MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells

Autores
Pérez-Pérez, Antonio; Gambino, Yésica Paola; Maymo, Julieta Lorena; Goberna, Raimundo; Fabiani, Fernando; Varone, Cecilia Laura; Sánchez Margalet, Víctor
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Leptin, the LEP gene product, is produced in placenta where it has been found to be an important autocrine signal for trophoblastic growth during pregnancy. Thus, we have recently described the antiapoptotic and trophic effect of leptin on choriocarcinoma cell line JEG-3, stimulating DNA and protein synthesis. We have also demonstrated the presence of leptin receptor and leptin signaling in normal human trophoblastic cells, activating JAK-STAT, PI3K and MAPK pathways. In the present work we have employed dominant negative forms of MAPK and PKB constructs to find out the signaling pathways that specifically mediates the effect of leptin on protein synthesis. As previously shown, leptin stimulates protein synthesis as assessed by 3H-leucine incorporation. However, both dominant negative forms of MAPK and PKB inhibited protein synthesis in JEG-3 choriocarcinoma cells. The inhibition of PKB and MAPK activity by transfection with the dominant negative kinases prevented the leptin stimulation of p70 S6K, which is known to be an important kinase in the regulation of protein synthesis. Moreover, leptin stimulation of phosphorylation of EIF4EBP1 and EIF4E, which allows the initiation of translation was also prevented by MAPK and PI3K dominant negative constructs. Therefore, these results demonstrate that both PI3K and MAPK are necessary to observe the effect of leptin signaling that mediates protein synthesis in choriocarcinoma cells JEG-3. © 2010 Elsevier Inc. All rights reserved.
Fil: Pérez-Pérez, Antonio. Universidad de Sevilla; España
Fil: Gambino, Yésica Paola. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Maymo, Julieta Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Goberna, Raimundo. Universidad de Sevilla; España
Fil: Fabiani, Fernando. Universidad de Sevilla; España
Fil: Varone, Cecilia Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Sánchez Margalet, Víctor. Universidad de Sevilla; España
Materia
Leptin
Placenta
Protein Synthesis
Signal Transduction
Translation
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:11336/66369
Acceder
id CONICETDig_b9e0ab3d400289ef31f9db650683a682
oai_identifier_str oai:ri.conicet.gov.ar:11336/66369
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cellsPérez-Pérez, AntonioGambino, Yésica PaolaMaymo, Julieta LorenaGoberna, RaimundoFabiani, FernandoVarone, Cecilia LauraSánchez Margalet, VíctorLeptinPlacentaProtein SynthesisSignal TransductionTranslationhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Leptin, the LEP gene product, is produced in placenta where it has been found to be an important autocrine signal for trophoblastic growth during pregnancy. Thus, we have recently described the antiapoptotic and trophic effect of leptin on choriocarcinoma cell line JEG-3, stimulating DNA and protein synthesis. We have also demonstrated the presence of leptin receptor and leptin signaling in normal human trophoblastic cells, activating JAK-STAT, PI3K and MAPK pathways. In the present work we have employed dominant negative forms of MAPK and PKB constructs to find out the signaling pathways that specifically mediates the effect of leptin on protein synthesis. As previously shown, leptin stimulates protein synthesis as assessed by 3H-leucine incorporation. However, both dominant negative forms of MAPK and PKB inhibited protein synthesis in JEG-3 choriocarcinoma cells. The inhibition of PKB and MAPK activity by transfection with the dominant negative kinases prevented the leptin stimulation of p70 S6K, which is known to be an important kinase in the regulation of protein synthesis. Moreover, leptin stimulation of phosphorylation of EIF4EBP1 and EIF4E, which allows the initiation of translation was also prevented by MAPK and PI3K dominant negative constructs. Therefore, these results demonstrate that both PI3K and MAPK are necessary to observe the effect of leptin signaling that mediates protein synthesis in choriocarcinoma cells JEG-3. © 2010 Elsevier Inc. All rights reserved.Fil: Pérez-Pérez, Antonio. Universidad de Sevilla; EspañaFil: Gambino, Yésica Paola. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Maymo, Julieta Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Goberna, Raimundo. Universidad de Sevilla; EspañaFil: Fabiani, Fernando. Universidad de Sevilla; EspañaFil: Varone, Cecilia Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Sánchez Margalet, Víctor. Universidad de Sevilla; EspañaAcademic Press Inc Elsevier Science2010-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66369Pérez-Pérez, Antonio; Gambino, Yésica Paola; Maymo, Julieta Lorena; Goberna, Raimundo; Fabiani, Fernando; et al.; MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 396; 4; 6-2010; 956-9600006-291XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2010.05.031info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006291X10009228info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-05T10:16:28Zoai:ri.conicet.gov.ar:11336/66369instacron: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:34982025-11-05 10:16:28.319CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
title MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
spellingShingle MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
Pérez-Pérez, Antonio
Leptin
Placenta
