| pubmed-article:11228545 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0021853 | lld:lifeskim |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0387583 | lld:lifeskim |
| pubmed-article:11228545 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11228545 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:11228545 | pubmed:dateCreated | 2001-3-6 | lld:pubmed |
| pubmed-article:11228545 | pubmed:abstractText | Modulation of cyclooxygenase-2 (COX-2) mRNA stability plays an important role in the regulation of its expression by oncogenic Ras. Here, we evaluate COX-2 mRNA stability in response to treatment with two known endogenous promoters of gastrointestinal cancer, the bile acid (chenodeoxycholate; CD) and ceramide. Treatment with CD and ceramide resulted in a 10-fold increase in the level of COX-2 protein and a four-fold lengthening of the half-life of COX-2 mRNA. COX-2 mRNA stability was assessed by Northern blot analysis and by evaluating the AU-rich element located in the COX-2 3'-UTR. A known inhibitor of mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase (MEK), PD98059, reversed the effects of CD or ceramide to stabilize COX-2 mRNA. Overexpression of a dominant-negative ERK-1 or ERK-2 protein also led to destabilization of COX-2 mRNA. Treatment with a p38 MAPK inhibitor, PD169316, or transfection with a dominant-negative p38 MAPK construct reversed the effect of CD or ceramide to stabilize COX-2 mRNA. Expression of a dominant-negative c-Jun N-terminal kinase (JNK) had no effect on COX-2 mRNA stability in cells treated with CD or ceramide. We conclude that posttranscriptional mechanisms play an important role in the regulation of COX-2 expression during carcinogenesis. | lld:pubmed |
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| pubmed-article:11228545 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11228545 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11228545 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11228545 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11228545 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11228545 | pubmed:issn | 1522-8002 | lld:pubmed |
| pubmed-article:11228545 | pubmed:author | pubmed-author:ShawBB | lld:pubmed |
| pubmed-article:11228545 | pubmed:author | pubmed-author:BeauchampR... | lld:pubmed |
| pubmed-article:11228545 | pubmed:author | pubmed-author:ZhangZZ | lld:pubmed |
| pubmed-article:11228545 | pubmed:author | pubmed-author:ShengHH | lld:pubmed |
| pubmed-article:11228545 | pubmed:author | pubmed-author:DuBoisR NRN | lld:pubmed |
| pubmed-article:11228545 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11228545 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:11228545 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11228545 | pubmed:authorsComplete | Y | lld:pubmed |
