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Title 

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

Authors 

In Pyo ChoiMin Ju LeeEun Joo KimHyung Sik KangKwang Ho Pyun

Publisher 

Elsevier

Issue Date 

1998

Citation 

Immunology Letters, vol. 61, no. 0, pp. 103-107

Keywords 

IL-6Protein phosphatase 2AIRF-1Hep3B

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 I 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 intefferons, 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-α or TGF-β. 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 events of IL-6 signaling in Hep3B.

ISSN 

0165-2478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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