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The carboxy-terminus of the hepatitis B virus X protein is necessary and sufficient for the activation of hypoxia-inducible factor-1alpha.

Authors
Yoo, YG; Cho, S; Park, S; Lee, MO
Citation
FEBS letters, 577(1-2):121-126, 2004
Journal Title
FEBS letters
ISSN
0014-57931873-3468
Abstract
Hepatitis B virus X protein (HBx) of the hepatitis B virus is strongly implicated in angiogenesis and metastasis during hepatocarcinogenesis. Previously, we reported that HBx enhances activity of hypoxia-inducible factor-1alpha (HIF-1alpha), a potent transactivator that induces angiogenic factors. Here, we delineate the structural region of HBx that potentiates HIF-1alpha. The carboxy-terminus of HBx increased the stability of HIF-1alpha protein, probably through inhibiting interaction with von Hippel-Lindau protein. Further, the carboxy-terminus of HBx enhanced the transactivation function of HIF-1alpha by enhancing its association with CREB binding protein (CBP). Finally, we demonstrated the physical association of HBx with the basic helix-loop-helix/PER-ARNT-SIM domain, the inhibitory domain, and the carboxy-terminal transactivation domain of HIF-1alpha in vivo.
MeSH terms
AnimalsBlotting, WesternCell LineHumansHypoxia-Inducible Factor 1, alpha SubunitMiceProtein BindingTrans-Activators/chemistry/*physiologyTranscription Factors/*metabolismTranscription, Genetic
DOI
10.1016/j.febslet.2004.10.004
PMID
15527772
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
AJOU Authors
박, 선
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