Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum

Autores
Vasconsuelo, Andrea Anahi; Picotto, Gabriela; Giuletti, Ana M.; Boland, Ricardo Leopoldo
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Elicitation with chitosan (200 mg/l) significantly stimulates (100%) anthraquinone (Aq) synthesis in Rubia tinctorum L. cultures, but the mechanism of elicitation is largely unknown.We recently showed that the effects of the elicitor involve phospholipase C (PLC), protein kinase C (PKC), phosphoinositide 3-kinase (PI3K) and mitogen activated protein kinase (MAPK) cascades. Here, we show that the elicitor action on Aq production can be blocked with the intracellular Ca2+ chelator BAPTA-AM but not in a Ca2+-free medium (+EGTA) or in the presence of the voltage-dependent Ca2+ channel antagonists verapamil and nifedipine. In agreement with these observations, spectrofluorimetric measurements in Fura 2-loaded R. tinctorum cells show that chitosan increases intracellular Ca2+ concentration in a medium devoid of calcium. Short treatment intervals (1?5 min) of cells with the elicitor significantly increased DAG and IP3 formation. Moreover, the PI-PLC inhibitors neomycin and U73122 diminished to a great extent chitosan-induced Aq synthesis. Blockers of Ca2+ release from inner stores such as 2-APB, TMB-8, caffeine, ruthenium red and dantrolene inhibited elicitation. Chitosan rapidly stimulated (phosphorylated) MAPK. This effect was significantly decreased by the calcium modulators used above. However, EGTA did not prevent activation of MAPK. Compound LY24009, a blocker of PI3K, inhibited MAPK phosphorylation by chitosan. Accordingly, an increase in PI3K activity was observed in parallel. The results of this study show that chitosan induction of anthraquinone synthesis in R. tinctorum involves the stimulation of PLC, intracellular Ca2+ mobilization and PI3K, which mediate MAPK activation.
Fil: Vasconsuelo, Andrea Anahi. 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: Picotto, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Giuletti, Ana M.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; 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
Materia
Rubia Tinctorum L
Protein G
Anthraquinone
Chitosan
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:11336/82507
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/82507
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorumVasconsuelo, Andrea AnahiPicotto, GabrielaGiuletti, Ana M.Boland, Ricardo LeopoldoRubia Tinctorum LProtein GAnthraquinoneChitosanhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Elicitation with chitosan (200 mg/l) significantly stimulates (100%) anthraquinone (Aq) synthesis in Rubia tinctorum L. cultures, but the mechanism of elicitation is largely unknown.We recently showed that the effects of the elicitor involve phospholipase C (PLC), protein kinase C (PKC), phosphoinositide 3-kinase (PI3K) and mitogen activated protein kinase (MAPK) cascades. Here, we show that the elicitor action on Aq production can be blocked with the intracellular Ca2+ chelator BAPTA-AM but not in a Ca2+-free medium (+EGTA) or in the presence of the voltage-dependent Ca2+ channel antagonists verapamil and nifedipine. In agreement with these observations, spectrofluorimetric measurements in Fura 2-loaded R. tinctorum cells show that chitosan increases intracellular Ca2+ concentration in a medium devoid of calcium. Short treatment intervals (1?5 min) of cells with the elicitor significantly increased DAG and IP3 formation. Moreover, the PI-PLC inhibitors neomycin and U73122 diminished to a great extent chitosan-induced Aq synthesis. Blockers of Ca2+ release from inner stores such as 2-APB, TMB-8, caffeine, ruthenium red and dantrolene inhibited elicitation. Chitosan rapidly stimulated (phosphorylated) MAPK. This effect was significantly decreased by the calcium modulators used above. However, EGTA did not prevent activation of MAPK. Compound LY24009, a blocker of PI3K, inhibited MAPK phosphorylation by chitosan. Accordingly, an increase in PI3K activity was observed in parallel. The results of this study show that chitosan induction of anthraquinone synthesis in R. tinctorum involves the stimulation of PLC, intracellular Ca2+ mobilization and PI3K, which mediate MAPK activation.Fil: Vasconsuelo, Andrea Anahi. 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: Picotto, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; ArgentinaFil: Giuletti, Ana M.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; 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; ArgentinaWiley Blackwell Publishing, Inc2006-12info: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/pdfhttp://hdl.handle.net/11336/82507Vasconsuelo, Andrea Anahi; Picotto, Gabriela; Giuletti, Ana M.; Boland, Ricardo Leopoldo; Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 128; 12-2006; 29-370031-93171399-3054CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1111/j.1399-3054.2006.00717.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1399-3054.2006.00717.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:15Zoai:ri.conicet.gov.ar:11336/82507instacron: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:34982025-09-03 09:59:16.139CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
title Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
spellingShingle Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
Vasconsuelo, Andrea Anahi
Rubia Tinctorum L
Protein G
Anthraquinone
Chitosan
title_short Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
title_full Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
title_fullStr Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
title_full_unstemmed Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
title_sort Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum
dc.creator.none.fl_str_mv Vasconsuelo, Andrea Anahi
Picotto, Gabriela
Giuletti, Ana M.
