Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester

Autores
Petiti, Juan Pablo; de Paul, Ana Lucia; Gutiérrez, Silvina; Palmeri, Claudia Mariela; Mukdsi, Jorge Humberto; Torres, Alicia Ines
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of this investigation was to contribute to current knowledge about intracellular mechanisms that are involved in lactotroph cell proliferation, by evaluating the role of PKCe, PKCa and extracellular-signal regulated kinase (ERK) 1/2 in response to phorbol 12-myristate13-acetate (PMA). In primary pituitary cultures, the activation of protein kinase C (PKC) by PMA for 15 min stimulated lactotroph proliferation; whereas a prolonged activation for 3?8 h diminished this proliferative effect. The use of PMA for 15 min activated PKCe and ERK1/2, whereas incubation with PMA for 3 h induced PKCa activation and attenuated the PMA-triggered phosphorylation of ERK1/2. The following inhibitors: PKCs (bisindolylmaleimide I), PKCe (eV1 peptide) and ERK1/2 (PD98059) prevented the mitogenic activity induced by PMA for 15 min. Lactotroph cells stimulated with PMA for 15 min showed a translocation of PKCe to membrane compartment and nucleus. These results thus establish that PKCe plays an essential role in the lactotroph proliferation induced by PMA by triggering signals that involve ERK1/2 activation.
Fil: Petiti, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: de Paul, Ana Lucia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Gutiérrez, Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: Palmeri, Claudia Mariela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Mukdsi, Jorge Humberto. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: Torres, Alicia Ines. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Materia
LACTOTROPH
PKC EPSILON
PKC ALPHA
ERK1/2
PMA
PROLIFERATION
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:11336/241060

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network_name_str CONICET Digital (CONICET)
spelling Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol esterPetiti, Juan Pablode Paul, Ana LuciaGutiérrez, SilvinaPalmeri, Claudia MarielaMukdsi, Jorge HumbertoTorres, Alicia InesLACTOTROPHPKC EPSILONPKC ALPHAERK1/2PMAPROLIFERATIONhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The aim of this investigation was to contribute to current knowledge about intracellular mechanisms that are involved in lactotroph cell proliferation, by evaluating the role of PKCe, PKCa and extracellular-signal regulated kinase (ERK) 1/2 in response to phorbol 12-myristate13-acetate (PMA). In primary pituitary cultures, the activation of protein kinase C (PKC) by PMA for 15 min stimulated lactotroph proliferation; whereas a prolonged activation for 3?8 h diminished this proliferative effect. The use of PMA for 15 min activated PKCe and ERK1/2, whereas incubation with PMA for 3 h induced PKCa activation and attenuated the PMA-triggered phosphorylation of ERK1/2. The following inhibitors: PKCs (bisindolylmaleimide I), PKCe (eV1 peptide) and ERK1/2 (PD98059) prevented the mitogenic activity induced by PMA for 15 min. Lactotroph cells stimulated with PMA for 15 min showed a translocation of PKCe to membrane compartment and nucleus. These results thus establish that PKCe plays an essential role in the lactotroph proliferation induced by PMA by triggering signals that involve ERK1/2 activation.Fil: Petiti, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; ArgentinaFil: de Paul, Ana Lucia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Gutiérrez, Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; ArgentinaFil: Palmeri, Claudia Mariela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Mukdsi, Jorge Humberto. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; ArgentinaFil: Torres, Alicia Ines. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaElsevier Ireland2008-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/241060Petiti, Juan Pablo; de Paul, Ana Lucia; Gutiérrez, Silvina; Palmeri, Claudia Mariela; Mukdsi, Jorge Humberto; et al.; Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester; Elsevier Ireland; Molecular and Cellular Endocrinology; 289; 1-2; 7-2008; 77-840303-7207CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0303720708001548info:eu-repo/semantics/altIdentifier/doi/10.1016/j.mce.2008.04.015info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:01:07Zoai:ri.conicet.gov.ar:11336/241060instacron: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 15:01:07.956CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
title Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
spellingShingle Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
Petiti, Juan Pablo
LACTOTROPH
PKC EPSILON
PKC ALPHA
ERK1/2
PMA
PROLIFERATION
title_short Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
