Interleukin-2 induces tyrosine phosphorylation and nuclear translocation of stat3 in human T lymphocytes
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Interleukin-2 induces tyrosine phosphorylation and nuclear translocation of stat3 in human T lymphocytes. / Nielsen, M; Svejgaard, A; Skov, S; Odum, Niels.
In: European Journal of Immunology, Vol. 24, No. 12, 1994, p. 3082-6.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Interleukin-2 induces tyrosine phosphorylation and nuclear translocation of stat3 in human T lymphocytes
AU - Nielsen, M
AU - Svejgaard, A
AU - Skov, S
AU - Odum, Niels
N1 - Keywords: Biological Transport; Cell Compartmentation; Cell Nucleus; Cells, Cultured; DNA-Binding Proteins; Humans; Interleukin-2; Nuclear Proteins; Phosphotyrosine; Protein-Tyrosine Kinases; Receptors, Interleukin-2; STAT1 Transcription Factor; STAT3 Transcription Factor; Signal Transduction; T-Lymphocytes; Trans-Activators; Tyrosine
PY - 1994
Y1 - 1994
N2 - An early biochemical event associated with T cell activation through the interleukin-2 receptor (IL-2R) is tyrosine phosphorylation of several intracellular substrates. The exact mechanism by which IL-2 regulates transcription of different genes is presently unknown. Here, we report that stimulation through the IL-2R induced tyrosine phosphorylation and subsequent nuclear translocation of stat3, a newly identified member of the signal transducers and activators of transcription (STAT) family of proteins. In contrast, stat1 proteins were not tyrosine phosphorylated after IL-2 ligation, whereas tyrosine-phosphorylated stat1 proteins (91 and 84 kDa proteins) were translocated to the nucleus following interferon-gamma treatment of HeLa cells. Apart from stat3, another cytoplasmic protein was tyrosine phosphorylated and subsequently translocated to the nucleus in response to IL-2. This protein had an apparent molecular mass of 84 kDa and was not recognized by stat3 or stat1 mAb or antisera. Since IL-2 induced nuclear translocation of the 84 kDa protein and stat3 followed identical kinetics, p84 is a candidate for a new, yet undefined, member of the STAT family. Taken together, we report that IL-2 induces tyrosine phosphorylation and subsequent nuclear translocation of stat3 and an as yet undefined 84-kDa protein in antigen-specific human T cell lines.
AB - An early biochemical event associated with T cell activation through the interleukin-2 receptor (IL-2R) is tyrosine phosphorylation of several intracellular substrates. The exact mechanism by which IL-2 regulates transcription of different genes is presently unknown. Here, we report that stimulation through the IL-2R induced tyrosine phosphorylation and subsequent nuclear translocation of stat3, a newly identified member of the signal transducers and activators of transcription (STAT) family of proteins. In contrast, stat1 proteins were not tyrosine phosphorylated after IL-2 ligation, whereas tyrosine-phosphorylated stat1 proteins (91 and 84 kDa proteins) were translocated to the nucleus following interferon-gamma treatment of HeLa cells. Apart from stat3, another cytoplasmic protein was tyrosine phosphorylated and subsequently translocated to the nucleus in response to IL-2. This protein had an apparent molecular mass of 84 kDa and was not recognized by stat3 or stat1 mAb or antisera. Since IL-2 induced nuclear translocation of the 84 kDa protein and stat3 followed identical kinetics, p84 is a candidate for a new, yet undefined, member of the STAT family. Taken together, we report that IL-2 induces tyrosine phosphorylation and subsequent nuclear translocation of stat3 and an as yet undefined 84-kDa protein in antigen-specific human T cell lines.
M3 - Journal article
C2 - 7528668
VL - 24
SP - 3082
EP - 3086
JO - European Journal of Immunology
JF - European Journal of Immunology
SN - 0014-2980
IS - 12
ER -
ID: 10636059