Source:http://linkedlifedata.com/resource/pubmed/id/15772294
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2005-5-17
|
pubmed:abstractText |
Transcriptional activation of the cyclooxygenase (COX)-2 gene is responsible for high level of prostaglandin production during inflammation and carcinogenesis. We found previously that c-Jun induction plays a crucial role in epidermal growth factor (EGF)-induced gene expression of COX-2. In this study, the functional role of c-Jun in EGF-induced transcriptional activation of COX-2 in A431 cells was investigated. We found that overexpression of c-Jun N-terminal phosphorylation site mutants had similar stimulatory effects on COX-2 promoter activity and protein expression as c-Jun wild type. TAM-67, a mutant of c-Jun that lacks the N-terminal transactivation domain of c-Jun, also enhanced COX-2 promoter activity and protein expression in cells treated with EGF. In vitro DNA affinity precipitation and reporter assays revealed that regulation of c-Jun C terminus by EGF enhanced c-Jun binding to COX-2 promoter and induced COX-2 expression. Furthermore, we demonstrated that c-Fos, which provides transactivation function in Jun/Fos heterodimer, was required for EGF-induced expression of COX-2. These results indicated that c-Jun N-terminal phosphorylation was not required for EGF-induced expression of COX-2. c-Jun, which could recruit other transcription factors such as c-Fos, was required for EGF-induced expression of COX-2 in A431 cells.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTGS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0026-895X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
67
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2057-69
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:15772294-Cell Line, Tumor,
pubmed-meshheading:15772294-Cyclooxygenase 2,
pubmed-meshheading:15772294-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15772294-Humans,
pubmed-meshheading:15772294-Membrane Proteins,
pubmed-meshheading:15772294-Peptide Fragments,
pubmed-meshheading:15772294-Phosphorylation,
pubmed-meshheading:15772294-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:15772294-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:15772294-Transcription Factor AP-1,
pubmed-meshheading:15772294-Transcriptional Activation
|
pubmed:year |
2005
|
pubmed:articleTitle |
Activating protein 1-mediated cyclooxygenase-2 expression is independent of N-terminal phosphorylation of c-Jun.
|
pubmed:affiliation |
Department of Pharmacology, College of Medicine, National Cheng-Kung University, No.1 Ta-Hsueh Road, Tainan 701, Taiwan.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|