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The Journal of Immunology, 2002, 168: 4871-4880.
Copyright © 2002 by The American Association of Immunologists

Human B Cells Become Highly Responsive to Macrophage-Inflammatory Protein-3{alpha}/CC Chemokine Ligand-20 After Cellular Activation Without Changes in CCR6 Expression or Ligand Binding

Fang Liao1,2, Aiko-Konno Shirakawa1, John F. Foley, Ronald L. Rabin and Joshua M. Farber3

Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892

CCR6 is the only known receptor for the chemokine macrophage-inflammatory protein (MIP)-3{alpha}/CC chemokine ligand (CCL)20. We have shown previously that CCR6 is expressed on peripheral blood B cells, but CCR6 activity on these cells is low in in vitro assays. We report that MIP-3{alpha}/CCL20-induced calcium flux and chemotaxis can be enhanced significantly on peripheral blood and tonsillar B cells after activation by cross-linking surface Ag receptors. Of particular interest is the fact that the enhanced activity on B cells was not associated with an increase in CCR6 expression as assessed by levels of receptor mRNA, surface staining, or MIP-3{alpha}/CCL20 binding sites, or by a change in the affinity of the receptor for ligand. These data convincingly demonstrate that responses to a chemokine can be regulated solely by changes in the downstream pathways for signal transduction resulting from Ag receptor activation, and establish CCR6 as an efficacious receptor on human B cells.




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