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dc.contributor.authorLappas, M
dc.contributor.authorPermezel, M
dc.contributor.authorRice, GE
dc.date.available2014-05-21T19:34:19Z
dc.date.issued2003-04-01
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000182211000049&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=d4d813f4571fa7d6246bdc0dfeca3a1c
dc.identifier.citationLappas, M., Permezel, M. & Rice, G. E. (2003). N-acetyl-cysteine inhibits phospholipid metabolism, proinflammatory cytokine release, protease activity, and nuclear factor-kappa B deoxyribonucleic acid-binding activity in human fetal membranes in vitro. JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM, 88 (4), pp.1723-1729. https://doi.org/10.1210/jc.2002-021677.
dc.identifier.issn0021-972X
dc.identifier.urihttp://hdl.handle.net/11343/26476
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractThe production of reactive oxygen species (ROS), prostaglandins (PGs), proinflammatory cytokines, and proteases has been implicated in the pathogenesis of term and preterm labor. The nuclear factor-kappaB (NF-kappaB) transcription pathway is activated by ROS and is a key regulator of PGs, proinflammatory cytokine release, and protease activity. N-Acetyl-cysteine (NAC) is an antioxidant that through its ability to scavenger ROS suppresses NF-kappaB DNA-binding activity and resultant gene expression. The aim of this study was to elucidate the effect of NAC on NF-kappaB DNA-binding activity, phospholipid metabolism, cytokine release, and protease activity from human fetal membranes. Human amnion and choriodecidua (n = 9 separate placentas) were treated with 0 (control), 5, 10, or 15 mM NAC in the presence of 10 micro g/ml lipopolysaccharide. After 6-h incubation, the tissues were collected, NF-kappaB DNA binding activity was assessed by gel shift binding assays, and matrix metalloproteinase-9 and urokinase-type plasminogen activator activity were determined by zymography. The incubation medium was collected and assayed for type II phospholipase A(2) tissue content, IL-6, IL-8, TNFalpha, and 8-isoprostane release by ELISA. The release of PGF(2alpha) was measured by RIA. Treatment of fetal membranes with NAC significantly suppressed lipopolysaccharide-stimulated type II phospholipase A(2) release and content; PGF(2alpha), IL-6, IL-8, TNFalpha, and 8-isoprostane release; and matrix metalloproteinase-9 and urokinase-type plasminogen activator enzyme activity and suppressed NF-kappaB DNA-binding activity (by ANOVA, P < 0.05). The data presented in this study demonstrate that NAC inhibits an NF-kappaB-activated pathway and subsequent phospholipid metabolism, proinflammatory cytokine release, and protease activity in human fetal membranes.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherENDOCRINE SOC
dc.subjectObstetrics and Gynaecology ; Endocrine Organs and Diseases (incl. Diabetes)
dc.titleN-acetyl-cysteine inhibits phospholipid metabolism, proinflammatory cytokine release, protease activity, and nuclear factor-kappa B deoxyribonucleic acid-binding activity in human fetal membranes in vitro
dc.typeJournal Article
dc.identifier.doi10.1210/jc.2002-021677
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentObstetrics And Gynaecology Royal Women'S Hospital/Mercy
melbourne.source.titleJOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
melbourne.source.volume88
melbourne.source.issue4
melbourne.source.pages1723-1729
dc.research.coderfcd321014
dc.research.codeseo1998730105
melbourne.publicationid22113
melbourne.elementsid260180
melbourne.contributor.authorLappas, Martha
melbourne.contributor.authorPermezel, John
melbourne.contributor.authorRice, Gregory
dc.identifier.eissn1945-7197
melbourne.accessrightsThis item is currently not available from this repository


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