| pubmed-article:8491191 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C0003402 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C0085828 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C0682538 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C0020281 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C1749855 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C0175668 | lld:lifeskim |
| pubmed-article:8491191 | lifeskim:mentions | umls-concept:C1521805 | lld:lifeskim |
| pubmed-article:8491191 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8491191 | pubmed:dateCreated | 1993-6-11 | lld:pubmed |
| pubmed-article:8491191 | pubmed:abstractText | We show that AP-1 is an antioxidant-responsive transcription factor. DNA binding and transactivation by AP-1 were induced in HeLa cells upon treatment with the antioxidants pyrrolidine dithiocarbamate (PDTC) and N-acetyl-L-cysteine (NAC), and upon transient expression of the antioxidative enzyme thioredoxin. While PDTC and NAC enhanced DNA binding and transactivation of AP-1 in response to phorbol ester, the oxidant H2O2 suppressed phorbol ester activation of the factor. H2O2 on its own was only a weak inducer of AP-1. Activation of AP-1 by PDTC was dependent on protein synthesis and involved transcriptional induction of c-jun and c-fos genes. Transcriptional activation of c-fos by PDTC was conferred by the serum response element, suggesting that serum response factor and associated proteins function as primary antioxidant-responsive transcription factors. In the same cell line, the oxidative stress-responsive transcription factor NF-kappa B behaved in a manner strikingly opposite to AP-1. DNA binding and transactivation by NF-kappa B were strongly activated by H2O2, while the antioxidants alone were ineffective. H2O2 potentiated the activation of NF-kappa B by phorbol ester, while PDTC and NAC suppressed PMA activation of the factor. PDTC did not influence protein kinase C (PKC) activity and PKC activation by PMA, indicating that the antioxidant acted downstream of and independently from PKC. | lld:pubmed |
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| pubmed-article:8491191 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8491191 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8491191 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8491191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8491191 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8491191 | pubmed:month | May | lld:pubmed |
| pubmed-article:8491191 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8491191 | pubmed:author | pubmed-author:MeyerMM | lld:pubmed |
| pubmed-article:8491191 | pubmed:author | pubmed-author:SchreckRR | lld:pubmed |
| pubmed-article:8491191 | pubmed:author | pubmed-author:BaeuerleP APA | lld:pubmed |
| pubmed-article:8491191 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8491191 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:8491191 | pubmed:geneSymbol | c-fos | lld:pubmed |
| pubmed-article:8491191 | pubmed:geneSymbol | c-jun | lld:pubmed |
