PMID: 9657261Jul 10, 1998Paper

Roles of protein phosphatase 2A in IL-6 signal transduction in Hep3B cells

Immunology Letters
I ChoiK H Pyun

Abstract

IL-6 is a pleiotropic cytokine that modulates the diverse functions of hepatocytes such as acute phase responses and inflammation. When human hepatoma cells, Hep3B cells, were treated with IL-6, p140 was phosphorylated rapidly and reached its maximal rate at 1 min after treatment. Okadaic acid, an inhibitor of protein phosphatase 1 and 2A, affected IL-6-induced p140 phosphorylation. Interferon regulatory factor-1 (IRF-1) is a transcription factor on the enhancer of type I interferons, and its gene expression is induced by IL-6. When IRF-1 promoter-luciferase construct was transfected into Hep3B cells, okadaic acid increased IL-6- induced IRF-1 promoter activity. In addition, co-transfection of protein phosphatase 2A (PP2A) antisense constructs further increased IL-6-induced IRF-1 promoter activity, suggesting that PP2A is involved in IL-6 signaling. In addition, IL-6 directly induced the PP2A phosphorylation. PP2A phosphorylation was maximal at 1 min after IL-6 stimulation, but it was not induced by other inflammatory cytokines such as TNF-alpha or TGF-beta. Furthermore, IL-6 activated PP2A activity simultaneously. Taken together, these data indicate that IL-6 modulates the functions of PP2A which is involved in downstream even...Continue Reading

References

Dec 1, 1990·Immunology Today·T HiranoT Kishimoto
Jan 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·T HiranoF Sakiyama
Jul 18, 1995·Proceedings of the National Academy of Sciences of the United States of America·T G BoultonG D Yancopoulos
Jan 15, 1993·Proceedings of the National Academy of Sciences of the United States of America·D ZafririA Kimchi
Jun 26, 1997·Nature·R StarrD J Hilton

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