File Download
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: Glycodelin-A as a modulator of trophoblast invasion
  • Basic View
  • Metadata View
  • XML View
TitleGlycodelin-A as a modulator of trophoblast invasion
 
AuthorsLam, KKW1
Chiu, PCN1
Chung, MK1
Lee, CL1
Lee, KF1
Koistinen, R2
Koistinen, H2
Seppala, M2
Ho, PC1
Yeung, WSB1
 
KeywordsGlycodelin
Invasion
Matrix metalloproteinase
Trophoblast
Urokinase plasminogen activator
 
Issue Date2009
 
PublisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
 
CitationHuman Reproduction, 2009, v. 24 n. 9, p. 2093-2103 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep205
 
AbstractBACKGROUND: Trophoblast invasion is crucial to placentation. The relationship between decidual glycodelin-A and trophoblast invasion is not known. METHODS: Invasiveness of First trimester extravillous cytotrophoblast-1 (TEV-1) cell line, TEV-1, cells was determined by trans-well invasion assay. The gene expression, protein secretion and activities of the matrix metalloproteinase (MMP)-2 and -9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase (TIMP)-1 and -2 and plasminogen activator inhibitor (PAI-1) of glycodelin-A-treated cells were measured by quantitative PCR, ELISA and gel zymography, respectively. RESULTS: Glycodelin-A bound to TEV-1 cells. At a concentration of 1 μg/ml, glycodelin-A, but not other glycodelin isoforms, suppressed the invasion of TEV-1 cells. The effect was glycosylation-dependent and was associated with reduction (P < 0.05) of MMP2, MMP9 and uPA activities in the conditioned medium from the treated culture. Glycodelin-A treatment suppressed the amount of MMP2 protein in the conditioned medium (P < 0.05) and MMP2 mRNA in the cells (P < 0.05), but did not affect that of MMP9. Glycodelin-A also significantly reduced the expression, secretion and activity of uPA (P < 0.05). The treatment did not affect the expression of TIMP-1, TIMP-2 or PAI-1, cell proliferation or survival of the cells. CONCLUSIONS: Glycodelin-A inhibits the invasion of extravillous cytotrophoblasts mainly by suppressing the activity of MMP2 and MMP9 in a glycosylation-dependent fashion. © The Author 2009. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
 
ISSN0268-1161
2013 Impact Factor: 4.585
 
DOIhttp://dx.doi.org/10.1093/humrep/dep205
 
ISI Accession Number IDWOS:000269001600007
Funding AgencyGrant Number
Research Grant Council of Hong KongHKU7635/08M
Helsinki University Central Hospital Research Fund
Funding Information:

This work is supported in part by the Research Grant Council of Hong Kong (grant HKU7635/08M) and the Helsinki University Central Hospital Research Fund.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLam, KKW
 
dc.contributor.authorChiu, PCN
 
dc.contributor.authorChung, MK
 
dc.contributor.authorLee, CL
 
dc.contributor.authorLee, KF
 
dc.contributor.authorKoistinen, R
 
dc.contributor.authorKoistinen, H
 
dc.contributor.authorSeppala, M
 
dc.contributor.authorHo, PC
 
dc.contributor.authorYeung, WSB
 
dc.date.accessioned2011-06-28T06:14:40Z
 
dc.date.available2011-06-28T06:14:40Z
 
dc.date.issued2009
 
dc.description.abstractBACKGROUND: Trophoblast invasion is crucial to placentation. The relationship between decidual glycodelin-A and trophoblast invasion is not known. METHODS: Invasiveness of First trimester extravillous cytotrophoblast-1 (TEV-1) cell line, TEV-1, cells was determined by trans-well invasion assay. The gene expression, protein secretion and activities of the matrix metalloproteinase (MMP)-2 and -9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase (TIMP)-1 and -2 and plasminogen activator inhibitor (PAI-1) of glycodelin-A-treated cells were measured by quantitative PCR, ELISA and gel zymography, respectively. RESULTS: Glycodelin-A bound to TEV-1 cells. At a concentration of 1 μg/ml, glycodelin-A, but not other glycodelin isoforms, suppressed the invasion of TEV-1 cells. The effect was glycosylation-dependent and was associated with reduction (P < 0.05) of MMP2, MMP9 and uPA activities in the conditioned medium from the treated culture. Glycodelin-A treatment suppressed the amount of MMP2 protein in the conditioned medium (P < 0.05) and MMP2 mRNA in the cells (P < 0.05), but did not affect that of MMP9. Glycodelin-A also significantly reduced the expression, secretion and activity of uPA (P < 0.05). The treatment did not affect the expression of TIMP-1, TIMP-2 or PAI-1, cell proliferation or survival of the cells. CONCLUSIONS: Glycodelin-A inhibits the invasion of extravillous cytotrophoblasts mainly by suppressing the activity of MMP2 and MMP9 in a glycosylation-dependent fashion. © The Author 2009. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationHuman Reproduction, 2009, v. 24 n. 9, p. 2093-2103 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep205
 
dc.identifier.citeulike4869695
 
dc.identifier.doihttp://dx.doi.org/10.1093/humrep/dep205
 
dc.identifier.eissn1460-2350
 
dc.identifier.epage2103
 
dc.identifier.hkuros171467
 
dc.identifier.isiWOS:000269001600007
Funding AgencyGrant Number
Research Grant Council of Hong KongHKU7635/08M
Helsinki University Central Hospital Research Fund
Funding Information:

This work is supported in part by the Research Grant Council of Hong Kong (grant HKU7635/08M) and the Helsinki University Central Hospital Research Fund.

