rdf:type |
|
lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0085536,
umls-concept:C0086982,
umls-concept:C0109317,
umls-concept:C0185117,
umls-concept:C0387583,
umls-concept:C0752312,
umls-concept:C1150579,
umls-concept:C1314939,
umls-concept:C1333340,
umls-concept:C1366882,
umls-concept:C1370600,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1709843,
umls-concept:C2911684
|
pubmed:issue |
4
|
pubmed:dateCreated |
2001-8-24
|
pubmed:abstractText |
Prostaglandins play regulatory roles in a variety of physiological and pathological processes in immune response and inflammation. Epigallocatechin-3-gallate (EGCG) is known to potent antitumor agent with antioxidant property. We first investigated the effect of EGCG on the production of prostaglandin E(2) (PGE(2)) and the expression of cyclooxygenase-2 (COX-2), the rate-limiting enzyme in the synthesis of PGE(2), using macrophage cell line, Raw264.7. Our results showed that COX-2 expression and PGE(2) production are upregulated by EGCG treatment and that this induction of COX-2 is regulated in part at the transcriptional level. In addition, we demonstrated the signal transduction pathway of mitogen-activated protein kinase (MAP kinase) in EGCG-mediated COX-2 expression. The MEK inhibitor (PD098059) prevented EGCG-induced COX-2 expression, whereas sodium orthovanadate (protein-tyrosine phosphatase inhibitor) significantly enhanced COX-2 expression and PGE(2) production. These results suggest that EGCG mediated COX-2 expression and PGE(2) production is associated with the activation of both the ERK and protein-tyrosine phosphatase signaling pathways.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catechin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Flavonoids,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PD 98059,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadates,
http://linkedlifedata.com/resource/pubmed/chemical/epigallocatechin gallate
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
286
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
721-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11520057-Animals,
pubmed-meshheading:11520057-Catechin,
pubmed-meshheading:11520057-Cell Line,
pubmed-meshheading:11520057-Cyclooxygenase 2,
pubmed-meshheading:11520057-Dinoprostone,
pubmed-meshheading:11520057-Enzyme Inhibitors,
pubmed-meshheading:11520057-Flavonoids,
pubmed-meshheading:11520057-Isoenzymes,
pubmed-meshheading:11520057-MAP Kinase Signaling System,
pubmed-meshheading:11520057-Macrophages,
pubmed-meshheading:11520057-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:11520057-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11520057-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:11520057-Protein Tyrosine Phosphatases,
pubmed-meshheading:11520057-RNA, Messenger,
pubmed-meshheading:11520057-Signal Transduction,
pubmed-meshheading:11520057-Up-Regulation,
pubmed-meshheading:11520057-Vanadates
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pubmed:year |
2001
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pubmed:articleTitle |
Involvement of ERK and protein tyrosine phosphatase signaling pathways in EGCG-induced cyclooxygenase-2 expression in Raw 264.7 cells.
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pubmed:affiliation |
Department of Immunology, School of Medicine, Keimyung University, 194 DongSan-Dong Jung-Gu, Taegu, 700-712, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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