File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Glycodelin-A as a modulator of trophoblast invasion

TitleGlycodelin-A as a modulator of trophoblast invasion
Authors
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/
Citation
Human Reproduction, 2009, v. 24 n. 9, p. 2093-2103 How to Cite?
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 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.
Persistent Identifierhttp://hdl.handle.net/10722/134619
ISSN
2013 Impact Factor: 4.585
ISI Accession Number ID
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.

References

 

Author Affiliations
  1. The University of Hong Kong
  2. Helsinki University Central Hospital
DC FieldValueLanguage
dc.contributor.authorLam, KKWen_HK
dc.contributor.authorChiu, PCNen_HK
dc.contributor.authorChung, MKen_HK
dc.contributor.authorLee, CLen_HK
dc.contributor.authorLee, KFen_HK
dc.contributor.authorKoistinen, Ren_HK
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorSeppala, Men_HK
dc.contributor.authorHo, PCen_HK
dc.contributor.authorYeung, WSBen_HK
dc.date.accessioned2011-06-28T06:14:40Z-
dc.date.available2011-06-28T06:14:40Z-
dc.date.issued2009en_HK
dc.identifier.citationHuman Reproduction, 2009, v. 24 n. 9, p. 2093-2103en_HK
dc.identifier.issn0268-1161en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134619-
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.en_HK
dc.languageeng-
dc.publisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/en_HK
dc.relation.ispartofHuman Reproductionen_HK
dc.subjectGlycodelinen_HK
dc.subjectInvasionen_HK
dc.subjectMatrix metalloproteinaseen_HK
dc.subjectTrophoblasten_HK
dc.subjectUrokinase plasminogen activatoren_HK
dc.subject.meshCell Line-
dc.subject.meshGlycoproteins - physiology-
dc.subject.meshPlacentation - drug effects - physiology-
dc.subject.meshPregnancy Proteins - physiology-
dc.subject.meshTrophoblasts - metabolism-
dc.titleGlycodelin-A as a modulator of trophoblast invasionen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0268-1161&volume=24&issue=9&spage=2093&epage=2103&date=2009&atitle=Glycodelin-A+as+a+modulator+of+trophoblast+invasion-
dc.identifier.emailChiu, PCN:pchiucn@hku.hken_HK
dc.identifier.emailLee, KF:ckflee@hku.hken_HK
dc.identifier.emailHo, PC:pcho@hku.hken_HK
dc.identifier.emailYeung, WSB:wsbyeung@hkucc.hku.hken_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.identifier.authorityLee, KF=rp00458en_HK
dc.identifier.authorityHo, PC=rp00325en_HK
dc.identifier.authorityYeung, WSB=rp00331en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1093/humrep/dep205en_HK
dc.identifier.pmid19520712en_HK
dc.identifier.scopuseid_2-s2.0-68949203615en_HK
dc.identifier.hkuros171467-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-68949203615&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume24en_HK
dc.identifier.issue9en_HK
dc.identifier.spage2093en_HK
dc.identifier.epage2103en_HK
dc.identifier.eissn1460-2350-
dc.identifier.isiWOS:000269001600007-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLam, KKW=25637362300en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.scopusauthoridChung, MK=8964203600en_HK
dc.identifier.scopusauthoridLee, CL=9277221100en_HK
dc.identifier.scopusauthoridLee, KF=26643097500en_HK
dc.identifier.scopusauthoridKoistinen, R=7006574669en_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridSeppala, M=35475165300en_HK
dc.identifier.scopusauthoridHo, PC=7402211440en_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.citeulike4869695-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats