Matrix metalloproteinases -2 and -9 and their endogenous tissue inhibitors in fetal membrane repair following fetoscopy in a rabbit model
Identifieur interne : 001B68 ( Main/Exploration ); précédent : 001B67; suivant : 001B69Matrix metalloproteinases -2 and -9 and their endogenous tissue inhibitors in fetal membrane repair following fetoscopy in a rabbit model
Auteurs : Roland Devlieger ; Jan A. Deprest ; Eduard Grataco S ; Robert Pijnenborg ; Rosemary Leask [Royaume-Uni] ; Simon C. Riley [Royaume-Uni]Source :
- Molecular Human Reproduction [ 1360-9947 ] ; 2000-05.
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Abstract
The cellular mechanisms underlying fetal membrane repair are poorly understood. Matrix metalloproteinases (MMP) and the endogenous tissue inhibitors of metalloproteinases (TIMP) play a key role in the control of turnover of extracellular matrix in fetal membranes at normal parturition and preterm prelabour rupture of the fetal membranes (PPROM). The time course of secretion of MMP-2 (72 kDa, gelatinase A) and MMP-9 (92 kDa, gelatinase B) and TIMP into extra-embryonic coelomic, allantoic and amniotic fluids in a rabbit model was examined. Furthermore, to evaluate their role in fetal membrane repair, the changes induced by fetoscopy at mid-gestation (23 days; gestation length is 32 days) were investigated. Zymography showed predominantly secretion of latent MMP-2 at 18, 23 and 30 days of gestation in all gestational compartments. Reverse zymography detected a broad range of TIMP activity with molecular weights of 27–30 kDa (TIMP-1, glycosylated TIMP-3 and TIMP-4), 24 kDa (unglycosylated TIMP-3) and 21 kDa (TIMP-2). Following fetoscopy, both MMP-2 and TIMP increased significantly in amniotic fluid and extra-embryonic coelomic fluid, but not in allantoic fluid, as demonstrated by densitometric analyses. These findings indicate a modulating role for MMP and TIMP in the repair processes following a surgically induced fetal membrane defect.
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DOI: 10.1093/molehr/6.5.479
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Deprest</name></author><author><name sortKey="Grataco S, Eduard" sort="Grataco S, Eduard" uniqKey="Grataco S E" first="Eduard" last="Grataco S">Eduard Grataco S</name></author><author><name sortKey="Pijnenborg, Robert" sort="Pijnenborg, Robert" uniqKey="Pijnenborg R" first="Robert" last="Pijnenborg">Robert Pijnenborg</name></author><author><name sortKey="Leask, Rosemary" sort="Leask, Rosemary" uniqKey="Leask R" first="Rosemary" last="Leask">Rosemary Leask</name></author><author><name sortKey="C Riley, Simon" sort="C Riley, Simon" uniqKey="C Riley S" first="Simon" last="C. Riley">Simon C. 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Deprest</name><affiliation></affiliation><affiliation><wicri:noCountry code="no comma">Department of Obstetrics and Gynaecology and</wicri:noCountry></affiliation></author><author><name sortKey="Grataco S, Eduard" sort="Grataco S, Eduard" uniqKey="Grataco S E" first="Eduard" last="Grataco S">Eduard Grataco S</name><affiliation></affiliation><affiliation><wicri:noCountry code="no comma">Department of Obstetrics and Gynaecology and</wicri:noCountry></affiliation></author><author><name sortKey="Pijnenborg, Robert" sort="Pijnenborg, Robert" uniqKey="Pijnenborg R" first="Robert" last="Pijnenborg">Robert Pijnenborg</name><affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Leask, Rosemary" sort="Leask, Rosemary" uniqKey="Leask R" first="Rosemary" last="Leask">Rosemary Leask</name><affiliation wicri:level="4"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Obstetrics and Gynaecology, Centre for Reproductive Biology, University of Edinburgh, 37 Chalmers Street, Edinburgh EH3 9ET</wicri:regionArea><orgName type="university">Université d'Édimbourg</orgName><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName></affiliation></author><author><name sortKey="C Riley, Simon" sort="C Riley, Simon" uniqKey="C Riley S" first="Simon" last="C. 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Reprod.</title><idno type="ISSN">1360-9947</idno><idno type="eISSN">1460-2407</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="2000-05">2000-05</date><biblScope unit="volume">6</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="479">479</biblScope><biblScope unit="page" to="485">485</biblScope></imprint><idno type="ISSN">1360-9947</idno></series><idno type="istex">5FFB73E0549D363A2CC56D50B01FECD62B3A72BF</idno><idno type="DOI">10.1093/molehr/6.5.479</idno><idno type="PII">1460-2407</idno><idno type="local">0060479</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1360-9947</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>TIMP</term><term>fetal membranes</term><term>fetoscopy</term><term>matrix metalloproteinases</term><term>rabbit</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The cellular mechanisms underlying fetal membrane repair are poorly understood. Matrix metalloproteinases (MMP) and the endogenous tissue inhibitors of metalloproteinases (TIMP) play a key role in the control of turnover of extracellular matrix in fetal membranes at normal parturition and preterm prelabour rupture of the fetal membranes (PPROM). The time course of secretion of MMP-2 (72 kDa, gelatinase A) and MMP-9 (92 kDa, gelatinase B) and TIMP into extra-embryonic coelomic, allantoic and amniotic fluids in a rabbit model was examined. Furthermore, to evaluate their role in fetal membrane repair, the changes induced by fetoscopy at mid-gestation (23 days; gestation length is 32 days) were investigated. Zymography showed predominantly secretion of latent MMP-2 at 18, 23 and 30 days of gestation in all gestational compartments. Reverse zymography detected a broad range of TIMP activity with molecular weights of 27–30 kDa (TIMP-1, glycosylated TIMP-3 and TIMP-4), 24 kDa (unglycosylated TIMP-3) and 21 kDa (TIMP-2). Following fetoscopy, both MMP-2 and TIMP increased significantly in amniotic fluid and extra-embryonic coelomic fluid, but not in allantoic fluid, as demonstrated by densitometric analyses. These findings indicate a modulating role for MMP and TIMP in the repair processes following a surgically induced fetal membrane defect.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Écosse</li></region><settlement><li>Édimbourg</li></settlement><orgName><li>Université d'Édimbourg</li></orgName></list><tree><noCountry><name sortKey="A Deprest, Jan" sort="A Deprest, Jan" uniqKey="A Deprest J" first="Jan" last="A. Deprest">Jan A. Deprest</name><name sortKey="Devlieger, Roland" sort="Devlieger, Roland" uniqKey="Devlieger R" first="Roland" last="Devlieger">Roland Devlieger</name><name sortKey="Grataco S, Eduard" sort="Grataco S, Eduard" uniqKey="Grataco S E" first="Eduard" last="Grataco S">Eduard Grataco S</name><name sortKey="Pijnenborg, Robert" sort="Pijnenborg, Robert" uniqKey="Pijnenborg R" first="Robert" last="Pijnenborg">Robert Pijnenborg</name></noCountry><country name="Royaume-Uni"><region name="Écosse"><name sortKey="Leask, Rosemary" sort="Leask, Rosemary" uniqKey="Leask R" first="Rosemary" last="Leask">Rosemary Leask</name></region><name sortKey="C Riley, Simon" sort="C Riley, Simon" uniqKey="C Riley S" first="Simon" last="C. Riley">Simon C. Riley</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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