 
dc.identifier.issn0268-1161
2013 Impact Factor: 4.585
 
dc.identifier.issue9
 
dc.identifier.openurl
 
dc.identifier.pmid19520712
 
dc.identifier.scopuseid_2-s2.0-68949203615
 
dc.identifier.spage2093
 
dc.identifier.urihttp://hdl.handle.net/10722/134619
 
dc.identifier.volume24
 
dc.languageeng
 
dc.publisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofHuman Reproduction
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshCell Line
 
dc.subject.meshGlycoproteins - physiology
 
dc.subject.meshPlacentation - drug effects - physiology
 
dc.subject.meshPregnancy Proteins - physiology
 
dc.subject.meshTrophoblasts - metabolism
 
dc.subjectGlycodelin
 
dc.subjectInvasion
 
dc.subjectMatrix metalloproteinase
 
dc.subjectTrophoblast
 
dc.subjectUrokinase plasminogen activator
 
dc.titleGlycodelin-A as a modulator of trophoblast invasion
 
dc.typeArticle
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Lam, KKW</contributor.author>
<contributor.author>Chiu, PCN</contributor.author>
<contributor.author>Chung, MK</contributor.author>
<contributor.author>Lee, CL</contributor.author>
<contributor.author>Lee, KF</contributor.author>
<contributor.author>Koistinen, R</contributor.author>
<contributor.author>Koistinen, H</contributor.author>
<contributor.author>Seppala, M</contributor.author>
<contributor.author>Ho, PC</contributor.author>
<contributor.author>Yeung, WSB</contributor.author>
<date.accessioned>2011-06-28T06:14:40Z</date.accessioned>
<date.available>2011-06-28T06:14:40Z</date.available>
<date.issued>2009</date.issued>
<identifier.citation>Human Reproduction, 2009, v. 24 n. 9, p. 2093-2103</identifier.citation>
<identifier.issn>0268-1161</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/134619</identifier.uri>
<description.abstract>BACKGROUND: Trophoblast invasion is crucial to placentation. The relationship between decidual glycodelin-A and trophoblast invasion is not known. METHODS: Invasiveness of First trimester extravillous cytotrophoblast-1 (TEV-1) cell line, TEV-1, cells was determined by trans-well invasion assay. The gene expression, protein secretion and activities of the matrix metalloproteinase (MMP)-2 and -9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase (TIMP)-1 and -2 and plasminogen activator inhibitor (PAI-1) of glycodelin-A-treated cells were measured by quantitative PCR, ELISA and gel zymography, respectively. RESULTS: Glycodelin-A bound to TEV-1 cells. At a concentration of 1 &#956;g/ml, glycodelin-A, but not other glycodelin isoforms, suppressed the invasion of TEV-1 cells. The effect was glycosylation-dependent and was associated with reduction (P &lt; 0.05) of MMP2, MMP9 and uPA activities in the conditioned medium from the treated culture. Glycodelin-A treatment suppressed the amount of MMP2 protein in the conditioned medium (P &lt; 0.05) and MMP2 mRNA in the cells (P &lt; 0.05), but did not affect that of MMP9. Glycodelin-A also significantly reduced the expression, secretion and activity of uPA (P &lt; 0.05). The treatment did not affect the expression of TIMP-1, TIMP-2 or PAI-1, cell proliferation or survival of the cells. CONCLUSIONS: Glycodelin-A inhibits the invasion of extravillous cytotrophoblasts mainly by suppressing the activity of MMP2 and MMP9 in a glycosylation-dependent fashion. &#169; The Author 2009. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved.</description.abstract>
<language>eng</language>
<publisher>Oxford University Press. The Journal&apos;s web site is located at http://humrep.oxfordjournals.org/</publisher>
<relation.ispartof>Human Reproduction</relation.ispartof>
<subject>Glycodelin</subject>
<subject>Invasion</subject>
<subject>Matrix metalloproteinase</subject>
<subject>Trophoblast</subject>
<subject>Urokinase plasminogen activator</subject>
<subject.mesh>Cell Line</subject.mesh>
<subject.mesh>Glycoproteins - physiology</subject.mesh>
<subject.mesh>Placentation - drug effects - physiology</subject.mesh>
<subject.mesh>Pregnancy Proteins - physiology</subject.mesh>
<subject.mesh>Trophoblasts - metabolism</subject.mesh>
<title>Glycodelin-A as a modulator of trophoblast invasion</title>
<type>Article</type>
<identifier.openurl>http://library.hku.hk:4550/resserv?sid=HKU:IR&amp;issn=0268-1161&amp;volume=24&amp;issue=9&amp;spage=2093&amp;epage=2103&amp;date=2009&amp;atitle=Glycodelin-A+as+a+modulator+of+trophoblast+invasion</identifier.openurl>
<description.nature>link_to_OA_fulltext</description.nature>
<identifier.doi>10.1093/humrep/dep205</identifier.doi>
<identifier.pmid>19520712</identifier.pmid>
<identifier.scopus>eid_2-s2.0-68949203615</identifier.scopus>
<identifier.hkuros>171467</identifier.hkuros>
<relation.references>http://www.scopus.com/mlt/select.url?eid=2-s2.0-68949203615&amp;selection=ref&amp;src=s&amp;origin=recordpage</relation.references>
<identifier.volume>24</identifier.volume>
<identifier.issue>9</identifier.issue>
<identifier.spage>2093</identifier.spage>
<identifier.epage>2103</identifier.epage>
<identifier.eissn>1460-2350</identifier.eissn>
<identifier.isi>WOS:000269001600007</identifier.isi>
<publisher.place>United Kingdom</publisher.place>
<identifier.citeulike>4869695</identifier.citeulike>
<bitstream.url>http://hub.hku.hk/bitstream/10722/134619/2/re01.htm</bitstream.url>
</item>
Author Affiliations
  1. The University of Hong Kong
  2. Helsinki University Central Hospital