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Article: Highly specific monoclonal antibody demonstrates that pregnancy-specific glycoprotein (PSG) is limited to syncytiotrophoblast in human early and term placenta

TitleHighly specific monoclonal antibody demonstrates that pregnancy-specific glycoprotein (PSG) is limited to syncytiotrophoblast in human early and term placenta
Authors
Issue Date1997
PublisherWB Saunders Co Ltd. The Journal's web site is located at http://www.elsevier.com/locate/placenta
Citation
Placenta, 1997, v. 18 n. 7, p. 491-501 How to Cite?
AbstractPregnancy specific glycoproteins (PSG) in humans constitute a family of 11 closely related glycoproteins (PSG1-8, PSG11-13) of unknown function(s), which are produced in large amounts by the placenta. As a step toward understanding the biology of PSG, specific monoclonal antibodies (mAbs) against PSG were developed and used to investigate the ultrastructural localization of PSG in the early and term placenta and in first trimester decidua. One mAb, BAP-3, was found to react with all six individually expressed PSGs representing five alternatively spliced forms, but not with any of the seven expressed members of the carcinoembryonic antigen (CEA) subfamily. The BAP-3 epitope is located in the PSG B2 domain. Using the BAP-3 mAb, PSGs were found to be expressed exclusively by the syncytiotrophoblast of first trimester and term villi. The intensity of the staining was much higher in early than in term placenta. All three main cellular compartments involved in the biosynthesis pathway of secreted proteins, i.e. rough endoplasmic reticulum, the Golgi complex and secretory vesicles, were stained for PSG. A second PSG-reactive mAb, BAP-1, also stained the apical plasma membrane of some glandular epithelial cells in first trimester decidua in addition to syncytiotrophoblast. This staining was most likely due to cross-reactivity with biliary glycoprotein (BGP).
Persistent Identifierhttp://hdl.handle.net/10722/170010
ISSN
2015 Impact Factor: 2.972
2015 SCImago Journal Rankings: 1.608
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, GQen_US
dc.contributor.authorBaranov, Ven_US
dc.contributor.authorZimmermann, Wen_US
dc.contributor.authorGrunert, Fen_US
dc.contributor.authorErhard, Ben_US
dc.contributor.authorMinchevaNilsson, Len_US
dc.contributor.authorHammarström, Sen_US
dc.contributor.authorThompson, Jen_US
dc.date.accessioned2012-10-30T06:04:43Z-
dc.date.available2012-10-30T06:04:43Z-
dc.date.issued1997en_US
dc.identifier.citationPlacenta, 1997, v. 18 n. 7, p. 491-501en_US
dc.identifier.issn0143-4004en_US
dc.identifier.urihttp://hdl.handle.net/10722/170010-
dc.description.abstractPregnancy specific glycoproteins (PSG) in humans constitute a family of 11 closely related glycoproteins (PSG1-8, PSG11-13) of unknown function(s), which are produced in large amounts by the placenta. As a step toward understanding the biology of PSG, specific monoclonal antibodies (mAbs) against PSG were developed and used to investigate the ultrastructural localization of PSG in the early and term placenta and in first trimester decidua. One mAb, BAP-3, was found to react with all six individually expressed PSGs representing five alternatively spliced forms, but not with any of the seven expressed members of the carcinoembryonic antigen (CEA) subfamily. The BAP-3 epitope is located in the PSG B2 domain. Using the BAP-3 mAb, PSGs were found to be expressed exclusively by the syncytiotrophoblast of first trimester and term villi. The intensity of the staining was much higher in early than in term placenta. All three main cellular compartments involved in the biosynthesis pathway of secreted proteins, i.e. rough endoplasmic reticulum, the Golgi complex and secretory vesicles, were stained for PSG. A second PSG-reactive mAb, BAP-1, also stained the apical plasma membrane of some glandular epithelial cells in first trimester decidua in addition to syncytiotrophoblast. This staining was most likely due to cross-reactivity with biliary glycoprotein (BGP).en_US
dc.languageengen_US
dc.publisherWB Saunders Co Ltd. The Journal's web site is located at http://www.elsevier.com/locate/placentaen_US
dc.relation.ispartofPlacentaen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntibodies, Monoclonalen_US
dc.subject.meshAntibody Specificityen_US
dc.subject.meshCho Cellsen_US
dc.subject.meshCricetinaeen_US
dc.subject.meshDecidua - Chemistry - Ultrastructureen_US
dc.subject.meshEpithelium - Chemistryen_US
dc.subject.meshFemaleen_US
dc.subject.meshGlycoproteins - Analysis - Geneticsen_US
dc.subject.meshHumansen_US
dc.subject.meshLabor, Obstetricen_US
dc.subject.meshMicroscopy, Immunoelectronen_US
dc.subject.meshPlacenta - Chemistry - Ultrastructureen_US
dc.subject.meshPregnancyen_US
dc.subject.meshPregnancy Proteins - Analysis - Geneticsen_US
dc.subject.meshPregnancy Trimester, Firsten_US
dc.subject.meshRna, Messenger - Analysisen_US
dc.subject.meshTrophoblasts - Chemistry - Ultrastructureen_US
dc.titleHighly specific monoclonal antibody demonstrates that pregnancy-specific glycoprotein (PSG) is limited to syncytiotrophoblast in human early and term placentaen_US
dc.typeArticleen_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0143-4004(77)90002-9en_US
dc.identifier.pmid9290143-
dc.identifier.scopuseid_2-s2.0-0030762666en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030762666&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume18en_US
dc.identifier.issue7en_US
dc.identifier.spage491en_US
dc.identifier.epage501en_US
dc.identifier.isiWOS:A1997XT99900003-
dc.publisher.placeUnited Kingdomen_US

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