Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line
- Autores
- Buzzi, Natalia Sol; Scodelaro Bilbao, Paola Gabriela; Boland, Ricardo Leopoldo; Russo, Ana Josefa
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Background: ATP exerts diverse effects on various cell types via speci fi c purinergic P2Y receptors. Intracellular signaling cascades are the main routes of communication between P2Y receptors and regulatory targets in the cell. Methods and results: We examined the role of ATP in the modulation of ERK1/2, JNK1/2, and p38 MAP kinases (MAPKs) in human colon cancer Caco-2 cells. Immunoblot analysis showed that ATP induces the phosphorylation of MAPKs in a time- and dose-dependent manner, peaking at 5 min at 10 μM ATP. Moreover, ATP γ S, UTP, and UDP but not ADP or ADP β S increased phosphorylation of MAPKs, indicating the involvement of, at least, P2Y 2 /P2Y 4 and P2Y 6 receptor subtypes. RT – PCR studies and PCR product sequencing supported the expression of P2Y 2 and P2Y 4 receptors in this cell line. Spectro fl uorimetric measurements showed that cell stimulation with ATP induced transient elevations in intracellular calcium concentration. In addition, ATP-induced phosphorylation ofMAPKs in Caco-2 cells was dependent onSrcfamily tyrosinekinases, calcium in fl ux, and intracellular Ca 2+ release and was partially dependent on the cAMP/PKA and PKC pathways and the EGFR. General signi fi cance: These fi ndings provide new molecular basis for further understanding the mechanisms involved in ATP functions, as a signal transducer and activator of MAP kinase cascades, in colon adenocarcinoma Caco-2 cells.
Fil: Buzzi, Natalia Sol. 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: Scodelaro Bilbao, Paola Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Centro de Recursos Naturales Renovables de la Zona Semiárida. Universidad Nacional del Sur. Centro de Recursos Naturales Renovables de la Zona Semiárida; 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
Fil: Russo, Ana Josefa. Universidad Nacional del Sur; Argentina - Materia
-
Atp
Mapks
P2y Receptors
Caco-2 Cells - 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:11336/28383
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Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell lineBuzzi, Natalia SolScodelaro Bilbao, Paola GabrielaBoland, Ricardo LeopoldoRusso, Ana JosefaAtpMapksP2y ReceptorsCaco-2 Cellshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Background: ATP exerts diverse effects on various cell types via speci fi c purinergic P2Y receptors. Intracellular signaling cascades are the main routes of communication between P2Y receptors and regulatory targets in the cell. Methods and results: We examined the role of ATP in the modulation of ERK1/2, JNK1/2, and p38 MAP kinases (MAPKs) in human colon cancer Caco-2 cells. Immunoblot analysis showed that ATP induces the phosphorylation of MAPKs in a time- and dose-dependent manner, peaking at 5 min at 10 μM ATP. Moreover, ATP γ S, UTP, and UDP but not ADP or ADP β S increased phosphorylation of MAPKs, indicating the involvement of, at least, P2Y 2 /P2Y 4 and P2Y 6 receptor subtypes. RT – PCR studies and PCR product sequencing supported the expression of P2Y 2 and P2Y 4 receptors in this cell line. Spectro fl uorimetric measurements showed that cell stimulation with ATP induced transient elevations in intracellular calcium concentration. In addition, ATP-induced phosphorylation ofMAPKs in Caco-2 cells was dependent onSrcfamily tyrosinekinases, calcium in fl ux, and intracellular Ca 2+ release and was partially dependent on the cAMP/PKA and PKC pathways and the EGFR. General signi fi cance: These fi ndings provide new molecular basis for further understanding the mechanisms involved in ATP functions, as a signal transducer and activator of MAP kinase cascades, in colon adenocarcinoma Caco-2 cells.Fil: Buzzi, Natalia Sol. 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: Scodelaro Bilbao, Paola Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Centro de Recursos Naturales Renovables de la Zona Semiárida. Universidad Nacional del Sur. Centro de Recursos Naturales Renovables de la Zona Semiárida; 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; ArgentinaFil: Russo, Ana Josefa. Universidad Nacional del Sur; ArgentinaElsevier2009-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/28383Buzzi, Natalia Sol; Scodelaro Bilbao, Paola Gabriela; Boland, Ricardo Leopoldo; Russo, Ana Josefa; Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line; Elsevier; Biochimica et Biophysica Acta- General Subjects; 1790; 12; 10-2009; 1651-16590304-4165CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2009.10.005info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0304416509002918info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:59:25Zoai:ri.conicet.gov.ar:11336/28383instacron: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:34982025-09-29 09:59:25.453CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
title |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
spellingShingle |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line Buzzi, Natalia Sol Atp Mapks P2y Receptors Caco-2 Cells |
