File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Interleukin-1β induces cyclo-oxygenase-2 expression in gastric cancer cells by the p38 and p44/42 mitogen-activated protein kinase signaling pathways

TitleInterleukin-1β induces cyclo-oxygenase-2 expression in gastric cancer cells by the p38 and p44/42 mitogen-activated protein kinase signaling pathways
Authors
KeywordsCyclooxygenase-2
Human gastric cancer cells
Interleukin-1β
Mitogen-activated protein kinase
Mitogen-activated protein-Erk kinase
P38
Issue Date2001
PublisherWiley-Blackwell Publishing Asia. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JGH
Citation
Journal Of Gastroenterology And Hepatology, 2001, v. 16 n. 10, p. 1098-1104 How to Cite?
AbstractBackground and Aims: Cyclo-oxygenase-2 (COX-2) is the inducible enzyme in the gastric mucosa responsible for prostaglandin production during inflammation and ulcer healing. The regulation of COX-2 gene expression in gastric epithelial cells is not well understood. In this study, we investigated the effect of interleukin (IL)-1β on COX-2 expression in the human gastric cancer cell, and explored the signaling pathways involved. Methods: Gastric cancer cell line AGS was treated with IL-1β or the inhibitors of mitogen-activated protein-Erk kinase (MEK) and p38 mitogen-activated protein (MAP) kinase prior to the addition of IL-1β. The COX-2 mRNA or protein levels were measured by using RT-PCR or western blot analysis, respectively. Prostaglandin E2 (PGE2) production/secretion was determined by using the prostaglandin E2 EIA assay. The phosphorylation/activation of p44/42 and p38 MAP kinases were determined by using western blot analysis and using phospho-specific antibodies. Results: Interleukin-1β treatment dose- and time-dependently increased COX-2 mRNA and protein expression levels, and enhanced PGE2 production/secretion in AGS cells. In contrast, IL-1β had no effect on the level of the constitutively expressed COX-1. In parallel to the increase of COX-2, we showed that p44/42 and p38 MAP kinase activities were also upregulated by IL-1β treatment. To demonstrate the cause-effect relationship, we showed that inhibition of MEK and p38 MAP kinase with specific inhibitors suppressed IL-1β-mediated increases in COX-2 mRNA and protein levels, and the PGE2 production. Conclusions: Our results demonstrated that in human gastric cancer cells, IL-1β upregulates the COX-2 gene expression through the activation of MEK/p44/42 and p38 MAP kinases pathway. © 2001 Blackwell Science Asia Pty Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/167675
ISSN
2023 Impact Factor: 3.7
2023 SCImago Journal Rankings: 1.179
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFan, XMen_US
dc.contributor.authorWong, BCYen_US
dc.contributor.authorLin, MCMen_US
dc.contributor.authorCho, CHen_US
dc.contributor.authorWang, WPen_US
dc.contributor.authorKung, HFen_US
dc.contributor.authorLam, SKen_US
dc.date.accessioned2012-10-08T03:09:50Z-
dc.date.available2012-10-08T03:09:50Z-
dc.date.issued2001en_US
dc.identifier.citationJournal Of Gastroenterology And Hepatology, 2001, v. 16 n. 10, p. 1098-1104en_US
dc.identifier.issn0815-9319en_US
dc.identifier.urihttp://hdl.handle.net/10722/167675-
dc.description.abstractBackground and Aims: Cyclo-oxygenase-2 (COX-2) is the inducible enzyme in the gastric mucosa responsible for prostaglandin production during inflammation and ulcer healing. The regulation of COX-2 gene expression in gastric epithelial cells is not well understood. In this study, we investigated the effect of interleukin (IL)-1β on COX-2 expression in the human gastric cancer cell, and explored the signaling pathways involved. Methods: Gastric cancer cell line AGS was treated with IL-1β or the inhibitors of mitogen-activated protein-Erk kinase (MEK) and p38 mitogen-activated protein (MAP) kinase prior to the addition of IL-1β. The COX-2 mRNA or protein levels were measured by using RT-PCR or