title_full Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
title_fullStr Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
title_full_unstemmed Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
title_sort Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
dc.creator.none.fl_str_mv Petiti, Juan Pablo
de Paul, Ana Lucia
Gutiérrez, Silvina
Palmeri, Claudia Mariela
Mukdsi, Jorge Humberto
Torres, Alicia Ines
author Petiti, Juan Pablo
author_facet Petiti, Juan Pablo
de Paul, Ana Lucia
Gutiérrez, Silvina
Palmeri, Claudia Mariela
Mukdsi, Jorge Humberto
Torres, Alicia Ines
author_role author
author2 de Paul, Ana Lucia
Gutiérrez, Silvina
Palmeri, Claudia Mariela
Mukdsi, Jorge Humberto
Torres, Alicia Ines
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv LACTOTROPH
PKC EPSILON
PKC ALPHA
ERK1/2
PMA
PROLIFERATION
topic LACTOTROPH
PKC EPSILON
PKC ALPHA
ERK1/2
PMA
PROLIFERATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv The aim of this investigation was to contribute to current knowledge about intracellular mechanisms that are involved in lactotroph cell proliferation, by evaluating the role of PKCe, PKCa and extracellular-signal regulated kinase (ERK) 1/2 in response to phorbol 12-myristate13-acetate (PMA). In primary pituitary cultures, the activation of protein kinase C (PKC) by PMA for 15 min stimulated lactotroph proliferation; whereas a prolonged activation for 3?8 h diminished this proliferative effect. The use of PMA for 15 min activated PKCe and ERK1/2, whereas incubation with PMA for 3 h induced PKCa activation and attenuated the PMA-triggered phosphorylation of ERK1/2. The following inhibitors: PKCs (bisindolylmaleimide I), PKCe (eV1 peptide) and ERK1/2 (PD98059) prevented the mitogenic activity induced by PMA for 15 min. Lactotroph cells stimulated with PMA for 15 min showed a translocation of PKCe to membrane compartment and nucleus. These results thus establish that PKCe plays an essential role in the lactotroph proliferation induced by PMA by triggering signals that involve ERK1/2 activation.
Fil: Petiti, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: de Paul, Ana Lucia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Gutiérrez, Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: Palmeri, Claudia Mariela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Mukdsi, Jorge Humberto. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina
Fil: Torres, Alicia Ines. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopía Electrónica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
description The aim of this investigation was to contribute to current knowledge about intracellular mechanisms that are involved in lactotroph cell proliferation, by evaluating the role of PKCe, PKCa and extracellular-signal regulated kinase (ERK) 1/2 in response to phorbol 12-myristate13-acetate (PMA). In primary pituitary cultures, the activation of protein kinase C (PKC) by PMA for 15 min stimulated lactotroph proliferation; whereas a prolonged activation for 3?8 h diminished this proliferative effect. The use of PMA for 15 min activated PKCe and ERK1/2, whereas incubation with PMA for 3 h induced PKCa activation and attenuated the PMA-triggered phosphorylation of ERK1/2. The following inhibitors: PKCs (bisindolylmaleimide I), PKCe (eV1 peptide) and ERK1/2 (PD98059) prevented the mitogenic activity induced by PMA for 15 min. Lactotroph cells stimulated with PMA for 15 min showed a translocation of PKCe to membrane compartment and nucleus. These results thus establish that PKCe plays an essential role in the lactotroph proliferation induced by PMA by triggering signals that involve ERK1/2 activation.
publishDate 2008
dc.date.none.fl_str_mv 2008-07
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/11336/241060
Petiti, Juan Pablo; de Paul, Ana Lucia; Gutiérrez, Silvina; Palmeri, Claudia Mariela; Mukdsi, Jorge Humberto; et al.; Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester; Elsevier Ireland; Molecular and Cellular Endocrinology; 289; 1-2; 7-2008; 77-84
0303-7207
CONICET Digital
CONICET
url http://hdl.handle.net/11336/241060
identifier_str_mv Petiti, Juan Pablo; de Paul, Ana Lucia; Gutiérrez, Silvina; Palmeri, Claudia Mariela; Mukdsi, Jorge Humberto; et al.; Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester; Elsevier Ireland; Molecular and Cellular Endocrinology; 289; 1-2; 7-2008; 77-84
0303-7207
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://www.sciencedirect.com/science/article/pii/S0303720708001548
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.mce.2008.04.015
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
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
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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