| http://purl.uniprot.org/citations/17643490 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17643490 | http://www.w3.org/2000/01/rdf-schema#comment | "Subunits of the mitochondrial ATP synthase complex are expressed on the surface of tumors, bind the TCR of human Vgamma9/Vdelta2 lymphocytes and promote their cytotoxicity. Present experiments show that detection of the complex (called ecto-F1-ATPase) at the cell surface by immunofluorescence correlates with low MHC-class I antigen expression. Strikingly, the alpha and beta chains of ecto-F1-ATPase are detected in membrane protein precipitates from immunofluorescence-negative cells, suggesting that ATPase epitopes are masked. Removal of beta2-microglobulin by mild acid treatment so that most surface MHC-I molecules become free heavy chains reveals F1-ATPase epitopes on MHC-I+ cell lines. Ecto-F1-ATPase is detected by immunofluorescence on primary fibroblasts which express moderate levels of MHC-I antigens. Up-regulation of MHC-I on these cells following IFN-gamma and/or TNF-alpha treatment induces a dose-dependent disappearance of F1-ATPase epitopes. Finally, biotinylated F1-ATPase cell surface components co-immunoprecipitate with MHC-I molecules confirming the association of both complexes on Raji cells. Confocal microscopy analysis of MHC-I and ecto-F1-ATPase beta chain expression on HepG2 cells shows a co-localization of both complexes in punctate membrane domains. This demonstrates that the TCR target F1-ATPase is in close contact with MHC-I antigens which are known to control Vgamma9/Vdelta2 T cell activity through binding to natural killer inhibitory receptors."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molimm.2007.05.026"xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/author | "Martinez L.O."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/author | "Fabre A."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/author | "Collet X."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/author | "Vantourout P."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/author | "Champagne E."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/name | "Mol Immunol"xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/pages | "485-492"xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/title | "Ecto-F1-ATPase and MHC-class I close association on cell membranes."xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://purl.uniprot.org/core/volume | "45"xsd:string |
| http://purl.uniprot.org/citations/17643490 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17643490 |
| http://purl.uniprot.org/citations/17643490 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17643490 |
| http://purl.uniprot.org/uniprot/P25705#attribution-40F57DF875AA260CFEB53D909058B10D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17643490 |
| http://purl.uniprot.org/uniprot/P06576#attribution-40F57DF875AA260CFEB53D909058B10D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17643490 |