Skip Navigation


Journal of Biochemistry Advance Access originally published online on February 21, 2007
Journal of Biochemistry 2007 141(5):635-640; doi:10.1093/jb/mvm066
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
141/5/635    most recent
mvm066v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Guo, H.
Right arrow Articles by Kuo, P. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Guo, H.
Right arrow Articles by Kuo, P. C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society.

Characterization of the PC4 Binding Domain and its Interactions with HNF4{alpha}

Hongtao Guo, Chengjiang Gao, Zhiyong Mi, Jinping Zhang and Paul C. Kuo*

Deparment of Surgery, Duke University Medical Center, Durham, NC, USA

*To whom correspondence should be addressed. Tel: 919-668-1856, Fax: 919-684-8716, E-mail: kuo00004{at}mc.duke.edu

Received January 22, 2007; Accepted February 13, 2007


  Abstract

In the presence of oxidative stress, the hepatocellular inflammatory-redox (IR) state upregulates inducible nitric oxide synthase (iNOS) expression as an anti-oxidant function. In IL-1ß and peroxide treated hepatocytes, we have identified hepatocyte nuclear factor-4{alpha} (HNF4) and the transcriptional co-activator, PC4, to be essential for upregulation of iNOS transcription in this setting. The co-activator, PC4, facilitates activator-dependent transcription via interactions with basal transcriptional machinery that are independent of PC4-DNA binding. The interaction between HNF4 and PC4 has not been previously characterized. In this study utilizing human HepG2 cells, we demonstrate the critical role for p38 MAP kinase mediated HNF4 Ser158 phosphorylation (P-HNF4-S158), binding of PC4 to P-HNF4-S158 and characterize the functional domain of PC4 required for P-HNF4-S158 binding. Our results indicate that the presence of the IR state enhances PC4-HNF4 binding to upregulate transcription of target hepatocyte genes, such as iNOS.

Key Words: co-activator, inflammation, nitric oxide, nuclear receptor

Abbreviations: ChIP, chromatin immunoprecipitation; HNF4, hepatocyte nuclear factor 4-alpha; IL-1, interleukin 1ß; iNOS, inducible nitric oxide synthase; IR, inflammatory-redox; MM, mismatch; NO, nitric oxide; PCR, polymerase chain reaction; WT, wild type


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Z. Xu, O. L. Tavares-Sanchez, Q. Li, J. Fernando, C. M. Rodriguez, E. J. Studer, W. M. Pandak, P. B. Hylemon, and G. Gil
Activation of Bile Acid Biosynthesis by the p38 Mitogen-activated Protein Kinase (MAPK): HEPATOCYTE NUCLEAR FACTOR-4{alpha} PHOSPHORYLATION BY THE p38 MAPK IS REQUIRED FOR CHOLESTEROL 7{alpha}-HYDROXYLASE EXPRESSION
J. Biol. Chem., August 24, 2007; 282(34): 24607 - 24614.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.