Hepatitis B virus X protein modulates peroxisome proliferator-activated receptor γ through protein-protein interaction

被引：26

作者：

Choi, YH

Kim, H

Seong, JK

Yu, DY

Cho, HS

Lee, MO

Lee, JM

Ahn, Y

Kim, SJ

Park, JH ^{[1
]}

机构：

[1] Inst Immunol & Immunol Dis, Dept Microbiol, Seoul, South Korea

[2] Inst Immunol & Immunol Dis, Brain Korea 21 Project Med Sci, Seoul, South Korea

[3] Yonsei Univ, Coll Med, Dept Biochem & Mol Biol, Seoul 120752, South Korea

[4] Seoul Natl Univ, Coll Vet Med, Lab Dev Biol & Genome, Seoul 150742, South Korea

[5] Korea Res Inst Biosci & Biotechnol, Taejon 305600, South Korea

[6] Ajou Univ, Sch Med, Dept Biochem, Suwon 442749, South Korea

[7] Sejong Univ, Dept Biosci & Biotechnol, Seoul 140747, South Korea

来源：

FEBS LETTERS | 2004年 / 557卷 / 1-3期

关键词：

hepatitis B virus X protein; peroxisome proliferator-activated receptor gamma; transactivation; protein-protein interaction;

D O I：

10.1016/S0014-5793(03)01449-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ligand activation of peroxisome proliferator-activated receptor gamma (PPARgamma) has been reported to induce growth inhibition and apoptosis in various cancers including hepatocellular carcinoma (HCC). However, the effect of hepatitis B virus X protein (HBx) on PPARgamma activation has not been characterized in hepatitis B virus (HBV)-associated HCC. Herein, we demonstrated that HBx counteracted growth inhibition caused by PPARgamma ligand in HBx-associated HCC cells. We found that HBx bound to DNA binding domain of PPARgamma and HBx/PPARgamma interaction blocked nuclear localization and binding to recognition site of PPARgamma. HBx significantly suppressed a PPARgamma-mediated transactivation. These results suggest that HBx modulates PPARgamma function through protein-protein interaction. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All Rights Reserved.

引用

页码：73 / 80

页数：8

共 43 条

[1] Nuclear receptors in cell life and death [J].