| pubmed-article:11739530 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C0008013 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C1332816 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C1332822 | lld:lifeskim |
| pubmed-article:11739530 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:11739530 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11739530 | pubmed:dateCreated | 2001-12-12 | lld:pubmed |
| pubmed-article:11739530 | pubmed:abstractText | Chemokine receptors are rapidly desensitized and internalized following ligand binding, a process that attenuates receptor-mediated responses. However, the physiological settings in which this process occurs are not clear. Therefore, we examined the fate of CXCR3, a chemokine receptor preferentially expressed on activated T cells following contact with endothelial cells. By immunofluorescence microscopy and flow cytometry, we found that CXCR3 was rapidly internalized when T cells were incubated with IFN-gamma-activated human saphenous vein endothelial cells (HSVEC), but not with resting HSVEC. Similar results were obtained using human CXCR3-transfected murine 300-19 B cells. CXCR3 down-regulation was significantly more pronounced when T cells were in contact with HSVEC than with their supernatants, suggesting that CXCR3 ligands were efficiently displayed on the surface of HSVEC. Using neutralizing mAbs to IFN-induced protein-10 (CXCL10), monokine induced by IFN-gamma (CXCL9), and IFN-inducible T cell alpha chemoattractant (I-TAC; CXCL11), we found that even though I-TAC was secreted from IFN-gamma-activated HSVEC to lower levels than IFN-induced protein-10 or the monokine induced by IFN-gamma, it was the principal chemokine responsible for CXCR3 internalization. This correlated with studies using recombinant chemokines, which revealed that I-TAC was the most potent inducer of CXCR3 down-regulation and of transendothelial migration. Known inhibitors of chemokine-induced chemotaxis, such as pertussis toxin or wortmannin, did not reduce ligand-induced internalization, suggesting that a distinct signal transduction pathway mediates internalization. Our data demonstrate that I-TAC is the physiological inducer of CXCR3 internalization and suggest that chemokine receptor internalization occurs in physiological settings, such as leukocyte contact with an activated endothelium. | lld:pubmed |
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| pubmed-article:11739530 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11739530 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:11739530 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11739530 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11739530 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:WagnerLL | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:RochatSS | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:SpertiniFF | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:ColvinR ARA | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:LusterA DAD | lld:pubmed |
| pubmed-article:11739530 | pubmed:author | pubmed-author:SautyAA | lld:pubmed |
| pubmed-article:11739530 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11739530 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11739530 | pubmed:volume | 167 | lld:pubmed |
| pubmed-article:11739530 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11739530 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11739530 | pubmed:pagination | 7084-93 | lld:pubmed |
| pubmed-article:11739530 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11739530 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11739530 | pubmed:articleTitle | CXCR3 internalization following T cell-endothelial cell contact: preferential role of IFN-inducible T cell alpha chemoattractant (CXCL11). | lld:pubmed |
| pubmed-article:11739530 | pubmed:affiliation | Division of Rheumatology, Allergy, and Immunology, Center for Immunology and Inflammatory Diseases, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA. | lld:pubmed |
| pubmed-article:11739530 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11739530 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11739530 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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