Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells

Autores
Rattila, Shemona; Kleefeldt, Florian; Ballesteros Gomez, Angela Patricia; Beltrame, Jimena Soledad; Ribeiro, Maria Laura; Ergün, Süleyman; Dveksler, Gabriela
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We previously reported that binding to heparan sulfate (HS) is required for the ability of the placentally secreted pregnancy-specific glycoprotein 1 (PSG1) to induce endothelial tubulogenesis. PSG1 is composed of four immunoglobulin-like domains but which domains of the protein bind to HS remains unknown. To analyze the interaction of PSG1 with HS, we generated several recombinant proteins, including the individual domains, chimeric proteins between two PSG1 domains, and mutants. Using flow cytometric and surface plasmon resonance studies, we determined that the B2 domain of PSG1 binds to HS and that the positively charged amino acids encompassed between amino acids 43-59 are required for this interaction. Furthermore, we showed that the B2 domain of PSG1 is required for the increase in the formation of tubes by endothelial cells (EC) including a human endometrial EC line and two extravillous trophoblast (EVT) cell lines and for the pro-angiogenic activity of PSG1 observed in an aortic ring assay. PSG1 enhanced the migration of ECs while it increased the expression of matrix metalloproteinase-2 in EVTs, indicating that the pro-angiogenic effect of PSG1 on these two cell types may be mediated by different mechanisms. Despite differences in amino acid sequence, we observed that all human PSGs bound to HS proteoglycans and confirmed that at least two other members of the family, PSG6 and PSG9, induce tube formation. These findings contribute to a better understanding of the pro-angiogenic activity of human PSGs and strongly suggest conservation of this function among all PSG family members.
Fil: Rattila, Shemona. Western University Of Health Sciences.; Estados Unidos
Fil: Kleefeldt, Florian. Julius Maximilians Universitat de Wurzburgo; Alemania
Fil: Ballesteros Gomez, Angela Patricia. National Institutes of Health; Estados Unidos
Fil: Beltrame, Jimena Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; Argentina
Fil: Ribeiro, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; Argentina
Fil: Ergün, Süleyman. Julius Maximilians Universitat de Wurzburgo; Alemania
Fil: Dveksler, Gabriela. Western University Of Health Sciences.; Estados Unidos
Materia
FIRST TRIMESTER TROPHOBLAST
VASCULAR REMODELING
PSG
PLACENTATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/132123
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/132123
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cellsRattila, ShemonaKleefeldt, FlorianBallesteros Gomez, Angela PatriciaBeltrame, Jimena SoledadRibeiro, Maria LauraErgün, SüleymanDveksler, GabrielaFIRST TRIMESTER TROPHOBLASTVASCULAR REMODELINGPSGPLACENTATIONhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3We previously reported that binding to heparan sulfate (HS) is required for the ability of the placentally secreted pregnancy-specific glycoprotein 1 (PSG1) to induce endothelial tubulogenesis. PSG1 is composed of four immunoglobulin-like domains but which domains of the protein bind to HS remains unknown. To analyze the interaction of PSG1 with HS, we generated several recombinant proteins, including the individual domains, chimeric proteins between two PSG1 domains, and mutants. Using flow cytometric and surface plasmon resonance studies, we determined that the B2 domain of PSG1 binds to HS and that the positively charged amino acids encompassed between amino acids 43-59 are required for this interaction. Furthermore, we showed that the B2 domain of PSG1 is required for the increase in the formation of tubes by endothelial cells (EC) including a human endometrial EC line and two extravillous trophoblast (EVT) cell lines and for the pro-angiogenic activity of PSG1 observed in an aortic ring assay. PSG1 enhanced the migration of ECs while it increased the expression of matrix metalloproteinase-2 in EVTs, indicating that the pro-angiogenic effect of PSG1 on these two cell types may be mediated by different mechanisms. Despite differences in amino acid sequence, we observed that all human PSGs bound to HS proteoglycans and confirmed that at least two other members of the family, PSG6 and PSG9, induce tube formation. These findings contribute to a better understanding of the pro-angiogenic activity of human PSGs and strongly suggest conservation of this function among all PSG family members.Fil: Rattila, Shemona. Western University Of Health Sciences.; Estados UnidosFil: Kleefeldt, Florian. Julius Maximilians Universitat de Wurzburgo; AlemaniaFil: Ballesteros Gomez, Angela Patricia. National Institutes of Health; Estados UnidosFil: Beltrame, Jimena Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; ArgentinaFil: Ribeiro, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; ArgentinaFil: Ergün, Süleyman. Julius Maximilians Universitat de Wurzburgo; AlemaniaFil: Dveksler, Gabriela. Western University Of Health Sciences.; Estados UnidosBioScientifica2020-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/132123Rattila, Shemona; Kleefeldt, Florian; Ballesteros Gomez, Angela Patricia; Beltrame, Jimena Soledad; Ribeiro, Maria Laura; et al.; Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells; BioScientifica; Reproduction; 160; 5; 11-2020; 737-7501470-1626CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://rep.bioscientifica.com/view/journals/rep/160/5/REP-20-0169.xmlinfo:eu-repo/semantics/altIdentifier/doi/10.1530/REP-20-0169info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:51:48Zoai:ri.conicet.gov.ar:11336/132123instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:51:48.56CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
title Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
spellingShingle Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
Rattila, Shemona
FIRST TRIMESTER TROPHOBLAST
