92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition

The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid bet...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biology of reproduction 1995-08, Vol.53 (2), p.339-344
Hauptverfasser: H Lei, F Vadillo-Ortega, L G Paavola, J F Strauss, 3rd
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 344
container_issue 2
container_start_page 339
container_title Biology of reproduction
container_volume 53
creator H Lei
F Vadillo-Ortega
L G Paavola
J F Strauss, 3rd
description The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid between Days 18-21 of pregnancy. Matrix metalloproteinase (MMP)-2 was present in amnion on all days, and its activity increased slightly on Day 21. The 92-kDa gelatinase, MMP-9, was not detected on Days 18-20 but appeared by the morning of Day 21. There was a marked increase in MMP-9 mRNA in the amnion on Day 20, preceding the appearance of MMP-9 activity. Western blotting confirmed an increase in MMP-9 protein in amnion on Day 21. MMP-2 and MMP-9 activities were detected in extracts of whole yolk sac placenta, placenta, and amniotic fluid, but there were no striking changes in these gelatinases between Days 18 and 21. However, the capsular regions of the visceral yolk sac placentae, which thin and rupture during labor, did show higher MMP-9 activity on Day 21 than on Days 18 and 20. We suggest that the striking increase in MMP-9 expression in amnion and possibly the capsular region of the visceral yolk sac placenta approximately 12 h prior to delivery is responsible, in part, for the alterations in the structure of these fetal membranes before parturition.
doi_str_mv 10.1095/biolreprod53.2.339
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_77745220</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77745220</sourcerecordid><originalsourceid>FETCH-LOGICAL-h265t-74085739f6c32a70ffb340f8dbec907491e8eeb0c3ced6013021efeff7fc36e63</originalsourceid><addsrcrecordid>eNo9kV1LwzAUhoMoc07_gCDkQkUvOtOcNlkvZX7CwBu9Lml7skXTdiYpc__e4IZX5-J9eHl4DyHnKZumrMjvKtNbh2vXNzlM-RSgOCDjNOdFIrmYHZIxY0wkAAKOyYn3n4ylGXAYkZHMikjkY7IqePL1oOgSrQqmUx7pTauCMz-0xaCs7WN9wL8kKW6p8dR0zVBjEy91KlDVdqbvqGlbbIwKaLd07UzvaOjpWrkwOBMicEqOtLIez_Z3Qj6eHt_nL8ni7fl1fr9IVlzkIZEZm-USCi1q4EoyrSvImJ41FdYFi9opzhArVkNUECwFxlPUqLXUNQgUMCHXu97o_T2gD2VrfI3Wqg77wZdSyiznnEXwYg8OVVQvo3Sr3LbcTxPzy32ufK2sdqqrjf_HQEiIZhG72mErs1xtjMPSt3G2WArlZrPJoeRlfAz8As5XgxI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77745220</pqid></control><display><type>article</type><title>92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>H Lei ; F Vadillo-Ortega ; L G Paavola ; J F Strauss, 3rd</creator><creatorcontrib>H Lei ; F Vadillo-Ortega ; L G Paavola ; J F Strauss, 3rd</creatorcontrib><description>The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid between Days 18-21 of pregnancy. Matrix metalloproteinase (MMP)-2 was present in amnion on all days, and its activity increased slightly on Day 21. The 92-kDa gelatinase, MMP-9, was not detected on Days 18-20 but appeared by the morning of Day 21. There was a marked increase in MMP-9 mRNA in the amnion on Day 20, preceding the appearance of MMP-9 activity. Western blotting confirmed an increase in MMP-9 protein in amnion on Day 21. MMP-2 and MMP-9 activities were detected in extracts of whole yolk sac placenta, placenta, and amniotic fluid, but there were no striking changes in these gelatinases between Days 18 and 21. However, the capsular regions of the visceral yolk sac placentae, which thin and rupture during labor, did show higher MMP-9 activity on Day 21 than on Days 18 and 20. We suggest that the striking increase in MMP-9 expression in amnion and possibly the capsular region of the visceral yolk sac placenta approximately 12 h prior to delivery is responsible, in part, for the alterations in the structure of these fetal membranes before parturition.