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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/28383

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oai_identifier_str oai:ri.conicet.gov.ar:11336/28383
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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
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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