| Literature DB >> 17055456 |
Ji Su Kim1, Bo young Rho, Tae Ho Lee, Jae Myun Lee, Se Jong Kim, Jeon Han Park.
Abstract
HBx has been suggested as an important determinant mediating the pathological effects of HBV via interacting with various cellular proteins. To identify new HBx-interacting proteins and elucidate a possible mechanism associated with HBx and HBx-interacting proteins in hepatocellular carcinoma, yeast two-hybrid screening was performed. We identified a novel HBx-interacting protein, serine/threonine protein phosphatase PP2Calpha, and investigated the effects of PP2Calpha on HBx-mediated IL-6 regulation. The interaction between endogenous PP2Calpha, and HBx was confirmed by co-immunoprecipitation. Recombinant HBx dose-dependently reduced enzyme activity of recombinant PP2Calphain vitro. While ectopically expressed PP2Calpha in Cos-7 and Huh-7 cells reduced the expression of IL-6, overexpressed HBx with recombinant HBx-expressing adenovirus overcame PP2Calpha-mediated IL-6 downregulation. In the response of IL-6, HBx phosphorylated STAT3 and recovered PP2Calpha-mediated dephosphorylation of STAT3. These results supported that HBx might play a crucial role in HBV-associated hepatocarcinogenesis even in cases where cells express a negative regulator, PP2Calpha.Entities:
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Year: 2006 PMID： 17055456 DOI： 10.1016/j.bbrc.2006.10.028
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575