title_short |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
title_full |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
title_fullStr |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
title_full_unstemmed |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
title_sort |
Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line |
dc.creator.none.fl_str_mv |
Buzzi, Natalia Sol Scodelaro Bilbao, Paola Gabriela Boland, Ricardo Leopoldo Russo, Ana Josefa |
author |
Buzzi, Natalia Sol |
author_facet |
Buzzi, Natalia Sol Scodelaro Bilbao, Paola Gabriela Boland, Ricardo Leopoldo Russo, Ana Josefa |
author_role |
author |
author2 |
Scodelaro Bilbao, Paola Gabriela Boland, Ricardo Leopoldo Russo, Ana Josefa |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Atp Mapks P2y Receptors Caco-2 Cells |
topic |
Atp Mapks P2y Receptors Caco-2 Cells |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Background: ATP exerts diverse effects on various cell types via speci fi c purinergic P2Y receptors. Intracellular signaling cascades are the main routes of communication between P2Y receptors and regulatory targets in the cell. Methods and results: We examined the role of ATP in the modulation of ERK1/2, JNK1/2, and p38 MAP kinases (MAPKs) in human colon cancer Caco-2 cells. Immunoblot analysis showed that ATP induces the phosphorylation of MAPKs in a time- and dose-dependent manner, peaking at 5 min at 10 μM ATP. Moreover, ATP γ S, UTP, and UDP but not ADP or ADP β S increased phosphorylation of MAPKs, indicating the involvement of, at least, P2Y 2 /P2Y 4 and P2Y 6 receptor subtypes. RT – PCR studies and PCR product sequencing supported the expression of P2Y 2 and P2Y 4 receptors in this cell line. Spectro fl uorimetric measurements showed that cell stimulation with ATP induced transient elevations in intracellular calcium concentration. In addition, ATP-induced phosphorylation ofMAPKs in Caco-2 cells was dependent onSrcfamily tyrosinekinases, calcium in fl ux, and intracellular Ca 2+ release and was partially dependent on the cAMP/PKA and PKC pathways and the EGFR. General signi fi cance: These fi ndings provide new molecular basis for further understanding the mechanisms involved in ATP functions, as a signal transducer and activator of MAP kinase cascades, in colon adenocarcinoma Caco-2 cells. Fil: Buzzi, Natalia Sol. 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: Scodelaro Bilbao, Paola Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Centro de Recursos Naturales Renovables de la Zona Semiárida. Universidad Nacional del Sur. Centro de Recursos Naturales Renovables de la Zona Semiárida; 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 Fil: Russo, Ana Josefa. Universidad Nacional del Sur; Argentina |
description |
Background: ATP exerts diverse effects on various cell types via speci fi c purinergic P2Y receptors. Intracellular signaling cascades are the main routes of communication between P2Y receptors and regulatory targets in the cell. Methods and results: We examined the role of ATP in the modulation of ERK1/2, JNK1/2, and p38 MAP kinases (MAPKs) in human colon cancer Caco-2 cells. Immunoblot analysis showed that ATP induces the phosphorylation of MAPKs in a time- and dose-dependent manner, peaking at 5 min at 10 μM ATP. Moreover, ATP γ S, UTP, and UDP but not ADP or ADP β S increased phosphorylation of MAPKs, indicating the involvement of, at least, P2Y 2 /P2Y 4 and P2Y 6 receptor subtypes. RT – PCR studies and PCR product sequencing supported the expression of P2Y 2 and P2Y 4 receptors in this cell line. Spectro fl uorimetric measurements showed that cell stimulation with ATP induced transient elevations in intracellular calcium concentration. In addition, ATP-induced phosphorylation ofMAPKs in Caco-2 cells was dependent onSrcfamily tyrosinekinases, calcium in fl ux, and intracellular Ca 2+ release and was partially dependent on the cAMP/PKA and PKC pathways and the EGFR. General signi fi cance: These fi ndings provide new molecular basis for further understanding the mechanisms involved in ATP functions, as a signal transducer and activator of MAP kinase cascades, in colon adenocarcinoma Caco-2 cells. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-10 |
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/11336/28383 Buzzi, Natalia Sol; Scodelaro Bilbao, Paola Gabriela; Boland, Ricardo Leopoldo; Russo, Ana Josefa; Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line; Elsevier; Biochimica et Biophysica Acta- General Subjects; 1790; 12; 10-2009; 1651-1659 0304-4165 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/28383 |
identifier_str_mv |
Buzzi, Natalia Sol; Scodelaro Bilbao, Paola Gabriela; Boland, Ricardo Leopoldo; Russo, Ana Josefa; Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line; Elsevier; Biochimica et Biophysica Acta- General Subjects; 1790; 12; 10-2009; 1651-1659 0304-4165 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.bbagen.2009.10.005 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0304416509002918 |
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 |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |