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

Authors
Choi, YH; Kim, HI; Seong, JK; Yu, DY; Cho, H; Lee, MO; Lee, JM; Ahn, YH; Kim, SJ; Park, JH
Citation
FEBS letters, 557(1-3):73-80, 2004
Journal Title
FEBS letters
ISSN
0014-57931873-3468
Abstract
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.
MeSH terms
AdenoviridaeApoptosis/drug effectsBase SequenceCarcinoma, Hepatocellular/pathology/virologyCell Division/drug effectsCell LineDNA PrimersGenes, ReporterGenetic VectorsGreen Fluorescent ProteinsHepatitis B Antigens/chemistry/pharmacologyHumansLigandsLiver Neoplasms/pathology/virologyLuminescent Proteins/geneticsProtein Transport/drug effectsReceptors, Cytoplasmic and Nuclear/chemistry/drug effects/genetics/*metabolismRecombinant Fusion Proteins/chemistry/drug effects/metabolismReverse Transcriptase Polymerase Chain ReactionTrans-Activators/chemistry/metabolism/*pharmacologyTranscription Factors/chemistry/drug effects/genetics/*metabolismTransfectionTumor Cells, Cultured
PMID
14741344
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
AJOU Authors
조, 혜성
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