activating Mac-1 (and possibly other integrins), having a synergistic effect on pathogen engulfment and promoting the adherence of phagocytes at sites of infection."xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m303704200"xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/author | "Grinstein S."xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/author | "Harrison R."xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/author | "Jongstra-Bilen J."xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/pages | "45720-45729"xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/title | "Fcgamma-receptors induce Mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis."xsd:string |
| http://purl.uniprot.org/citations/12941957 | http://purl.uniprot.org/core/volume | "278"xsd:string |
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