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Departments of
*
Microbiology and
Pharmacology, University of Washington, Seattle, WA 98195;
Immunex Corporation, Seattle, WA 98101;
§
Robert-Roessle-Klinik, Charite, Humboldt University of Berlin, Berlin, Germany; and
¶
Pacific Northwest Research Institute, Seattle, WA 98122
The inducible costimulator (ICOS) is the newest member of the
CD28/CD152 receptor family involved in regulating T cell activation. We
constructed a soluble-Ig fusion protein of the extracellular domain of
human ICOS and used it as a probe to characterize expression patterns
of the ICOS ligand (ICOSL). ICOSIg did not bind to CD80- or
CD86-transfected Chinese hamster ovary cell lines, demonstrating that
ICOSL is distinct from those ligands identified for CD28/CD152. ICOSIg
showed selective binding to monocytic and B cell lines, whereas binding
was undetectable on unstimulated monocytes and peripheral blood T and B
cells. Expression of ICOSL was induced on monocytes after
integrin-dependent plastic adhesion. Pretreatment of monocytes with mAb
to the ß2-integrin subunit CD18 decreased adhesion and
abolished ICOSL up-regulation but had no effect on CD80/86 (CD152
ligand (CD152L)) expression. Both ICOSL and CD152L were up-regulated on
monocytes by IFN-
but by distinct signaling pathways. Unlike CD152L
expression, ICOSL expression did not change when monocytes were
differentiated into dendritic cells (DCs) or after DCs were induced to
mature by LPS, TNF-
, or CD40 ligation. Addition of ICOSIg to
allogeneic MLRs between DCs and T cells reduced T cell proliferative
responses but did so less efficiently than CTLA4Ig (CD152Ig) did.
Similarly, ICOSIg also blocked Ag-specific T cell proliferation to
tetanus toxoid. Thus, ICOSL, like CD80/86, is expressed on activated
monocytes and dendritic cells but is regulated differently and delivers
distinct signals to T cells that can be specifically inhibited by
ICOSIg.
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