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod53.2.339</identifier><identifier>PMID: 7492685</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Amnion - enzymology ; Amniotic Fluid - enzymology ; Animals ; Base Sequence ; Biological and medical sciences ; Blotting, Western ; Collagenases - biosynthesis ; Collagenases - genetics ; Embryology: invertebrates and vertebrates. Teratology ; Extracellular Matrix - metabolism ; Female ; Fetal membranes ; Fundamental and applied biological sciences. Psychology ; General aspects. Development. Fetal membranes ; Labor, Obstetric - physiology ; Matrix Metalloproteinase 9 ; Molecular Sequence Data ; Molecular Weight ; Placenta - enzymology ; Pregnancy ; Rats ; Rats, Sprague-Dawley ; RNA, Messenger - analysis ; Time Factors ; Yolk Sac - enzymology</subject><ispartof>Biology of reproduction, 1995-08, Vol.53 (2), p.339-344</ispartof><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27928,27929</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=3673340$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7492685$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>H Lei</creatorcontrib><creatorcontrib>F Vadillo-Ortega</creatorcontrib><creatorcontrib>L G Paavola</creatorcontrib><creatorcontrib>J F Strauss, 3rd</creatorcontrib><title>92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid between Days 18-21 of pregnancy. Matrix metalloproteinase (MMP)-2 was present in amnion on all days, and its activity increased slightly on Day 21. The 92-kDa gelatinase, MMP-9, was not detected on Days 18-20 but appeared by the morning of Day 21. There was a marked increase in MMP-9 mRNA in the amnion on Day 20, preceding the appearance of MMP-9 activity. Western blotting confirmed an increase in MMP-9 protein in amnion on Day 21. MMP-2 and MMP-9 activities were detected in extracts of whole yolk sac placenta, placenta, and amniotic fluid, but there were no striking changes in these gelatinases between Days 18 and 21. However, the capsular regions of the visceral yolk sac placentae, which thin and rupture during labor, did show higher MMP-9 activity on Day 21 than on Days 18 and 20. We suggest that the striking increase in MMP-9 expression in amnion and possibly the capsular region of the visceral yolk sac placenta approximately 12 h prior to delivery is responsible, in part, for the alterations in the structure of these fetal membranes before parturition.</description><subject>Amnion - enzymology</subject><subject>Amniotic Fluid - enzymology</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Collagenases - biosynthesis</subject><subject>Collagenases - genetics</subject><subject>Embryology: invertebrates and vertebrates. Teratology</subject><subject>Extracellular Matrix - metabolism</subject><subject>Female</subject><subject>Fetal membranes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects. Development. Fetal membranes</subject><subject>Labor, Obstetric - physiology</subject><subject>Matrix Metalloproteinase 9</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Placenta - enzymology</subject><subject>Pregnancy</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>RNA, Messenger - analysis</subject><subject>Time Factors</subject><subject>Yolk Sac - enzymology</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kV1LwzAUhoMoc07_gCDkQkUvOtOcNlkvZX7CwBu9Lml7skXTdiYpc__e4IZX5-J9eHl4DyHnKZumrMjvKtNbh2vXNzlM-RSgOCDjNOdFIrmYHZIxY0wkAAKOyYn3n4ylGXAYkZHMikjkY7IqePL1oOgSrQqmUx7pTauCMz-0xaCs7WN9wL8kKW6p8dR0zVBjEy91KlDVdqbvqGlbbIwKaLd07UzvaOjpWrkwOBMicEqOtLIez_Z3Qj6eHt_nL8ni7fl1fr9IVlzkIZEZm-USCi1q4EoyrSvImJ41FdYFi9opzhArVkNUECwFxlPUqLXUNQgUMCHXu97o_T2gD2VrfI3Wqg77wZdSyiznnEXwYg8OVVQvo3Sr3LbcTxPzy32ufK2sdqqrjf_HQEiIZhG72mErs1xtjMPSt3G2WArlZrPJoeRlfAz8As5XgxI</recordid><startdate>19950801</startdate><enddate>19950801</enddate><creator>H Lei</creator><creator>F Vadillo-Ortega</creator><creator>L G Paavola</creator><creator>J F Strauss, 3rd</creator><general>Society for the Study of Reproduction</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19950801</creationdate><title>92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition</title><author>H Lei ; F Vadillo-Ortega ; L G Paavola ; J F Strauss, 3rd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h265t-74085739f6c32a70ffb340f8dbec907491e8eeb0c3ced6013021efeff7fc36e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amnion - enzymology</topic><topic>Amniotic Fluid - enzymology</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Collagenases - biosynthesis</topic><topic>Collagenases - genetics</topic><topic>Embryology: invertebrates and vertebrates. Teratology</topic><topic>Extracellular Matrix - metabolism</topic><topic>Female</topic><topic>Fetal membranes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects. Development. Fetal membranes</topic><topic>Labor, Obstetric - physiology</topic><topic>Matrix Metalloproteinase 9</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Placenta - enzymology</topic><topic>Pregnancy</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>RNA, Messenger - analysis</topic><topic>Time Factors</topic><topic>Yolk Sac - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>H Lei</creatorcontrib><creatorcontrib>F Vadillo-Ortega</creatorcontrib><creatorcontrib>L G Paavola</creatorcontrib><creatorcontrib>J F Strauss, 3rd</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>H Lei</au><au>F Vadillo-Ortega</au><au>L G Paavola</au><au>J F Strauss, 3rd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>1995-08-01</date><risdate>1995</risdate><volume>53</volume><issue>2</issue><spage>339</spage><epage>344</epage><pages>339-344</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>The fetal membranes undergo striking changes in structure before delivery that involve catabolism of the extracellular matrix. To investigate the role of specific enzymes in this process, we examined gelatinase activities in rat amnion, visceral yolk sac placenta, and placenta and amniotic fluid between Days 18-21 of pregnancy. Matrix metalloproteinase (MMP)-2 was present in amnion on all days, and its activity increased slightly on Day 21. The 92-kDa gelatinase, MMP-9, was not detected on Days 18-20 but appeared by the morning of Day 21. There was a marked increase in MMP-9 mRNA in the amnion on Day 20, preceding the appearance of MMP-9 activity. Western blotting confirmed an increase in MMP-9 protein in amnion on Day 21. MMP-2 and MMP-9 activities were detected in extracts of whole yolk sac placenta, placenta, and amniotic fluid, but there were no striking changes in these gelatinases between Days 18 and 21. However, the capsular regions of the visceral yolk sac placentae, which thin and rupture during labor, did show higher MMP-9 activity on Day 21 than on Days 18 and 20. We suggest that the striking increase in MMP-9 expression in amnion and possibly the capsular region of the visceral yolk sac placenta approximately 12 h prior to delivery is responsible, in part, for the alterations in the structure of these fetal membranes before parturition.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>7492685</pmid><doi>10.1095/biolreprod53.2.339</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-3363
ispartof Biology of reproduction, 1995-08, Vol.53 (2), p.339-344
issn 0006-3363
1529-7268
language eng
recordid cdi_proquest_miscellaneous_77745220
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
subjects Amnion - enzymology
Amniotic Fluid - enzymology
Animals
Base Sequence
Biological and medical sciences
Blotting, Western
Collagenases - biosynthesis
Collagenases - genetics
Embryology: invertebrates and vertebrates. Teratology
Extracellular Matrix - metabolism
Female
Fetal membranes
Fundamental and applied biological sciences. Psychology
General aspects. Development. Fetal membranes
Labor, Obstetric - physiology
Matrix Metalloproteinase 9
Molecular Sequence Data
Molecular Weight
Placenta - enzymology
Pregnancy
Rats
Rats, Sprague-Dawley
RNA, Messenger - analysis
Time Factors
Yolk Sac - enzymology
title 92-kDa gelatinase (matrix metalloproteinase-9) is induced in rat amnion immediately prior to parturition
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-17T02%3A33%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=92-kDa%20gelatinase%20(matrix%20metalloproteinase-9)%20is%20induced%20in%20rat%20amnion%20immediately%20prior%20to%20parturition&rft.jtitle=Biology%20of%20reproduction&rft.au=H%20Lei&rft.date=1995-08-01&rft.volume=53&rft.issue=2&rft.spage=339&rft.epage=344&rft.pages=339-344&rft.issn=0006-3363&rft.eissn=1529-7268&rft.coden=BIREBV&rft_id=info:doi/10.1095/biolreprod53.2.339&rft_dat=%3Cproquest_pubme%3E77745220%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77745220&rft_id=info:pmid/7492685&rfr_iscdi=true