The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells
The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal...
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| Veröffentlicht in: | Biology of reproduction 2007-04, Vol.76 (4), p.654-659 |
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| creator | Li, Wei Unlugedik, Elif Bocking, Alan D Challis, John R. G |
| description | The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal membranes by causing matrix degradation. The aim of this study was to assess the mediating role of PGs on lipopolysaccharide (LPS)-induced MMP9 secretion in vitro. ELISA, zymography, and Western blotting were performed on cells and medium from cultures of purified chorion trophoblasts (CTs) and syncytiotrophoblasts (STs) from the human placenta and fetal membranes treated with LPS, meloxicam, (a selective prostaglandin-endoperoxide synthase 2 [PTGS2, previously known as cyclooxygenase 2] inhibitor), or replacement PGE2 or PGF2alpha. LPS significantly (P < 0.01) increased proMMP9 secretion and prostaglandin E2 (PGE2) output by cultured CTs and STs, but there was no effect on tissue inhibitor of matrix metalloproteinase 1 (TIMP1) secretion. In these cells, meloxicam significantly blocked LPS-induced proMMP9 secretion and PGE2 output (P < 0.01). Exogenous PGE2 and PGF2alpha significantly reversed the reduction in proMMP9 secretion caused by meloxicam in a dose-dependent manner (P < 0.01). The expression of PTGS2 protein in CTs and STs was increased dramatically after LPS treatment, but there was no significant effect on the expression of PTGS1 (previously known as cyclooxygenase 1), membrane-associated prostaglandin E synthases (membrane-associated PTGES, previously known as mPGES) 1 and 2, or cytosolic prostaglandin E synthase (cytosolic PTGES, previously knows as cPGES) proteins. Our results suggest that PGs may mediate the selective increase in MMP9 after exposure of trophoblast cells to LPS. There was no effect of LPS on TIMP1. Understanding this relationship may help in developing strategies for the prevention and management of pPROM and preterm labor. |
| doi_str_mv | 10.1095/biolreprod.106.057034 |
| format | Article |
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G</creator><creatorcontrib>Li, Wei ; Unlugedik, Elif ; Bocking, Alan D ; Challis, John R. G</creatorcontrib><description>The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal membranes by causing matrix degradation. The aim of this study was to assess the mediating role of PGs on lipopolysaccharide (LPS)-induced MMP9 secretion in vitro. ELISA, zymography, and Western blotting were performed on cells and medium from cultures of purified chorion trophoblasts (CTs) and syncytiotrophoblasts (STs) from the human placenta and fetal membranes treated with LPS, meloxicam, (a selective prostaglandin-endoperoxide synthase 2 [PTGS2, previously known as cyclooxygenase 2] inhibitor), or replacement PGE2 or PGF2alpha. LPS significantly (P < 0.01) increased proMMP9 secretion and prostaglandin E2 (PGE2) output by cultured CTs and STs, but there was no effect on tissue inhibitor of matrix metalloproteinase 1 (TIMP1) secretion. In these cells, meloxicam significantly blocked LPS-induced proMMP9 secretion and PGE2 output (P < 0.01). Exogenous PGE2 and PGF2alpha significantly reversed the reduction in proMMP9 secretion caused by meloxicam in a dose-dependent manner (P < 0.01). The expression of PTGS2 protein in CTs and STs was increased dramatically after LPS treatment, but there was no significant effect on the expression of PTGS1 (previously known as cyclooxygenase 1), membrane-associated prostaglandin E synthases (membrane-associated PTGES, previously known as mPGES) 1 and 2, or cytosolic prostaglandin E synthase (cytosolic PTGES, previously knows as cPGES) proteins. Our results suggest that PGs may mediate the selective increase in MMP9 after exposure of trophoblast cells to LPS. There was no effect of LPS on TIMP1. Understanding this relationship may help in developing strategies for the prevention and management of pPROM and preterm labor.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.106.057034</identifier><identifier>PMID: 17167167</identifier><language>eng</language><publisher>United States: Society for the Study of Reproduction, Inc</publisher><subject>Cells, Cultured ; Cyclooxygenase 2 - metabolism ; Dose-Response Relationship, Drug ; Enzyme Precursors - secretion ; Extraembryonic Membranes - drug effects ; Extraembryonic Membranes - metabolism ; Extraembryonic Membranes - secretion ; Female ; human fetal membrane ; Humans ; lipopolysaccharide ; Lipopolysaccharides - pharmacology ; matrix metalloproteinase ; Matrix Metalloproteinase 9 - secretion ; mechanisms of hormone action ; Membrane Proteins - antagonists & inhibitors ; Membrane Proteins - metabolism ; Placenta - drug effects ; Placenta - metabolism ; Placenta - secretion ; Pregnancy ; prostaglandin ; Prostaglandins - physiology ; syncytiotrophoblast ; Tissue Inhibitor of Metalloproteinase-1 - secretion ; trophoblast</subject><ispartof>Biology of reproduction, 2007-04, Vol.76 (4), p.654-659</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b518t-7df545aa861c5d25757a26221cf3ed10b28ad62f8ab67073707d785dad08a7173</citedby><cites>FETCH-LOGICAL-b518t-7df545aa861c5d25757a26221cf3ed10b28ad62f8ab67073707d785dad08a7173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://bioone.org/doi/pdf/10.1095/biolreprod.106.057034$$EPDF$$P50$$Gbioone$$H</linktopdf><link.rule.ids>314,776,780,26955,27901,27902,52338</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17167167$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Unlugedik, Elif</creatorcontrib><creatorcontrib>Bocking, Alan D</creatorcontrib><creatorcontrib>Challis, John R. G</creatorcontrib><title>The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal membranes by causing matrix degradation. The aim of this study was to assess the mediating role of PGs on lipopolysaccharide (LPS)-induced MMP9 secretion in vitro. ELISA, zymography, and Western blotting were performed on cells and medium from cultures of purified chorion trophoblasts (CTs) and syncytiotrophoblasts (STs) from the human placenta and fetal membranes treated with LPS, meloxicam, (a selective prostaglandin-endoperoxide synthase 2 [PTGS2, previously known as cyclooxygenase 2] inhibitor), or replacement PGE2 or PGF2alpha. LPS significantly (P < 0.01) increased proMMP9 secretion and prostaglandin E2 (PGE2) output by cultured CTs and STs, but there was no effect on tissue inhibitor of matrix metalloproteinase 1 (TIMP1) secretion. In these cells, meloxicam significantly blocked LPS-induced proMMP9 secretion and PGE2 output (P < 0.01). Exogenous PGE2 and PGF2alpha significantly reversed the reduction in proMMP9 secretion caused by meloxicam in a dose-dependent manner (P < 0.01). The expression of PTGS2 protein in CTs and STs was increased dramatically after LPS treatment, but there was no significant effect on the expression of PTGS1 (previously known as cyclooxygenase 1), membrane-associated prostaglandin E synthases (membrane-associated PTGES, previously known as mPGES) 1 and 2, or cytosolic prostaglandin E synthase (cytosolic PTGES, previously knows as cPGES) proteins. Our results suggest that PGs may mediate the selective increase in MMP9 after exposure of trophoblast cells to LPS. There was no effect of LPS on TIMP1. Understanding this relationship may help in developing strategies for the prevention and management of pPROM and preterm labor.</description><subject>Cells, Cultured</subject><subject>Cyclooxygenase 2 - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzyme Precursors - secretion</subject><subject>Extraembryonic Membranes - drug effects</subject><subject>Extraembryonic Membranes - metabolism</subject><subject>Extraembryonic Membranes - secretion</subject><subject>Female</subject><subject>human fetal membrane</subject><subject>Humans</subject><subject>lipopolysaccharide</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>matrix metalloproteinase</subject><subject>Matrix Metalloproteinase 9 - secretion</subject><subject>mechanisms of hormone action</subject><subject>Membrane Proteins - antagonists & inhibitors</subject><subject>Membrane Proteins - metabolism</subject><subject>Placenta - drug effects</subject><subject>Placenta - metabolism</subject><subject>Placenta - secretion</subject><subject>Pregnancy</subject><subject>prostaglandin</subject><subject>Prostaglandins - physiology</subject><subject>syncytiotrophoblast</subject><subject>Tissue Inhibitor of Metalloproteinase-1 - secretion</subject><subject>trophoblast</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1uGyEUhVHVqnHSPkJbNu1uUn4MjJeVlTSRbNVqkjW6MzA2FQMuzMjKG_Sxy2gsZRsJhC5893B0LkKfKLmmZCW-Ny76ZI8pmlLLayIU4cs3aEEFW1WKyfotWhBCZMW55BfoMuc_hNAlZ_w9uqCKymkt0L_Hg8W_o7c4dniXYh5g7yEYFzJ2AQ_ldWvbAwSX-wnZuGM8Rv-coS23yRlb3Qczttbg4mW73a3wg22THVwMuEuxx3djDwHvPLQ2DICLNr61A_ii2zcJgsVr633-gN514LP9eD6v0NPtzeP6rtr8-nm__rGpGkHroVKmE0sBUEvaCsOEEgqYZIy2HbeGkobVYCTramikIoqXbVQtDBhSg6KKX6Fvs26x-3e0edC9y21xUJzEMesSI1kRtiqgmMG2pJKT7fQxuR7Ss6ZETyPQLyMotdTzCErf5_MHY9Nb89J1zrwAX2fg4PaHk0tW5x68LzjXp9NJSb3UUkxCX2aug6hhn1zWTw-MUE6IkoTUk0U-E8VJDPaVBv8DrMetaA</recordid><startdate>20070401</startdate><enddate>20070401</enddate><creator>Li, Wei</creator><creator>Unlugedik, Elif</creator><creator>Bocking, Alan D</creator><creator>Challis, John R. G</creator><general>Society for the Study of Reproduction, Inc</general><general>Society for the Study of Reproduction</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20070401</creationdate><title>The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells</title><author>Li, Wei ; Unlugedik, Elif ; Bocking, Alan D ; Challis, John R. G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b518t-7df545aa861c5d25757a26221cf3ed10b28ad62f8ab67073707d785dad08a7173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Cells, Cultured</topic><topic>Cyclooxygenase 2 - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Enzyme Precursors - secretion</topic><topic>Extraembryonic Membranes - drug effects</topic><topic>Extraembryonic Membranes - metabolism</topic><topic>Extraembryonic Membranes - secretion</topic><topic>Female</topic><topic>human fetal membrane</topic><topic>Humans</topic><topic>lipopolysaccharide</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>matrix metalloproteinase</topic><topic>Matrix Metalloproteinase 9 - secretion</topic><topic>mechanisms of hormone action</topic><topic>Membrane Proteins - antagonists & inhibitors</topic><topic>Membrane Proteins - metabolism</topic><topic>Placenta - drug effects</topic><topic>Placenta - metabolism</topic><topic>Placenta - secretion</topic><topic>Pregnancy</topic><topic>prostaglandin</topic><topic>Prostaglandins - physiology</topic><topic>syncytiotrophoblast</topic><topic>Tissue Inhibitor of Metalloproteinase-1 - secretion</topic><topic>trophoblast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Unlugedik, Elif</creatorcontrib><creatorcontrib>Bocking, Alan D</creatorcontrib><creatorcontrib>Challis, John R. G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Wei</au><au>Unlugedik, Elif</au><au>Bocking, Alan D</au><au>Challis, John R. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2007-04-01</date><risdate>2007</risdate><volume>76</volume><issue>4</issue><spage>654</spage><epage>659</epage><pages>654-659</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><abstract>The abnormal degradation of the extracellular matrix by matrix metalloproteinases (MMPs) in the fetal membranes has been proposed as a central event in preterm premature rupture of the membranes (pPROM). Prostaglandins (PGs) are thought to increase the risk of preterm premature rupture of the fetal membranes by causing matrix degradation. The aim of this study was to assess the mediating role of PGs on lipopolysaccharide (LPS)-induced MMP9 secretion in vitro. ELISA, zymography, and Western blotting were performed on cells and medium from cultures of purified chorion trophoblasts (CTs) and syncytiotrophoblasts (STs) from the human placenta and fetal membranes treated with LPS, meloxicam, (a selective prostaglandin-endoperoxide synthase 2 [PTGS2, previously known as cyclooxygenase 2] inhibitor), or replacement PGE2 or PGF2alpha. LPS significantly (P < 0.01) increased proMMP9 secretion and prostaglandin E2 (PGE2) output by cultured CTs and STs, but there was no effect on tissue inhibitor of matrix metalloproteinase 1 (TIMP1) secretion. In these cells, meloxicam significantly blocked LPS-induced proMMP9 secretion and PGE2 output (P < 0.01). Exogenous PGE2 and PGF2alpha significantly reversed the reduction in proMMP9 secretion caused by meloxicam in a dose-dependent manner (P < 0.01). The expression of PTGS2 protein in CTs and STs was increased dramatically after LPS treatment, but there was no significant effect on the expression of PTGS1 (previously known as cyclooxygenase 1), membrane-associated prostaglandin E synthases (membrane-associated PTGES, previously known as mPGES) 1 and 2, or cytosolic prostaglandin E synthase (cytosolic PTGES, previously knows as cPGES) proteins. Our results suggest that PGs may mediate the selective increase in MMP9 after exposure of trophoblast cells to LPS. There was no effect of LPS on TIMP1. Understanding this relationship may help in developing strategies for the prevention and management of pPROM and preterm labor.</abstract><cop>United States</cop><pub>Society for the Study of Reproduction, Inc</pub><pmid>17167167</pmid><doi>10.1095/biolreprod.106.057034</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; BioOne Complete |
| subjects | Cells, Cultured Cyclooxygenase 2 - metabolism Dose-Response Relationship, Drug Enzyme Precursors - secretion Extraembryonic Membranes - drug effects Extraembryonic Membranes - metabolism Extraembryonic Membranes - secretion Female human fetal membrane Humans lipopolysaccharide Lipopolysaccharides - pharmacology matrix metalloproteinase Matrix Metalloproteinase 9 - secretion mechanisms of hormone action Membrane Proteins - antagonists & inhibitors Membrane Proteins - metabolism Placenta - drug effects Placenta - metabolism Placenta - secretion Pregnancy prostaglandin Prostaglandins - physiology syncytiotrophoblast Tissue Inhibitor of Metalloproteinase-1 - secretion trophoblast |
| title | The Role of Prostaglandins in the Mechanism of Lipopolysaccharide-Induced proMMP9 Secretion from Human Placenta and Fetal Membrane Cells |
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