western blot analysis, respectively. Prostaglandin E2 (PGE2) production/secretion was determined by using the prostaglandin E2 EIA assay. The phosphorylation/activation of p44/42 and p38 MAP kinases were determined by using western blot analysis and using phospho-specific antibodies. Results: Interleukin-1β treatment dose- and time-dependently increased COX-2 mRNA and protein expression levels, and enhanced PGE2 production/secretion in AGS cells. In contrast, IL-1β had no effect on the level of the constitutively expressed COX-1. In parallel to the increase of COX-2, we showed that p44/42 and p38 MAP kinase activities were also upregulated by IL-1β treatment. To demonstrate the cause-effect relationship, we showed that inhibition of MEK and p38 MAP kinase with specific inhibitors suppressed IL-1β-mediated increases in COX-2 mRNA and protein levels, and the PGE2 production. Conclusions: Our results demonstrated that in human gastric cancer cells, IL-1β upregulates the COX-2 gene expression through the activation of MEK/p44/42 and p38 MAP kinases pathway. © 2001 Blackwell Science Asia Pty Ltd.en_US
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing Asia. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JGHen_US
dc.relation.ispartofJournal of Gastroenterology and Hepatologyen_US
dc.subjectCyclooxygenase-2-
dc.subjectHuman gastric cancer cells-
dc.subjectInterleukin-1β-
dc.subjectMitogen-activated protein kinase-
dc.subjectMitogen-activated protein-Erk kinase-
dc.subjectP38-
dc.subject.meshAdenocarcinoma - Metabolismen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCyclooxygenase 2en_US
dc.subject.meshDinoprostone - Biosynthesis - Geneticsen_US
dc.subject.meshEnzyme Inhibitors - Pharmacologyen_US
dc.subject.meshFlavonoids - Pharmacologyen_US
dc.subject.meshGene Expression - Drug Effectsen_US
dc.subject.meshHumansen_US
dc.subject.meshImidazoles - Pharmacologyen_US
dc.subject.meshInterleukin-1 - Pharmacologyen_US
dc.subject.meshIsoenzymes - Genetics - Metabolismen_US
dc.subject.meshMembrane Proteinsen_US
dc.subject.meshMitogen-Activated Protein Kinase 1 - Metabolismen_US
dc.subject.meshMitogen-Activated Protein Kinases - Metabolismen_US
dc.subject.meshProstaglandin-Endoperoxide Synthases - Genetics - Metabolismen_US
dc.subject.meshPyridines - Pharmacologyen_US
dc.subject.meshRna, Messenger - Biosynthesisen_US
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen_US
dc.subject.meshSignal Transductionen_US
dc.subject.meshStomach Neoplasms - Metabolismen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.subject.meshUp-Regulationen_US
dc.subject.meshP38 Mitogen-Activated Protein Kinasesen_US
dc.titleInterleukin-1β induces cyclo-oxygenase-2 expression in gastric cancer cells by the p38 and p44/42 mitogen-activated protein kinase signaling pathwaysen_US
dc.typeArticleen_US
dc.identifier.emailWong, BCY:bcywong@hku.hken_US
dc.identifier.emailLin, MCM:mcllin@hkucc.hku.hken_US
dc.identifier.authorityWong, BCY=rp00429en_US
dc.identifier.authorityLin, MCM=rp00746en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1046/j.1440-1746.2001.02593.xen_US
dc.identifier.pmid11686835en_US
dc.identifier.scopuseid_2-s2.0-0034767758en_US
dc.identifier.hkuros73399-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034767758&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume16en_US
dc.identifier.issue10en_US
dc.identifier.spage1098en_US
dc.identifier.epage1104en_US
dc.identifier.isiWOS:000179450900005-
dc.publisher.placeAustraliaen_US
dc.identifier.scopusauthoridFan, XM=36991450500en_US
dc.identifier.scopusauthoridWong, BCY=7402023340en_US
dc.identifier.scopusauthoridLin, MCM=7404816359en_US
dc.identifier.scopusauthoridCho, CH=14067000400en_US
dc.identifier.scopusauthoridWang, WP=7501765704en_US
dc.identifier.scopusauthoridKung, HF=7402514190en_US
dc.identifier.scopusauthoridLam, SK=7402279473en_US
dc.identifier.issnl0815-9319-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats