| pubmed-article:9535875 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0677626 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0037473 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0538674 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9535875 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:9535875 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:9535875 | pubmed:dateCreated | 1998-5-14 | lld:pubmed |
| pubmed-article:9535875 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9535875 | pubmed:abstractText | Heme oxygenase-1 is an inducible enzyme that catalyzes heme degradation and has been proposed to play a role in protecting cells against oxidative stress-related injury. We investigated the induction of heme oxygenase-1 by the tumor promoter arsenite in a chicken hepatoma cell line, LMH. We identified a heme oxygenase-1 promoter-driven luciferase reporter construct that was highly and reproducibly expressed in response to sodium arsenite treatment. This construct was used to investigate the role of mitogen-activated protein (MAP) kinases in arsenite-mediated heme oxygenase-1 gene expression. In LMH cells, sodium arsenite, cadmium, and heat shock, but not heme, induced activity of the MAP kinases extracellular-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. To examine whether these MAP kinases were involved in mediating heme oxygenase-1 gene expression, we utilized constitutively activated and dominant negative components of the ERK, JNK, and p38 MAP kinase signaling pathways. Involvement of an AP-1 site in arsenite induction of heme oxygenase-1 gene expression was studied. We conclude that the MAP kinases ERK and p38 are involved in the induction of heme oxygenase-1, and that at least one AP-1 element (located -1576 base pairs upstream of the transcription start site) is involved in this response. | lld:pubmed |
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| pubmed-article:9535875 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9535875 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9535875 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9535875 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9535875 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9535875 | pubmed:author | pubmed-author:DavisR JRJ | lld:pubmed |
| pubmed-article:9535875 | pubmed:author | pubmed-author:BonkovskyH... | lld:pubmed |
| pubmed-article:9535875 | pubmed:author | pubmed-author:WhitmarshA... | lld:pubmed |
| pubmed-article:9535875 | pubmed:author | pubmed-author:ElbirtK KKK | lld:pubmed |
| pubmed-article:9535875 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9535875 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:9535875 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9535875 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9535875 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9535875 | pubmed:pagination | 8922-31 | lld:pubmed |
| pubmed-article:9535875 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9535875 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9535875 | pubmed:articleTitle | Mechanism of sodium arsenite-mediated induction of heme oxygenase-1 in hepatoma cells. Role of mitogen-activated protein kinases. | lld:pubmed |
| pubmed-article:9535875 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Worcester, Massachusetts 01655, USA. kimberly.gabis@ummed.edu | lld:pubmed |
| pubmed-article:9535875 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9535875 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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