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Article: Glycodelin-A as a modulator of trophoblast invasion
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TitleGlycodelin-A as a modulator of trophoblast invasion
 
AuthorsLam, KKW1
Chiu, PCN1
Chung, MK1
Lee, CL1
Lee, KF1
Koistinen, R2 2
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
2012 Impact Factor: 4.67
2012 SCImago Journal Rankings: 2.172
 
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
2012 Impact Factor: 4.67
2012 SCImago Journal Rankings: 2.172
 
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
 
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<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>
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<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>
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Author Affiliations
  1. The University of Hong Kong
  2. Helsinki University Central Hospital