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Effect of interleukin-10 on NF-kB and AP-1 activities in interleukin-2 dependent CD8 T lymphoblasts
M Hurme1, T Henttinen, M Karppelin
1Department of Biomedical Sciences, University of Tampere, Finland.
Insights
Interleukin-10 (IL-10) activates transcription factors AP-1 and NF-kappa B in CD8 T cells, similar to Interleukin-2 (IL-2). This suggests a shared signaling pathway involving tyrosine kinases for immune cell regulation.
Area of Science:
- Immunology
- Molecular Biology
- Cell Signaling
Background:
- Interleukin-10 (IL-10) is a key cytokine regulating immune cell function.
- In CD8 T cells, IL-10 promotes proliferation and differentiation into cytotoxic cells, often in conjunction with Interleukin-2 (IL-2).
Purpose of the Study:
- To investigate the intracellular signaling mechanisms induced by IL-10 in human IL-2 dependent CD8 T lymphoblasts.
- To compare IL-10 signaling pathways with those of IL-2 in the same cell type.
Main Methods:
- Analysis of transcription factor activation (AP-1 and NF-kappa B).
- Assessment of protein tyrosine phosphorylation patterns induced by IL-10.
- Comparison of IL-10 and IL-2 signaling.
Main Results:
- IL-10 alone activated the AP-1 transcription factor.
- IL-10 potentiated IL-2 induced NF-kappa B activity.
- IL-10 triggered rapid tyrosine phosphorylation of proteins, mirroring IL-2's effect.
Conclusions:
- Tyrosine kinase-dependent activation of NF-kappa B and AP-1 are implicated in IL-10 signaling.
- IL-10 utilizes signaling pathways similar to IL-2 in CD8 T lymphoblasts.
Abstract:
Interleukin-10 is a multifunctional cytokine, which regulates the function of various cell types of the immune system. In CD8 T cells it is known to accelerate the interleukin-2 dependent proliferation and to induce the differentiation of these cells to active cytolytic cells. Now we have studied interleukin-10 induced intracellular signaling mechanisms in human interleukin-2 dependent CD8 T lymphoblasts. The data obtained demonstrate that interleukin-10 alone can activate the AP-1 transcription factor and potentiate the interleukin-2 induced NF-kappa B activity. Moreover, interleukin-10 induced a rapid tyrosine phosphorylation of several proteins. The pattern of proteins phosphorylated was very similar to that induced by interleukin-2. Together, these findings suggest that tyrosine kinase dependent activation of NF-kappa B and AP-1 transcription factors are involved in the signaling mechanism of interleukin-10. This activation pathway resembles that of interleukin-2 in the same cell type.