Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells

Autores
Ronda, Ana Carolina; Buitrago, Claudia Graciela; Boland, Ricardo Leopoldo
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We have previously reported in C2C12 murine skeletal muscle cells that 10-8M 17β-estradiol promotes MAPKs stimulation which in turn mediates the activation of CREB and Elk-1 transcription factors. In this work, we demonstrated that the hormone induces ERK2 phosphorylation (without affecting ERK1 activation) and also stimulates p38 MAPK, both in a dose-dependent manner. Moreover, estrogen receptors involvement in MAPKs activation by the estrogen was studied. The use of ICI182780 (1μM), an antagonist of ERs, and specific siRNAs to block ERα and ERβ expression, demonstrated that ERα mediates ERK2 activation but not p38 MAPK phosphorylation by 17β-estradiol, and that ERβ isoform is not implicated in MAPKs activation by the hormone. Furthermore, Src and PKC contribution in estrogen stimulation of the MAPKs was investigated. Compounds PP2 and Ro318220, Src and PKC family inhibitors, respectively abrogated ERK2 and p38 MAPK phosphorylation by 17β-estradiol. Of interest, the hormone was able to induce Src and PKCδ activation. In addition, Ro318220 decreased estrogen-dependent Src modulation implicating PKC in hormone upregulation of Src. Accordingly, PP2 and Ro318220 suppressed CREB and Elk-1 phosphorylation as well as c-Fos and c-Jun oncoprotein levels induced by 17β-estradiol. Altogether, these data indicate that 17β-estradiol activates ERK2 through ERα and p38 MAPK in an ERα/β-independent manner and that PKC and Src proteins are key upstream components on MAPKs activation in C2C12 skeletal muscle cells. © 2010 Elsevier Ltd.
Fil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Buitrago, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; Argentina
Fil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; Argentina
Materia
C2c12 Muscle Cells
Ers
Estrogen
Mapks
Proto-Oncogene Expression
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:11336/62082
Acceder
id CONICETDig_f52a8415d7cb44cd135d4b4b3a7fbad2
oai_identifier_str oai:ri.conicet.gov.ar:11336/62082
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cellsRonda, Ana CarolinaBuitrago, Claudia GracielaBoland, Ricardo LeopoldoC2c12 Muscle CellsErsEstrogenMapksProto-Oncogene Expressionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We have previously reported in C2C12 murine skeletal muscle cells that 10-8M 17β-estradiol promotes MAPKs stimulation which in turn mediates the activation of CREB and Elk-1 transcription factors. In this work, we demonstrated that the hormone induces ERK2 phosphorylation (without affecting ERK1 activation) and also stimulates p38 MAPK, both in a dose-dependent manner. Moreover, estrogen receptors involvement in MAPKs activation by the estrogen was studied. The use of ICI182780 (1μM), an antagonist of ERs, and specific siRNAs to block ERα and ERβ expression, demonstrated that ERα mediates ERK2 activation but not p38 MAPK phosphorylation by 17β-estradiol, and that ERβ isoform is not implicated in MAPKs activation by the hormone. Furthermore, Src and PKC contribution in estrogen stimulation of the MAPKs was investigated. Compounds PP2 and Ro318220, Src and PKC family inhibitors, respectively abrogated ERK2 and p38 MAPK phosphorylation by 17β-estradiol. Of interest, the hormone was able to induce Src and PKCδ activation. In addition, Ro318220 decreased estrogen-dependent Src modulation implicating PKC in hormone upregulation of Src. Accordingly, PP2 and Ro318220 suppressed CREB and Elk-1 phosphorylation as well as c-Fos and c-Jun oncoprotein levels induced by 17β-estradiol. Altogether, these data indicate that 17β-estradiol activates ERK2 through ERα and p38 MAPK in an ERα/β-independent manner and that PKC and Src proteins are key upstream components on MAPKs activation in C2C12 skeletal muscle cells. © 2010 Elsevier Ltd.Fil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; ArgentinaFil: Buitrago, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; ArgentinaFil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; ArgentinaPergamon-Elsevier Science Ltd2010-10info: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/11336/62082Ronda, Ana Carolina; Buitrago, Claudia Graciela; Boland, Ricardo Leopoldo; Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells; Pergamon-Elsevier Science Ltd; Journal of Steroid Biochemistry and Molecular Biology; 122; 4; 10-2010; 287-2940960-0760CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jsbmb.2010.05.002info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0960076010002347info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:07:44Zoai:ri.conicet.gov.ar:11336/62082instacron: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:34982025-10-15 15:07:44.484CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
title Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
spellingShingle Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
Ronda, Ana Carolina
C2c12 Muscle Cells
Ers
Estrogen
Mapks
Proto-Oncogene Expression
title_short Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
title_full Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
