Source:http://linkedlifedata.com/resource/pubmed/id/12512699
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4 Pt 1
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pubmed:dateCreated |
2003-1-6
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pubmed:abstractText |
Prostaglandin endoperoxide H2 (PGH2) is generated from arachidonic acid by either constitutive (COX-1) or inducible (COX-2) cyclooxygenases. In arterial wall PGH2 is converted by PGI2 synthase (PGI-S) to prostacyclin (PGI2), and in platelets by thromboxane synthase (TX-S) to thromboxane (TXA2). Other prostanoids as PGD2, PGF2alpha, or PGE2 were believed to arise non-enzymatically from PGH2. Only recently, human prostaglandin E synthase (PGE-S) has been identified and cloned as a membrane bound, microsomal, glutathione-dependent inducible enzyme. Here we demonstrated that interleukin 1beta (IL-1beta) is an inducer of COX-2 and PGE-S in human umbilical vein endothelial cells (HUVEC). Functional expression of PGE-S was measured at the level of specific mRNA by semi-quantitative RT-PCR, PGE-S protein was detected by Western blot in HUVEC, while PGE2 was measured by immunoassay in the supernatant. Actinomycin D, a classical transcription inhibitor, was used to prove that indeed IL-1beta induced the functional PGE-S enzyme. PGE2 generation in HUVEC was inhibited by indomethacin, acetaminophen and dexamethasone. In conclusion, we found that in cultured endothelial cells IL-1beta induced as evidenced by the appearance of its transcript and its functional enzyme. The induction of endothelial PGE-S and COX-2 appeared to be and their transcripts were induced as fast as one might expect from immediate early genes. It means that IL-1beta-triggered-PGE2 biosynthesis in endothelial cells is probably regulated by induction of both COX-2 and PGE-S. This is way we hypothesise the existence of at least two distinct pools of COX-2: the first selectively coupled to PGE-S and the second one that is coupled to PGI-S yielding the main endothelial product--PGI2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
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, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/prostaglandin-E synthase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0867-5910
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
643-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12512699-Blotting, Western,
pubmed-meshheading:12512699-Cells, Cultured,
pubmed-meshheading:12512699-Cyclooxygenase 2,
pubmed-meshheading:12512699-Endothelium, Vascular,
pubmed-meshheading:12512699-Humans,
pubmed-meshheading:12512699-Interleukin-1,
pubmed-meshheading:12512699-Intramolecular Oxidoreductases,
pubmed-meshheading:12512699-Isoenzymes,
pubmed-meshheading:12512699-Membrane Proteins,
pubmed-meshheading:12512699-Osmolar Concentration,
pubmed-meshheading:12512699-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:12512699-RNA, Messenger,
pubmed-meshheading:12512699-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12512699-Umbilical Veins
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pubmed:year |
2002
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pubmed:articleTitle |
Interleukin 1beta induces functional prostaglandin E synthase in cultured human umbilical vein endothelial cells.
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pubmed:affiliation |
Molecular Pharmacology Laboratory, Chair of Pharmacology, Medical College of Jagiellonian University, Grzegórzecka 16 31-531 Krakow, Poland. miuracz@kinga.cyf-kr.edu.pl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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