J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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A more recent version of this article appeared on November 1, 2005

Papers In Press, published online ahead of print August 16, 2005
J. Lipid Res., doi:10.1194/jlr.M500337-JLR200
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Submitted on August 1, 2005
Accepted on August 14, 2005

Ceramide- and extracellularly regulated kinase (ERK)- dependent pathway in interleukin 1beta -induced activation of CCAAT-enhancer binding protein in hepatocytes

Natalia V. Giltiay, Alexander A. Karakashian, Alexander P. Alimov, Sandy Ligthle, and Mariana N. Nikolova-Karakashian

Physiology Dept., University of Kentucky, Lexington, KY 40502

Corresponding Author: mnikolo{at}uky.edu

IL-1 beta is a major inducer of liver acute phase proteins (APP) expression in response to infection. Several transcription factors including C/EBP, are known mediators in this process, although the mechanisms by which they modulate IL-1beta ’s action are not completely understood. Activation of Sphingomyelinase and the subsequent generation of ceramide are early steps in the IL-1beta signaling cascade. In this study, we investigate the role of ceramide in the IL-1beta regulation of C/EBP in primary hepatocytes. The C/EBP DNA binding activity was found to increase in a dose-dependent manner following stimulation with IL-1beta and exogenous addition of C2-ceramide or treatment with Sphingomyelinase (SMase). These changes were accompanied by an elevation in nuclear content of C/EBPbeta . Both, IL-1beta and ceramide lead to ERK1/2 activation as early as 15 minutes following treatment. Furthermore, elevation of cellular ceramide content resulted in increased phosphorylation of C/EBPbeta at Ser 105 at later time points. Concurrently, the cytosolic levels of C/EBPbeta dropped, suggesting that IL-1beta and ceramide induced nuclear translocation of C/EBPbeta . Ceramide-induced C/EBPbeta phosphorylation, translocation and DNA binding were suppressed by the addition of PD98059, an inhibitor of the ERK1/2 phosphorylation. These results suggest that ceramide and ERK mediate a pathway in the IL-1beta signaling cascade, which results in rapid post-translational activation of C/EBPbeta


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