Boland, Ricardo Leopoldo
author Vasconsuelo, Andrea Anahi
author_facet Vasconsuelo, Andrea Anahi
Picotto, Gabriela
Giuletti, Ana M.
Boland, Ricardo Leopoldo
author_role author
author2 Picotto, Gabriela
Giuletti, Ana M.
Boland, Ricardo Leopoldo
author2_role author
author
author
dc.subject.none.fl_str_mv Rubia Tinctorum L
Protein G
Anthraquinone
Chitosan
topic Rubia Tinctorum L
Protein G
Anthraquinone
Chitosan
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Elicitation with chitosan (200 mg/l) significantly stimulates (100%) anthraquinone (Aq) synthesis in Rubia tinctorum L. cultures, but the mechanism of elicitation is largely unknown.We recently showed that the effects of the elicitor involve phospholipase C (PLC), protein kinase C (PKC), phosphoinositide 3-kinase (PI3K) and mitogen activated protein kinase (MAPK) cascades. Here, we show that the elicitor action on Aq production can be blocked with the intracellular Ca2+ chelator BAPTA-AM but not in a Ca2+-free medium (+EGTA) or in the presence of the voltage-dependent Ca2+ channel antagonists verapamil and nifedipine. In agreement with these observations, spectrofluorimetric measurements in Fura 2-loaded R. tinctorum cells show that chitosan increases intracellular Ca2+ concentration in a medium devoid of calcium. Short treatment intervals (1?5 min) of cells with the elicitor significantly increased DAG and IP3 formation. Moreover, the PI-PLC inhibitors neomycin and U73122 diminished to a great extent chitosan-induced Aq synthesis. Blockers of Ca2+ release from inner stores such as 2-APB, TMB-8, caffeine, ruthenium red and dantrolene inhibited elicitation. Chitosan rapidly stimulated (phosphorylated) MAPK. This effect was significantly decreased by the calcium modulators used above. However, EGTA did not prevent activation of MAPK. Compound LY24009, a blocker of PI3K, inhibited MAPK phosphorylation by chitosan. Accordingly, an increase in PI3K activity was observed in parallel. The results of this study show that chitosan induction of anthraquinone synthesis in R. tinctorum involves the stimulation of PLC, intracellular Ca2+ mobilization and PI3K, which mediate MAPK activation.
Fil: Vasconsuelo, Andrea Anahi. 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: Picotto, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Giuletti, Ana M.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; 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
description Elicitation with chitosan (200 mg/l) significantly stimulates (100%) anthraquinone (Aq) synthesis in Rubia tinctorum L. cultures, but the mechanism of elicitation is largely unknown.We recently showed that the effects of the elicitor involve phospholipase C (PLC), protein kinase C (PKC), phosphoinositide 3-kinase (PI3K) and mitogen activated protein kinase (MAPK) cascades. Here, we show that the elicitor action on Aq production can be blocked with the intracellular Ca2+ chelator BAPTA-AM but not in a Ca2+-free medium (+EGTA) or in the presence of the voltage-dependent Ca2+ channel antagonists verapamil and nifedipine. In agreement with these observations, spectrofluorimetric measurements in Fura 2-loaded R. tinctorum cells show that chitosan increases intracellular Ca2+ concentration in a medium devoid of calcium. Short treatment intervals (1?5 min) of cells with the elicitor significantly increased DAG and IP3 formation. Moreover, the PI-PLC inhibitors neomycin and U73122 diminished to a great extent chitosan-induced Aq synthesis. Blockers of Ca2+ release from inner stores such as 2-APB, TMB-8, caffeine, ruthenium red and dantrolene inhibited elicitation. Chitosan rapidly stimulated (phosphorylated) MAPK. This effect was significantly decreased by the calcium modulators used above. However, EGTA did not prevent activation of MAPK. Compound LY24009, a blocker of PI3K, inhibited MAPK phosphorylation by chitosan. Accordingly, an increase in PI3K activity was observed in parallel. The results of this study show that chitosan induction of anthraquinone synthesis in R. tinctorum involves the stimulation of PLC, intracellular Ca2+ mobilization and PI3K, which mediate MAPK activation.
publishDate 2006
dc.date.none.fl_str_mv 2006-12
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/11336/82507
Vasconsuelo, Andrea Anahi; Picotto, Gabriela; Giuletti, Ana M.; Boland, Ricardo Leopoldo; Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 128; 12-2006; 29-37
0031-9317
1399-3054
CONICET Digital
CONICET
url http://hdl.handle.net/11336/82507
identifier_str_mv Vasconsuelo, Andrea Anahi; Picotto, Gabriela; Giuletti, Ana M.; Boland, Ricardo Leopoldo; Involvement of G‐proteins in chitosan‐induced Anthraquinone synthesis in Rubia tinctorum; Wiley Blackwell Publishing, Inc; Physiologia Plantarum; 128; 12-2006; 29-37
0031-9317
1399-3054
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://onlinelibrary.wiley.com/doi/full/10.1111/j.1399-3054.2006.00717.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1399-3054.2006.00717.x
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
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application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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score 13.13397

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