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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2003-4-14
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pubmed:abstractText |
In human colorectal adenocarcinoma cell lines, we found two major transcripts of cyclooxygenase-2, the full-length mRNA and a short polyadenylation variant (2577 kb) lacking the distal segment of the 3'-untranslated region. Tristetraprolin, an mRNA-binding protein that promotes message instability, was shown to bind the cyclooxygenase-2 mRNA in the region of the 3'-untranslated region between nucleotides 3125 and 3432 and to reduce levels of the full-length mRNA. During cell growth and confluence, the expression of tristetraprolin mRNA was inversely correlated with that of the full-length cyclooxygenase-2 transcript, and transfection of tristetraprolin into HCA-7 cells reduced the level of full-length cyclooxygenase-2 mRNA. However, the truncated transcript escaped tristetraprolin binding and downregulation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3' Untranslated Regions,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTGS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Tristetraprolin,
http://linkedlifedata.com/resource/pubmed/chemical/ZFP36 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13928-35
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12578839-3' Untranslated Regions,
pubmed-meshheading:12578839-Base Sequence,
pubmed-meshheading:12578839-Binding Sites,
pubmed-meshheading:12578839-Blotting, Northern,
pubmed-meshheading:12578839-Blotting, Western,
pubmed-meshheading:12578839-Catalysis,
pubmed-meshheading:12578839-Cells, Cultured,
pubmed-meshheading:12578839-Cross-Linking Reagents,
pubmed-meshheading:12578839-Cyclooxygenase 2,
pubmed-meshheading:12578839-DNA, Complementary,
pubmed-meshheading:12578839-DNA-Binding Proteins,
pubmed-meshheading:12578839-Dose-Response Relationship, Drug,
pubmed-meshheading:12578839-Down-Regulation,
pubmed-meshheading:12578839-Endothelium, Vascular,
pubmed-meshheading:12578839-Humans,
pubmed-meshheading:12578839-Immediate-Early Proteins,
pubmed-meshheading:12578839-Isoenzymes,
pubmed-meshheading:12578839-Lipopolysaccharides,
pubmed-meshheading:12578839-Membrane Proteins,
pubmed-meshheading:12578839-Molecular Sequence Data,
pubmed-meshheading:12578839-Polyadenylation,
pubmed-meshheading:12578839-Precipitin Tests,
pubmed-meshheading:12578839-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:12578839-Protein Binding,
pubmed-meshheading:12578839-RNA,
pubmed-meshheading:12578839-RNA, Messenger,
pubmed-meshheading:12578839-Ribonucleases,
pubmed-meshheading:12578839-Time Factors,
pubmed-meshheading:12578839-Transcription, Genetic,
pubmed-meshheading:12578839-Transfection,
pubmed-meshheading:12578839-Tristetraprolin,
pubmed-meshheading:12578839-Tumor Cells, Cultured,
pubmed-meshheading:12578839-Umbilical Veins,
pubmed-meshheading:12578839-Up-Regulation
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pubmed:year |
2003
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pubmed:articleTitle |
Tristetraprolin binds to the 3'-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site.
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pubmed:affiliation |
Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6602, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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