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*
Institut für Klinische Mikrobiologie und Immunologie, Universität Erlangen, Erlangen, Germany;
Department of Pathology, Free University Hospital, Amsterdam, The Netherlands; and
Cancer Research Laboratories, Queen’s University, Kingston, Canada
Previously, we described the expression of an energy-dependent pump
in resting murine Th2 (but not resting Th1) cells which extruded the
fluorescent dye Fluo-3. After stimulation with Ag and APCs, Th1 cells
also expressed this pump. Furthermore, expression of the murine
multidrug resistance protein 1 (mrp1) correlated with the presence of
the pump. In this study, we report that Fluo-3 is indeed transported by
murine mrp1 or its human ortholog MRP1, as revealed by transfection of
HEK 293 cells with mrp1 or MRP1 cDNA. Like antigenic activation, IL-2
dose-dependently enhanced the Fluo-3-extruding activity in murine Th1
cells. Although TNF-
and IL-12 by themselves only weakly enhanced
Fluo-3 extrusion, each of them did so in strong synergism with IL-2. An
Ab directed against mrp1 was used to quantify the expression of mrp1
protein in T cells at the single-cell level. Like the Fluo-3 pump, mrp1
protein expression was enhanced by IL-2. Immunohistochemical studies
using confocal laser microscopy indicated that mrp1 is localized mainly
at the plasma membrane. In addition, protein expression of mrp1 was
induced in V
8+CD4+ T cells 12 h after
in vivo application of Staphylococcal enterotoxin B. Finally, mrp1 was
functionally relevant during the activation process of Th1 cells,
because T cell activation could be suppressed by exposure of cells to
the mrp1 inhibitor MK571. Thus, we present mrp1 as a novel,
functionally important activation marker for Th1 cells and short-term
in vivo activated CD4+ T cells, whereas its expression
seems to be constitutive in Th2 cells.
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