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Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697
Human endothelial cells (ECs) provide costimulatory signals
sufficient to activate resting memory T cells to produce IL-2 and
IFN-
, at least in part through CD58-CD2 interactions. Recently, the
B7-like molecule, B7-H1 (PD-L1), was described and shown to regulate T
cell activation; however, there are conflicting reports on whether it
stimulates or inhibits T cell cytokine synthesis. B7-H1 is not
expressed constitutively by ECs; however, it is rapidly induced by
IFN-, and synergistically by IFN- and TNF. In inflamed skin,
B7-H1 is expressed by a subset of microvessels, and by keratinocytes,
but is barely detectable in normal skin. Blocking the interaction of
EC-expressed B7-H1 with its T cell ligand, programmed death-1 (PD-1),
using a PD-1-Fc fusion protein, or by blocking B7-H1 expression with
morpholino antisense oligonucleotides, augments expression of IL-2 and
IFN-, implicating B7-H1 as a negative regulator of cytokine
synthesis. However, signaling through PD-1 does not affect induction of
the activation markers CD25 or CD69 on T cells, suggesting that its
effects are specific to cytokine synthesis. The suppressive effects of
B7-H1 on cytokine expression are proportional to the strength of the
primary stimulus, allowing for B7-H1 to determine the level of T cell
activation in response to ECs. Our results demonstrate that B7-H1
negatively regulates cytokine synthesis in T cells activated by
ECs.
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