title_fullStr Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
title_full_unstemmed Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
title_sort Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells
dc.creator.none.fl_str_mv Ronda, Ana Carolina
Buitrago, Claudia Graciela
Boland, Ricardo Leopoldo
author Ronda, Ana Carolina
author_facet Ronda, Ana Carolina
Buitrago, Claudia Graciela
Boland, Ricardo Leopoldo
author_role author
author2 Buitrago, Claudia Graciela
Boland, Ricardo Leopoldo
author2_role author
author
dc.subject.none.fl_str_mv C2c12 Muscle Cells
Ers
Estrogen
Mapks
Proto-Oncogene Expression
topic C2c12 Muscle Cells
Ers
Estrogen
Mapks
Proto-Oncogene Expression
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We have previously reported in C2C12 murine skeletal muscle cells that 10-8M 17β-estradiol promotes MAPKs stimulation which in turn mediates the activation of CREB and Elk-1 transcription factors. In this work, we demonstrated that the hormone induces ERK2 phosphorylation (without affecting ERK1 activation) and also stimulates p38 MAPK, both in a dose-dependent manner. Moreover, estrogen receptors involvement in MAPKs activation by the estrogen was studied. The use of ICI182780 (1μM), an antagonist of ERs, and specific siRNAs to block ERα and ERβ expression, demonstrated that ERα mediates ERK2 activation but not p38 MAPK phosphorylation by 17β-estradiol, and that ERβ isoform is not implicated in MAPKs activation by the hormone. Furthermore, Src and PKC contribution in estrogen stimulation of the MAPKs was investigated. Compounds PP2 and Ro318220, Src and PKC family inhibitors, respectively abrogated ERK2 and p38 MAPK phosphorylation by 17β-estradiol. Of interest, the hormone was able to induce Src and PKCδ activation. In addition, Ro318220 decreased estrogen-dependent Src modulation implicating PKC in hormone upregulation of Src. Accordingly, PP2 and Ro318220 suppressed CREB and Elk-1 phosphorylation as well as c-Fos and c-Jun oncoprotein levels induced by 17β-estradiol. Altogether, these data indicate that 17β-estradiol activates ERK2 through ERα and p38 MAPK in an ERα/β-independent manner and that PKC and Src proteins are key upstream components on MAPKs activation in C2C12 skeletal muscle cells. © 2010 Elsevier Ltd.
Fil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Buitrago, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; Argentina
Fil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Ciencias Biológicas y Biomédicas del Sur. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia. Instituto de Ciencias Biológicas y Biomédicas del Sur; Argentina
description We have previously reported in C2C12 murine skeletal muscle cells that 10-8M 17β-estradiol promotes MAPKs stimulation which in turn mediates the activation of CREB and Elk-1 transcription factors. In this work, we demonstrated that the hormone induces ERK2 phosphorylation (without affecting ERK1 activation) and also stimulates p38 MAPK, both in a dose-dependent manner. Moreover, estrogen receptors involvement in MAPKs activation by the estrogen was studied. The use of ICI182780 (1μM), an antagonist of ERs, and specific siRNAs to block ERα and ERβ expression, demonstrated that ERα mediates ERK2 activation but not p38 MAPK phosphorylation by 17β-estradiol, and that ERβ isoform is not implicated in MAPKs activation by the hormone. Furthermore, Src and PKC contribution in estrogen stimulation of the MAPKs was investigated. Compounds PP2 and Ro318220, Src and PKC family inhibitors, respectively abrogated ERK2 and p38 MAPK phosphorylation by 17β-estradiol. Of interest, the hormone was able to induce Src and PKCδ activation. In addition, Ro318220 decreased estrogen-dependent Src modulation implicating PKC in hormone upregulation of Src. Accordingly, PP2 and Ro318220 suppressed CREB and Elk-1 phosphorylation as well as c-Fos and c-Jun oncoprotein levels induced by 17β-estradiol. Altogether, these data indicate that 17β-estradiol activates ERK2 through ERα and p38 MAPK in an ERα/β-independent manner and that PKC and Src proteins are key upstream components on MAPKs activation in C2C12 skeletal muscle cells. © 2010 Elsevier Ltd.
publishDate 2010
dc.date.none.fl_str_mv 2010-10
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/11336/62082
Ronda, Ana Carolina; Buitrago, Claudia Graciela; Boland, Ricardo Leopoldo; Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells; Pergamon-Elsevier Science Ltd; Journal of Steroid Biochemistry and Molecular Biology; 122; 4; 10-2010; 287-294
0960-0760
CONICET Digital
CONICET
url http://hdl.handle.net/11336/62082
identifier_str_mv Ronda, Ana Carolina; Buitrago, Claudia Graciela; Boland, Ricardo Leopoldo; Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells; Pergamon-Elsevier Science Ltd; Journal of Steroid Biochemistry and Molecular Biology; 122; 4; 10-2010; 287-294
0960-0760
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jsbmb.2010.05.002
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0960076010002347
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 Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
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 13.22299

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