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CUTTING EDGE |
*
Institute of Medical Microbiology and Immunology, and
Institute for Medical Anatomy, Section A, University of Copenhagen, Copenhagen, Denmark;
Wallenberg Laboratory, Lund University, Lund, Sweden; and
§
Tissue Typing Laboratory, Department of Clinical Immunology, National University Hospital, Copenhagen, Denmark
Recent data show that TCR/CD3 stimulation induces activation of
Stat5 in murine T cells. Here, we show that CD3 ligation by mAb and
Staphylococcal enterotoxin (SE) induce a rapid, gradually accumulating,
long-lasting tyrosine, and serine phosphorylation of
Stat3 (but not Stat5) in allogen-specific human CD4+ T cell
lines. In contrast, IL-2 induces a rapid and transient tyrosine and
serine phosphorylation of Stat3. Compared with IL-2,
CD3 ligation induces a delayed Stat3 binding to oligonucleotide probes
from the ICAM-1 and IL-2R
promoter. CD3-mediated activation of Stat3
is almost completely inhibited by a Src kinase inhibitor (PP1), whereas
IL-2-induced Stat3 activation is unaffected. In conclusion, we show
that CD3 ligation by mAb and SE triggers a rapid, PP1-sensitive
tyrosine and serine phosphorylation of Stat3 in human
CD4+ T cells. Moreover, we provide evidence that TCR/CD3
and IL-2 induce Stat3 activation via distinct signaling
pathways.
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