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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-3-25
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pubmed:abstractText |
Human hepatitis B virus (HBV) X protein, HBx, transactivates virus and host genes through a wide variety of cis-elements. Expression of HBx is controlled by HBV enhancer 1 (Enh1). Both Enh1 and the core sequence of Enh1, which consists of an AP-1 related site (cFAP1) and a C stretch, respond to HBx and a phorbol ester (TPA). Biochemical pathways of the responses to HBx and TPA are still controversial. We therefore asked whether HBx and TPA stimulate Enh1 core activity through a common process. Protein kinase C (PKC) inhibitors, H-7 and staurosporin, did not inhibit HBx transactivation at concentrations sufficient to abolish the TPA effects in HepG2 cells. Although HBx transactivation synergized independently with TPA or a phosphoprotein phosphatase inhibitor, okadaic acid (OA), the PKC inhibitors eliminated only the TPA contribution. HBx transactivation required both the cFAP1 and the C stretch of the Enh1 core region; however, mutations in either or both of the two cis-elements demonstrated that TPA augmentation required only cFAP1. These results imply that HBx transactivation operates through a mechanism distinct from the PKC and OA activation pathways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Ethers, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/hepatitis B virus X protein
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
199
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
243-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8116251-Base Sequence,
pubmed-meshheading:8116251-Cell Line,
pubmed-meshheading:8116251-DNA, Viral,
pubmed-meshheading:8116251-Ethers, Cyclic,
pubmed-meshheading:8116251-Hepatitis B virus,
pubmed-meshheading:8116251-Humans,
pubmed-meshheading:8116251-Molecular Sequence Data,
pubmed-meshheading:8116251-Okadaic Acid,
pubmed-meshheading:8116251-Protein Kinase C,
pubmed-meshheading:8116251-Tetradecanoylphorbol Acetate,
pubmed-meshheading:8116251-Trans-Activators,
pubmed-meshheading:8116251-Transcriptional Activation
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pubmed:year |
1994
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pubmed:articleTitle |
Transactivation of human hepatitis B virus X protein, HBx, operates through a mechanism distinct from protein kinase C and okadaic acid activation pathways.
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pubmed:affiliation |
Department of Biophysics, Medical School, Kanazawa University, Japan.
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pubmed:publicationType |
Journal Article
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