pubmed-article:15542609 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15542609 | lifeskim:mentions | umls-concept:C0044894 | lld:lifeskim |
pubmed-article:15542609 | lifeskim:mentions | umls-concept:C1527249 | lld:lifeskim |
pubmed-article:15542609 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:15542609 | pubmed:dateCreated | 2005-2-7 | lld:pubmed |
pubmed-article:15542609 | pubmed:abstractText | Prostaglandin E2 (PGE2) can stimulate tumor progression by modulating several proneoplastic pathways, including proliferation, angiogenesis, cell migration, invasion, and apoptosis. Although steady-state tissue levels of PGE2 stem from relative rates of biosynthesis and breakdown, most reports examining PGE2 have focused solely on the cyclooxygenase-dependent formation of this bioactive lipid. Enzymatic degradation of PGE2 involves the NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH). The present study examined a range of normal tissues in the human and mouse and found high levels of 15-PGDH in the large intestine. By contrast, the expression of 15-PGDH is decreased in several colorectal carcinoma cell lines and in other human malignancies such as breast and lung carcinomas. Consistent with these findings, we observe diminished 15-Pgdh expression in ApcMin+/- mouse adenomas. Enzymatic activity of 15-PGDH correlates with expression levels and the genetic disruption of 15-Pgdh completely blocks production of the urinary PGE2 metabolite. Finally, 15-PGDH expression and activity are significantly down-regulated in human colorectal carcinomas relative to matched normal tissue. In summary, these results suggest a novel tumor suppressive role for 15-PGDH due to loss of expression during colorectal tumor progression. | lld:pubmed |
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pubmed-article:15542609 | pubmed:language | eng | lld:pubmed |
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pubmed-article:15542609 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15542609 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15542609 | pubmed:month | Feb | lld:pubmed |
pubmed-article:15542609 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15542609 | pubmed:author | pubmed-author:DuBoisRaymond... | lld:pubmed |
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pubmed-article:15542609 | pubmed:author | pubmed-author:TaiHsin-Hsiun... | lld:pubmed |
pubmed-article:15542609 | pubmed:author | pubmed-author:BuchananF... | lld:pubmed |
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pubmed-article:15542609 | pubmed:author | pubmed-author:KatkuriSharad... | lld:pubmed |
pubmed-article:15542609 | pubmed:author | pubmed-author:MannJason RJR | lld:pubmed |
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pubmed-article:15542609 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15542609 | pubmed:day | 4 | lld:pubmed |
pubmed-article:15542609 | pubmed:volume | 280 | lld:pubmed |
pubmed-article:15542609 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15542609 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15542609 | pubmed:pagination | 3217-23 | lld:pubmed |
pubmed-article:15542609 | pubmed:dateRevised | 2011-5-25 | lld:pubmed |
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pubmed-article:15542609 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15542609 | pubmed:articleTitle | 15-Hydroxyprostaglandin dehydrogenase is down-regulated in colorectal cancer. | lld:pubmed |
pubmed-article:15542609 | pubmed:affiliation | Department of Medicine, Cell and Developmental Biology, Vanderbilt University Medical Center and the Vanderbilt-Ingram Cancer Center, Nashville, Tennessee 37232-6838, USA. | lld:pubmed |
pubmed-article:15542609 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15542609 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15542609 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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