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Article: Glycodelin-A protein interacts with Siglec-6 protein to suppress trophoblast invasiveness by down-regulating extracellular signal-regulated kinase (ERK)/c-jun signaling pathway

TitleGlycodelin-A protein interacts with Siglec-6 protein to suppress trophoblast invasiveness by down-regulating extracellular signal-regulated kinase (ERK)/c-jun signaling pathway
Authors
Issue Date2011
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2011, v. 286 n. 43, p. 37118-37127 How to Cite?
AbstractDuring placentation, the cytotrophoblast differentiates into the villous cytotrophoblast and the extravillous cytotrophoblast. The latter invades the decidualized endometrium. Glycodelin-A (GdA) is abundantly synthesized by the decidua but not the trophoblast. Previous data indicate that GdA suppresses the invasion of trophoblast cell lines by down-regulating proteinase expression and activities. This study addresses the signaling pathway involved in the above phenomenon. GdA was found to suppress phosphorylation of ERKs and expression of their downstream effector c-Jun, a component of the transcription factor activator protein-1 (AP-1). The involvement of ERKs and c-Jun in suppressing trophoblast invasion and biosynthesis of proteinases was confirmed by using siRNA knockdown and pharmacological inhibitors. Desialylation reduced binding affinity of Gd A toward and invasion suppressive activities on the trophoblast. Co-immunoprecipitation showed that Siglec-6 on the trophoblast was the binding protein of GdA. The binding of GdA to Siglec-6 was sialic acid-dependent. Treatment with anti-Siglec-6 antibody abolished the invasion suppressive activities of GdA. These results show that GdA interacts with Siglec-6 to suppress trophoblast invasiveness by down-regulating the ERK/c-Jun signaling pathway. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/144615
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Research Grant Council of Hong KongHKU7635/08M
Academy of Finland
Helsinki University Central Hospital
Funding Information:

This work was supported in part by the Research Grant Council of Hong Kong (Grant HKU7635/08M) and by the Academy of Finland and Helsinki University Central Hospital Research Funds.

References

 

DC FieldValueLanguage
dc.contributor.authorLam, KKWen_HK
dc.contributor.authorChiu, PCNen_HK
dc.contributor.authorLee, CLen_HK
dc.contributor.authorPang, RTKen_HK
dc.contributor.authorLeung, CONen_HK
dc.contributor.authorKoistinen, Hen_HK
dc.contributor.authorSeppala, Men_HK
dc.contributor.authorHo, PCen_HK
dc.contributor.authorYeung, WSBen_HK
dc.date.accessioned2012-02-03T06:15:55Z-
dc.date.available2012-02-03T06:15:55Z-
dc.date.issued2011en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2011, v. 286 n. 43, p. 37118-37127en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144615-
dc.description.abstractDuring placentation, the cytotrophoblast differentiates into the villous cytotrophoblast and the extravillous cytotrophoblast. The latter invades the decidualized endometrium. Glycodelin-A (GdA) is abundantly synthesized by the decidua but not the trophoblast. Previous data indicate that GdA suppresses the invasion of trophoblast cell lines by down-regulating proteinase expression and activities. This study addresses the signaling pathway involved in the above phenomenon. GdA was found to suppress phosphorylation of ERKs and expression of their downstream effector c-Jun, a component of the transcription factor activator protein-1 (AP-1). The involvement of ERKs and c-Jun in suppressing trophoblast invasion and biosynthesis of proteinases was confirmed by using siRNA knockdown and pharmacological inhibitors. Desialylation reduced binding affinity of Gd A toward and invasion suppressive activities on the trophoblast. Co-immunoprecipitation showed that Siglec-6 on the trophoblast was the binding protein of GdA. The binding of GdA to Siglec-6 was sialic acid-dependent. Treatment with anti-Siglec-6 antibody abolished the invasion suppressive activities of GdA. These results show that GdA interacts with Siglec-6 to suppress trophoblast invasiveness by down-regulating the ERK/c-Jun signaling pathway. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.subject.meshAntigens, CD - genetics - metabolism-
dc.subject.meshAntigens, Differentiation, Myelomonocytic - genetics - metabolism-
dc.subject.meshEndometrium - cytology - metabolism-
dc.subject.meshExtracellular Signal-Regulated MAP Kinases - genetics - metabolism-
dc.subject.meshGlycoproteins - genetics - metabolism-
dc.titleGlycodelin-A protein interacts with Siglec-6 protein to suppress trophoblast invasiveness by down-regulating extracellular signal-regulated kinase (ERK)/c-jun signaling pathwayen_HK
dc.typeArticleen_HK
dc.identifier.emailChiu, PCN: pchiucn@hku.hken_HK
dc.identifier.emailPang, RTK: rtkpang@hku.hken_HK
dc.identifier.emailHo, PC: pcho@hku.hken_HK
dc.identifier.authorityChiu, PCN=rp00424en_HK
dc.identifier.authorityPang, RTK=rp01761en_HK
dc.identifier.authorityHo, PC=rp00325en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M111.233841en_HK
dc.identifier.pmid21880722-
dc.identifier.pmcidPMC3199459-
dc.identifier.scopuseid_2-s2.0-80054829295en_HK
dc.identifier.hkuros198176en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80054829295&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume286en_HK
dc.identifier.issue43en_HK
dc.identifier.spage37118en_HK
dc.identifier.epage37127en_HK
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000296542400012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLam, KKW=25637362300en_HK
dc.identifier.scopusauthoridChiu, PCN=25959969200en_HK
dc.identifier.scopusauthoridLee, CL=9277221100en_HK
dc.identifier.scopusauthoridPang, RTK=7004376636en_HK
dc.identifier.scopusauthoridLeung, CON=36140510700en_HK
dc.identifier.scopusauthoridKoistinen, H=7003612125en_HK
dc.identifier.scopusauthoridSeppala, M=35475165300en_HK
dc.identifier.scopusauthoridHo, PC=7402211440en_HK
dc.identifier.scopusauthoridYeung, WSB=55763794907en_HK
dc.identifier.citeulike9743705-

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