Protein Synthesis
Signal Transduction
Translation
title_short MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
title_full MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
title_fullStr MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
title_full_unstemmed MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
title_sort MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells
dc.creator.none.fl_str_mv Pérez-Pérez, Antonio
Gambino, Yésica Paola
Maymo, Julieta Lorena
Goberna, Raimundo
Fabiani, Fernando
Varone, Cecilia Laura
Sánchez Margalet, Víctor
author Pérez-Pérez, Antonio
author_facet Pérez-Pérez, Antonio
Gambino, Yésica Paola
Maymo, Julieta Lorena
Goberna, Raimundo
Fabiani, Fernando
Varone, Cecilia Laura
Sánchez Margalet, Víctor
author_role author
author2 Gambino, Yésica Paola
Maymo, Julieta Lorena
Goberna, Raimundo
Fabiani, Fernando
Varone, Cecilia Laura
Sánchez Margalet, Víctor
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Leptin
Placenta
Protein Synthesis
Signal Transduction
Translation
topic Leptin
Placenta
Protein Synthesis
Signal Transduction
Translation
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Leptin, the LEP gene product, is produced in placenta where it has been found to be an important autocrine signal for trophoblastic growth during pregnancy. Thus, we have recently described the antiapoptotic and trophic effect of leptin on choriocarcinoma cell line JEG-3, stimulating DNA and protein synthesis. We have also demonstrated the presence of leptin receptor and leptin signaling in normal human trophoblastic cells, activating JAK-STAT, PI3K and MAPK pathways. In the present work we have employed dominant negative forms of MAPK and PKB constructs to find out the signaling pathways that specifically mediates the effect of leptin on protein synthesis. As previously shown, leptin stimulates protein synthesis as assessed by 3H-leucine incorporation. However, both dominant negative forms of MAPK and PKB inhibited protein synthesis in JEG-3 choriocarcinoma cells. The inhibition of PKB and MAPK activity by transfection with the dominant negative kinases prevented the leptin stimulation of p70 S6K, which is known to be an important kinase in the regulation of protein synthesis. Moreover, leptin stimulation of phosphorylation of EIF4EBP1 and EIF4E, which allows the initiation of translation was also prevented by MAPK and PI3K dominant negative constructs. Therefore, these results demonstrate that both PI3K and MAPK are necessary to observe the effect of leptin signaling that mediates protein synthesis in choriocarcinoma cells JEG-3. © 2010 Elsevier Inc. All rights reserved.
Fil: Pérez-Pérez, Antonio. Universidad de Sevilla; España
Fil: Gambino, Yésica Paola. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Maymo, Julieta Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Goberna, Raimundo. Universidad de Sevilla; España
Fil: Fabiani, Fernando. Universidad de Sevilla; España
Fil: Varone, Cecilia Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Sánchez Margalet, Víctor. Universidad de Sevilla; España
description Leptin, the LEP gene product, is produced in placenta where it has been found to be an important autocrine signal for trophoblastic growth during pregnancy. Thus, we have recently described the antiapoptotic and trophic effect of leptin on choriocarcinoma cell line JEG-3, stimulating DNA and protein synthesis. We have also demonstrated the presence of leptin receptor and leptin signaling in normal human trophoblastic cells, activating JAK-STAT, PI3K and MAPK pathways. In the present work we have employed dominant negative forms of MAPK and PKB constructs to find out the signaling pathways that specifically mediates the effect of leptin on protein synthesis. As previously shown, leptin stimulates protein synthesis as assessed by 3H-leucine incorporation. However, both dominant negative forms of MAPK and PKB inhibited protein synthesis in JEG-3 choriocarcinoma cells. The inhibition of PKB and MAPK activity by transfection with the dominant negative kinases prevented the leptin stimulation of p70 S6K, which is known to be an important kinase in the regulation of protein synthesis. Moreover, leptin stimulation of phosphorylation of EIF4EBP1 and EIF4E, which allows the initiation of translation was also prevented by MAPK and PI3K dominant negative constructs. Therefore, these results demonstrate that both PI3K and MAPK are necessary to observe the effect of leptin signaling that mediates protein synthesis in choriocarcinoma cells JEG-3. © 2010 Elsevier Inc. All rights reserved.
publishDate 2010
dc.date.none.fl_str_mv 2010-06
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/11336/66369
Pérez-Pérez, Antonio; Gambino, Yésica Paola; Maymo, Julieta Lorena; Goberna, Raimundo; Fabiani, Fernando; et al.; MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 396; 4; 6-2010; 956-960
0006-291X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/66369
identifier_str_mv Pérez-Pérez, Antonio; Gambino, Yésica Paola; Maymo, Julieta Lorena; Goberna, Raimundo; Fabiani, Fernando; et al.; MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 396; 4; 6-2010; 956-960
0006-291X
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.bbrc.2010.05.031
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006291X10009228
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
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
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_ 1847977732228513792
score 13.087074

Publicaciones similares