rdf:type |
|
lifeskim:mentions |
umls-concept:C0007600,
umls-concept:C0038925,
umls-concept:C0040669,
umls-concept:C0041904,
umls-concept:C0086418,
umls-concept:C0162493,
umls-concept:C0387583,
umls-concept:C1412362,
umls-concept:C1427539,
umls-concept:C1510779,
umls-concept:C1553655
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
1998-11-20
|
pubmed:abstractText |
Five-lipoxygenase-activating protein (FLAP) is usually described as an essential protein to activate the leukotriene (LTs) synthesis via the 5-lipoxygenase pathway. In the enterocyte model HT29 cl.19A cell line, 5-lipoxygenase metabolism was found despite the lack of FLAP expression. Therefore HT29 cl.19A represents an original mammalian model to study FLAP-dependent leukotriene synthesis. In FLAP cDNA transfected HT29 cl.19A cells, FLAP expression led to an increase in cyclooxygenase pathway products (mainly PGE2) without an increase in 5-lipoxygenase metabolism. This increase in PGE2 synthesis was associated with a cyclooxygenase-2 upregulation in comparison to untransfected HT29 cl.19A cells. These results suggest a possible interaction between the two major pathways of arachidonic acid metabolism.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5-Lipoxygenase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ALOX5AP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Leukotriene B4,
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/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
|
pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
437
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
49-55
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pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:9804170-5-Lipoxygenase-Activating Proteins,
pubmed-meshheading:9804170-Baculoviridae,
pubmed-meshheading:9804170-Blotting, Western,
pubmed-meshheading:9804170-Carrier Proteins,
pubmed-meshheading:9804170-Cyclooxygenase 2,
pubmed-meshheading:9804170-Dinoprostone,
pubmed-meshheading:9804170-HT29 Cells,
pubmed-meshheading:9804170-Humans,
pubmed-meshheading:9804170-Immunohistochemistry,
pubmed-meshheading:9804170-Isoenzymes,
pubmed-meshheading:9804170-Leukotriene B4,
pubmed-meshheading:9804170-Membrane Proteins,
pubmed-meshheading:9804170-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:9804170-Recombinant Proteins,
pubmed-meshheading:9804170-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:9804170-Transfection,
pubmed-meshheading:9804170-Up-Regulation
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pubmed:year |
1998
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pubmed:articleTitle |
Cyclooxygenase-2 up-regulation after FLAP transfection in human adenocarcinoma cell line HT29 cl.19A.
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pubmed:affiliation |
Facultés de Médecine et de Pharmacie, Limoges, France.
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pubmed:publicationType |
Journal Article
|