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Anti-inflammatory mechanism of α-viniferin regulates lipopolysaccharide-induced release of proinflammatory mediators in BV2 microglial cells

DC Field Value Language
dc.contributor.author김락균-
dc.date.accessioned2018-05-10T06:46:11Z-
dc.date.available2018-05-10T06:46:11Z-
dc.date.issued2014-
dc.identifier.issn0008-8749-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/158598-
dc.description.abstractα-Viniferin is an oligostilbene of trimeric resveratrol and has anticancer activity; however, the molecular mechanism underlying the anti-inflammatory effects of α-viniferin has not been completely elucidated thus far. Therefore, we determined the mechanism by which α-viniferin regulates lipopolysaccharide (LPS)-induced expression of proinflammatory mediators in BV2 microglial cells. Treatment with α-viniferin isolated from Clematis mandshurica decreased LPS-induced production of nitric oxide (NO) and prostaglandin E2 (PGE2). α-Viniferin also downregulated the LPS-induced expression of proinflammatory genes such as iNOS and COX-2 by suppressing the activity of nuclear factor kappa B (NF-κB) via dephosphorylation of Akt/PI3K. Treatment with a specific NF-κB inhibitor, pyrrolidine dithiocarbamate (PDTC), indirectly showed that NF-κB is a crucial transcription factor for expression of these genes in the early stage of inflammation. Additionally, our results indicated that α-viniferin suppresses NO and PGE2 production in the late stage of inflammation through induction of heme oxygenase-1 (HO-1) regulated by nuclear factor erythroid 2-related factor (Nrf2). Taken together, our data indicate that α-viniferin suppresses the expression of proinflammatory genes iNOS and COX-2 in the early stage of inflammation by inhibiting the Akt/PI3K-dependent NF-κB activation and inhibits the production of proinflammatory mediators NO and PGE2 in the late stage by stimulating Nrf2-mediated HO-1 signaling pathway in LPS-stimulated BV2 microglial cells. These results suggest that α-viniferin may be a potential candidate to regulate LPS-induced inflammation.-
dc.description.statementOfResponsibilityrestriction-
dc.languageEnglish-
dc.publisherElsevier-
dc.relation.isPartOfCELLULAR IMMUNOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAnimals-
dc.subject.MESHAnti-Inflammatory Agents, Non-Steroidal/pharmacology*-
dc.subject.MESHBenzofurans/pharmacology*-
dc.subject.MESHCell Line-
dc.subject.MESHClematis-
dc.subject.MESHCyclooxygenase 2/biosynthesis*-
dc.subject.MESHDinoprostone/biosynthesis-
dc.subject.MESHHeme Oxygenase-1/biosynthesis-
dc.subject.MESHHeme Oxygenase-1/immunology-
dc.subject.MESHInflammation Mediators-
dc.subject.MESHLipopolysaccharides-
dc.subject.MESHMembrane Proteins/biosynthesis-
dc.subject.MESHMembrane Proteins/immunology-
dc.subject.MESHMice-
dc.subject.MESHMicroglia/immunology*-
dc.subject.MESHNF-E2-Related Factor 2/biosynthesis-
dc.subject.MESHNF-E2-Related Factor 2/genetics-
dc.subject.MESHNF-kappa B/antagonists & inhibitors*-
dc.subject.MESHNF-kappa B/genetics-
dc.subject.MESHNitric Oxide/biosynthesis-
dc.subject.MESHNitric Oxide Synthase Type II/biosynthesis*-
dc.subject.MESHPhosphatidylinositol 3-Kinases/antagonists & inhibitors-
dc.subject.MESHPhosphatidylinositol 3-Kinases/immunology-
dc.subject.MESHPhosphorylation-
dc.subject.MESHPlant Extracts-
dc.subject.MESHPlant Roots-
dc.subject.MESHProto-Oncogene Proteins c-akt/antagonists & inhibitors-
dc.subject.MESHProto-Oncogene Proteins c-akt/immunology-
dc.subject.MESHPyrrolidines/pharmacology-
dc.subject.MESHRNA Interference-
dc.subject.MESHRNA, Small Interfering-
dc.subject.MESHThiocarbamates/pharmacology-
dc.titleAnti-inflammatory mechanism of α-viniferin regulates lipopolysaccharide-induced release of proinflammatory mediators in BV2 microglial cells-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Life Science-
dc.contributor.googleauthorMatharage Gayani Dilshara-
dc.contributor.googleauthorKyoung-Tae Lee-
dc.contributor.googleauthorHee Ju Kim-
dc.contributor.googleauthorHak-Ju Lee-
dc.contributor.googleauthorYung Hyun Choi-
dc.contributor.googleauthorChang-Min Lee-
dc.contributor.googleauthorLark Kyun Kim-
dc.contributor.googleauthorGi-Young Kim-
dc.identifier.doi10.1016/j.cellimm.2014.04.009-
dc.contributor.localIdA04520-
dc.relation.journalcodeJ00498-
dc.identifier.eissn1090-2163-
dc.identifier.pmid24859013-
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S0008874914000744-
dc.contributor.alternativeNameKim, Lark Kyun-
dc.contributor.affiliatedAuthorKim, Lark Kyun-
dc.citation.volume290-
dc.citation.number1-
dc.citation.startPage21-
dc.citation.endPage29-
dc.identifier.bibliographicCitationCELLULAR IMMUNOLOGY, Vol.290(1) : 21-29, 2014-
dc.identifier.rimsid43177-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers

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