Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase

Autores
Sanchez, Angel Matias; Flamini, Marina Ines; Zullino, Sara; Gopal, Santhosh; Genazzani, Andrea Riccardo; Simoncini, Tommaso
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Sex steroids play a key role in cell movement and tissue organization. Cell migration requires the integration of events that induce changes in cell structure such as protrusion, polarization and traction toward the direction of migration. These actions are driven by actin remodeling and are stabilized by the development of adhesion sites to extracellular matrix via transmembrane receptors linked to the actin cytoskeleton. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that facilitates cell migration via the control of the turnover of focal adhesion complexes. In this work, we demonstrated that 17β-estradiol (E2) regulates actin remodeling and cell movement in human umbilical vein endothelial cells through the recruitment of FAK. E2 induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extra-nuclear signaling of estrogen receptor-a (ERa) that interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase and FAK. Phosphorylation of FAK is fundamental for its activation, translocation to the plasmatic membrane and the subsequent formation of focal adhesion complexes. In conclusion, we found that ERα enhances endothelial cell motility through the dynamic control of actin arrangement and the formation of focal adhesion complexes. The identification of these processes broadens the understanding of the actions of estrogens on endothelial cells and could be relevant in physiological or pathological settings.
Fil: Sanchez, Angel Matias. Università degli Studi di Pisa; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Flamini, Marina Ines. Università degli Studi di Pisa; Italia
Fil: Zullino, Sara. Università degli Studi di Pisa; Italia
Fil: Gopal, Santhosh. Università degli Studi di Pisa; Italia
Fil: Genazzani, Andrea Riccardo. Università degli Studi di Pisa; Italia
Fil: Simoncini, Tommaso. Università degli Studi di Pisa; Italia
Materia
Endothelial Cells
Estrogen
Estrogen Receptor
Focal Adhesion Complexes
Focal Adhesion Kinase
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:11336/80343
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/80343
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinaseSanchez, Angel MatiasFlamini, Marina InesZullino, SaraGopal, SanthoshGenazzani, Andrea RiccardoSimoncini, TommasoEndothelial CellsEstrogenEstrogen ReceptorFocal Adhesion ComplexesFocal Adhesion Kinasehttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Sex steroids play a key role in cell movement and tissue organization. Cell migration requires the integration of events that induce changes in cell structure such as protrusion, polarization and traction toward the direction of migration. These actions are driven by actin remodeling and are stabilized by the development of adhesion sites to extracellular matrix via transmembrane receptors linked to the actin cytoskeleton. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that facilitates cell migration via the control of the turnover of focal adhesion complexes. In this work, we demonstrated that 17β-estradiol (E2) regulates actin remodeling and cell movement in human umbilical vein endothelial cells through the recruitment of FAK. E2 induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extra-nuclear signaling of estrogen receptor-a (ERa) that interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase and FAK. Phosphorylation of FAK is fundamental for its activation, translocation to the plasmatic membrane and the subsequent formation of focal adhesion complexes. In conclusion, we found that ERα enhances endothelial cell motility through the dynamic control of actin arrangement and the formation of focal adhesion complexes. The identification of these processes broadens the understanding of the actions of estrogens on endothelial cells and could be relevant in physiological or pathological settings.Fil: Sanchez, Angel Matias. Università degli Studi di Pisa; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Flamini, Marina Ines. Università degli Studi di Pisa; ItaliaFil: Zullino, Sara. Università degli Studi di Pisa; ItaliaFil: Gopal, Santhosh. Università degli Studi di Pisa; ItaliaFil: Genazzani, Andrea Riccardo. Università degli Studi di Pisa; ItaliaFil: Simoncini, Tommaso. Università degli Studi di Pisa; ItaliaOxford University Press2011-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/80343Sanchez, Angel Matias; Flamini, Marina Ines; Zullino, Sara; Gopal, Santhosh; Genazzani, Andrea Riccardo; et al.; Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase; Oxford University Press; Molecular Human Reproduction; 17; 4; 4-2011; 219-2261360-9947CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gaq097info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/molehr/article/17/4/219/992231info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:08:39Zoai:ri.conicet.gov.ar:11336/80343instacron: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:34982025-09-10 13:08:39.365CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
title Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
spellingShingle Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
Sanchez, Angel Matias
Endothelial Cells
Estrogen
Estrogen Receptor
Focal Adhesion Complexes
Focal Adhesion Kinase
