| pubmed-article:1639069 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0019169 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0003402 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0040627 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C1749855 | lld:lifeskim |
| pubmed-article:1639069 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:1639069 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:1639069 | pubmed:dateCreated | 1992-8-28 | lld:pubmed |
| pubmed-article:1639069 | pubmed:abstractText | C-terminal truncation of the middle surface antigen from hepatitis B virus (MHBs) gives rise to a novel transactivating protein, called MHBst. In this study we show that MHBst like the HBx protein of HBV, can cause nuclear appearance of NF-kappa B DNA binding activity and induce various kappa B-controlled reporter genes. While an inhibitor of protein kinase C could not block gene induction by MHBst, the antioxidants N-acetyl-L-cysteine (NAC) and pyrrolidine dithiocarbamate (PDTC) could potently suppress transactivation at mM and microM concentrations, respectively. Also, kappa B-dependent gene induction by the transactivator HBx was blocked. The effects were selective because PDTC did not interfere with MHBst and HBx-induced activation of the c-fos promoter/enhancer, nor with the basal activity of several other reporter genes lacking functional NF-kappa B binding motifs. Our data suggest that induction of a prooxidant state is crucial for the activation of NF-kappa B by MHBst and HBx and might be related to the hepatocarcinogenic potential of the viral proteins. MHBst had a subcellular localization unusual for a viral transactivator: it appeared to be an integral membrane protein of the endoplasmic reticulum. | lld:pubmed |
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| pubmed-article:1639069 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1639069 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1639069 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1639069 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1639069 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1639069 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1639069 | pubmed:author | pubmed-author:MeyerMM | lld:pubmed |
| pubmed-article:1639069 | pubmed:author | pubmed-author:HofschneiderP... | lld:pubmed |
| pubmed-article:1639069 | pubmed:author | pubmed-author:SchreckRR | lld:pubmed |
| pubmed-article:1639069 | pubmed:author | pubmed-author:BaeuerleP APA | lld:pubmed |
| pubmed-article:1639069 | pubmed:author | pubmed-author:CaselmannW... | lld:pubmed |
