TY - JOUR

T1 - Cutting edge: TCR stimulation by antibody and bacterial superantigen induces Stat3 activation in human T cells

AU - Gerwien, J

AU - Nielsen, M

AU - Labuda, T

AU - Nissen, M H

AU - Svejgaard, A

AU - Geisler, C

AU - Röpke, C

AU - Odum, N

N1 - Keywords: Antibodies, Monoclonal; Antigens, CD3; Binding Sites; CD4-Positive T-Lymphocytes; Cell Line; DNA; DNA-Binding Proteins; Enterotoxins; Epitopes, T-Lymphocyte; Humans; Interleukin-2; Oligonucleotides; Phosphorylation; Promoter Regions (Genetics); Receptors, Antigen, T-Cell; STAT3 Transcription Factor; Signal Transduction; Staphylococcus aureus; Superantigens; Trans-Activators; Tyrosine

PY - 1999

Y1 - 1999

N2 - 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 alpha 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.

AB - 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 alpha 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.

M3 - Journal article

C2 - 10438903

VL - 163

SP - 1742

EP - 1745

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 4

ER -