title_short Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
title_full Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
title_fullStr Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
title_full_unstemmed Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
title_sort Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase
dc.creator.none.fl_str_mv Sanchez, Angel Matias
Flamini, Marina Ines
Zullino, Sara
Gopal, Santhosh
Genazzani, Andrea Riccardo
Simoncini, Tommaso
author Sanchez, Angel Matias
author_facet Sanchez, Angel Matias
Flamini, Marina Ines
Zullino, Sara
Gopal, Santhosh
Genazzani, Andrea Riccardo
Simoncini, Tommaso
author_role author
author2 Flamini, Marina Ines
Zullino, Sara
Gopal, Santhosh
Genazzani, Andrea Riccardo
Simoncini, Tommaso
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Endothelial Cells
Estrogen
Estrogen Receptor
Focal Adhesion Complexes
Focal Adhesion Kinase
topic Endothelial Cells
Estrogen
Estrogen Receptor
Focal Adhesion Complexes
Focal Adhesion Kinase
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Sex steroids play a key role in cell movement and tissue organization. Cell migration requires the integration of events that induce changes in cell structure such as protrusion, polarization and traction toward the direction of migration. These actions are driven by actin remodeling and are stabilized by the development of adhesion sites to extracellular matrix via transmembrane receptors linked to the actin cytoskeleton. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that facilitates cell migration via the control of the turnover of focal adhesion complexes. In this work, we demonstrated that 17β-estradiol (E2) regulates actin remodeling and cell movement in human umbilical vein endothelial cells through the recruitment of FAK. E2 induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extra-nuclear signaling of estrogen receptor-a (ERa) that interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase and FAK. Phosphorylation of FAK is fundamental for its activation, translocation to the plasmatic membrane and the subsequent formation of focal adhesion complexes. In conclusion, we found that ERα enhances endothelial cell motility through the dynamic control of actin arrangement and the formation of focal adhesion complexes. The identification of these processes broadens the understanding of the actions of estrogens on endothelial cells and could be relevant in physiological or pathological settings.
Fil: Sanchez, Angel Matias. Università degli Studi di Pisa; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Flamini, Marina Ines. Università degli Studi di Pisa; Italia
Fil: Zullino, Sara. Università degli Studi di Pisa; Italia
Fil: Gopal, Santhosh. Università degli Studi di Pisa; Italia
Fil: Genazzani, Andrea Riccardo. Università degli Studi di Pisa; Italia
Fil: Simoncini, Tommaso. Università degli Studi di Pisa; Italia
description Sex steroids play a key role in cell movement and tissue organization. Cell migration requires the integration of events that induce changes in cell structure such as protrusion, polarization and traction toward the direction of migration. These actions are driven by actin remodeling and are stabilized by the development of adhesion sites to extracellular matrix via transmembrane receptors linked to the actin cytoskeleton. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that facilitates cell migration via the control of the turnover of focal adhesion complexes. In this work, we demonstrated that 17β-estradiol (E2) regulates actin remodeling and cell movement in human umbilical vein endothelial cells through the recruitment of FAK. E2 induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extra-nuclear signaling of estrogen receptor-a (ERa) that interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase and FAK. Phosphorylation of FAK is fundamental for its activation, translocation to the plasmatic membrane and the subsequent formation of focal adhesion complexes. In conclusion, we found that ERα enhances endothelial cell motility through the dynamic control of actin arrangement and the formation of focal adhesion complexes. The identification of these processes broadens the understanding of the actions of estrogens on endothelial cells and could be relevant in physiological or pathological settings.
publishDate 2011
dc.date.none.fl_str_mv 2011-04
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/11336/80343
Sanchez, Angel Matias; Flamini, Marina Ines; Zullino, Sara; Gopal, Santhosh; Genazzani, Andrea Riccardo; et al.; Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase; Oxford University Press; Molecular Human Reproduction; 17; 4; 4-2011; 219-226
1360-9947
CONICET Digital
CONICET
url http://hdl.handle.net/11336/80343
identifier_str_mv Sanchez, Angel Matias; Flamini, Marina Ines; Zullino, Sara; Gopal, Santhosh; Genazzani, Andrea Riccardo; et al.; Estrogen receptor-α promotes endothelial cell motility through focal adhesion kinase; Oxford University Press; Molecular Human Reproduction; 17; 4; 4-2011; 219-226
1360-9947
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gaq097
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/molehr/article/17/4/219/992231
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
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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
_version_ 1842980413828497408
score 12.993085

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