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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/241060
Ver los metadatos del registro completo
id |
CONICETDig_58b3062ada4e498312527f24e5082536 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/241060 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
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 |
_version_ |
1846083151487565824 |
score |
13.22299 |