VASCULAR REMODELING
PSG
PLACENTATION
title_short Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
title_full Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
title_fullStr Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
title_full_unstemmed Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
title_sort Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells
dc.creator.none.fl_str_mv Rattila, Shemona
Kleefeldt, Florian
Ballesteros Gomez, Angela Patricia
Beltrame, Jimena Soledad
Ribeiro, Maria Laura
Ergün, Süleyman
Dveksler, Gabriela
author Rattila, Shemona
author_facet Rattila, Shemona
Kleefeldt, Florian
Ballesteros Gomez, Angela Patricia
Beltrame, Jimena Soledad
Ribeiro, Maria Laura
Ergün, Süleyman
Dveksler, Gabriela
author_role author
author2 Kleefeldt, Florian
Ballesteros Gomez, Angela Patricia
Beltrame, Jimena Soledad
Ribeiro, Maria Laura
Ergün, Süleyman
Dveksler, Gabriela
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv FIRST TRIMESTER TROPHOBLAST
VASCULAR REMODELING
PSG
PLACENTATION
topic FIRST TRIMESTER TROPHOBLAST
VASCULAR REMODELING
PSG
PLACENTATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv We previously reported that binding to heparan sulfate (HS) is required for the ability of the placentally secreted pregnancy-specific glycoprotein 1 (PSG1) to induce endothelial tubulogenesis. PSG1 is composed of four immunoglobulin-like domains but which domains of the protein bind to HS remains unknown. To analyze the interaction of PSG1 with HS, we generated several recombinant proteins, including the individual domains, chimeric proteins between two PSG1 domains, and mutants. Using flow cytometric and surface plasmon resonance studies, we determined that the B2 domain of PSG1 binds to HS and that the positively charged amino acids encompassed between amino acids 43-59 are required for this interaction. Furthermore, we showed that the B2 domain of PSG1 is required for the increase in the formation of tubes by endothelial cells (EC) including a human endometrial EC line and two extravillous trophoblast (EVT) cell lines and for the pro-angiogenic activity of PSG1 observed in an aortic ring assay. PSG1 enhanced the migration of ECs while it increased the expression of matrix metalloproteinase-2 in EVTs, indicating that the pro-angiogenic effect of PSG1 on these two cell types may be mediated by different mechanisms. Despite differences in amino acid sequence, we observed that all human PSGs bound to HS proteoglycans and confirmed that at least two other members of the family, PSG6 and PSG9, induce tube formation. These findings contribute to a better understanding of the pro-angiogenic activity of human PSGs and strongly suggest conservation of this function among all PSG family members.
Fil: Rattila, Shemona. Western University Of Health Sciences.; Estados Unidos
Fil: Kleefeldt, Florian. Julius Maximilians Universitat de Wurzburgo; Alemania
Fil: Ballesteros Gomez, Angela Patricia. National Institutes of Health; Estados Unidos
Fil: Beltrame, Jimena Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; Argentina
Fil: Ribeiro, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; Argentina
Fil: Ergün, Süleyman. Julius Maximilians Universitat de Wurzburgo; Alemania
Fil: Dveksler, Gabriela. Western University Of Health Sciences.; Estados Unidos
description We previously reported that binding to heparan sulfate (HS) is required for the ability of the placentally secreted pregnancy-specific glycoprotein 1 (PSG1) to induce endothelial tubulogenesis. PSG1 is composed of four immunoglobulin-like domains but which domains of the protein bind to HS remains unknown. To analyze the interaction of PSG1 with HS, we generated several recombinant proteins, including the individual domains, chimeric proteins between two PSG1 domains, and mutants. Using flow cytometric and surface plasmon resonance studies, we determined that the B2 domain of PSG1 binds to HS and that the positively charged amino acids encompassed between amino acids 43-59 are required for this interaction. Furthermore, we showed that the B2 domain of PSG1 is required for the increase in the formation of tubes by endothelial cells (EC) including a human endometrial EC line and two extravillous trophoblast (EVT) cell lines and for the pro-angiogenic activity of PSG1 observed in an aortic ring assay. PSG1 enhanced the migration of ECs while it increased the expression of matrix metalloproteinase-2 in EVTs, indicating that the pro-angiogenic effect of PSG1 on these two cell types may be mediated by different mechanisms. Despite differences in amino acid sequence, we observed that all human PSGs bound to HS proteoglycans and confirmed that at least two other members of the family, PSG6 and PSG9, induce tube formation. These findings contribute to a better understanding of the pro-angiogenic activity of human PSGs and strongly suggest conservation of this function among all PSG family members.
publishDate 2020
dc.date.none.fl_str_mv 2020-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/132123
Rattila, Shemona; Kleefeldt, Florian; Ballesteros Gomez, Angela Patricia; Beltrame, Jimena Soledad; Ribeiro, Maria Laura; et al.; Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells; BioScientifica; Reproduction; 160; 5; 11-2020; 737-750
1470-1626
CONICET Digital
CONICET
url http://hdl.handle.net/11336/132123
identifier_str_mv Rattila, Shemona; Kleefeldt, Florian; Ballesteros Gomez, Angela Patricia; Beltrame, Jimena Soledad; Ribeiro, Maria Laura; et al.; Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells; BioScientifica; Reproduction; 160; 5; 11-2020; 737-750
1470-1626
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://rep.bioscientifica.com/view/journals/rep/160/5/REP-20-0169.xml
info:eu-repo/semantics/altIdentifier/doi/10.1530/REP-20-0169
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv BioScientifica
publisher.none.fl_str_mv BioScientifica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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