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    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

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    Author
    Lappas, M; Permezel, M; Rice, GE
    Date
    2003-04-01
    Source Title
    JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
    Publisher
    ENDOCRINE SOC
    University of Melbourne Author/s
    Lappas, Martha; Permezel, John; Rice, Gregory
    Affiliation
    Obstetrics And Gynaecology Royal Women'S Hospital/Mercy
    Metadata
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    Document Type
    Journal Article
    Citations
    Lappas, 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.
    Access Status
    This item is currently not available from this repository
    URI
    http://hdl.handle.net/11343/26476
    DOI
    10.1210/jc.2002-021677
    Description

    C1 - Journal Articles Refereed

    Abstract
    The 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.
    Keywords
    Obstetrics and Gynaecology ; Endocrine Organs and Diseases (incl. Diabetes)

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