Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones

Autores
Mariani, Maria Elisa; Madoery, Ricardo Román; Fidelio, Gerardo Daniel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces. The effect of IAA and IPA auxins over the activity of recombinant sPLA2 isoforms from Glycine max was studied using membrane model systems including mixed micelles and Langmuir lipid monolayers. Both phytohormones stimulate the activity of both plant sPLA2 using DLPC/Triton mixed micelles as substrate. To elucidate the mechanism of action of the phytohormones, we showed that both auxins are able to self-penetrate lipid monolayers and cause an increment in surface pressure and an expansion of lipid/phytohormone mixed interfaces. The stimulating effect of auxins over phospholipase A2 activity was still present when using Langmuir mixed monolayers as organized substrate regardless of sPLA2 source (plant or animal). All the data suggest that the stimulating effect of auxins over sPLA2 is due to a more favorable interfacial environment rather to a direct effect over the enzyme.
Fil: Mariani, Maria Elisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Fil: Madoery, Ricardo Román. Universidad Nacional de Cordoba. Facultad de Cs.agropecuarias. Departamento de Fundamentacion Biologica; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Materia
Glycine Max Phospholipase A2
Auxin Stimulation
Interfacial Catalysis
Soybean Spla2s
Indole-3-Propionic Acid
Indole-3-Acetic Acid
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10627
Acceder
id CONICETDig_4220a98ff0727043c0bf5aaf345f03bd
oai_identifier_str oai:ri.conicet.gov.ar:11336/10627
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormonesMariani, Maria ElisaMadoery, Ricardo RománFidelio, Gerardo DanielGlycine Max Phospholipase A2Auxin StimulationInterfacial CatalysisSoybean Spla2sIndole-3-Propionic AcidIndole-3-Acetic Acidhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces. The effect of IAA and IPA auxins over the activity of recombinant sPLA2 isoforms from Glycine max was studied using membrane model systems including mixed micelles and Langmuir lipid monolayers. Both phytohormones stimulate the activity of both plant sPLA2 using DLPC/Triton mixed micelles as substrate. To elucidate the mechanism of action of the phytohormones, we showed that both auxins are able to self-penetrate lipid monolayers and cause an increment in surface pressure and an expansion of lipid/phytohormone mixed interfaces. The stimulating effect of auxins over phospholipase A2 activity was still present when using Langmuir mixed monolayers as organized substrate regardless of sPLA2 source (plant or animal). All the data suggest that the stimulating effect of auxins over sPLA2 is due to a more favorable interfacial environment rather to a direct effect over the enzyme.Fil: Mariani, Maria Elisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; ArgentinaFil: Madoery, Ricardo Román. Universidad Nacional de Cordoba. Facultad de Cs.agropecuarias. Departamento de Fundamentacion Biologica; ArgentinaFil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; ArgentinaElsevier Ireland2015-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10627Mariani, Maria Elisa; Madoery, Ricardo Román; Fidelio, Gerardo Daniel; Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones; Elsevier Ireland; Chemistry And Physics Of Lipids; 189; 7-2015; 1-60009-3084enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.chemphyslip.2015.05.003info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0009308415000328info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:18:44Zoai:ri.conicet.gov.ar:11336/10627instacron: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:34982025-10-22 12:18:44.683CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
title Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
spellingShingle Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
Mariani, Maria Elisa
Glycine Max Phospholipase A2
Auxin Stimulation
Interfacial Catalysis
Soybean Spla2s
Indole-3-Propionic Acid
Indole-3-Acetic Acid
title_short Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
title_full Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
title_fullStr Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
title_full_unstemmed Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
title_sort Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones
dc.creator.none.fl_str_mv Mariani, Maria Elisa
Madoery, Ricardo Román
Fidelio, Gerardo Daniel
author Mariani, Maria Elisa
author_facet Mariani, Maria Elisa
Madoery, Ricardo Román
Fidelio, Gerardo Daniel
author_role author
author2 Madoery, Ricardo Román
Fidelio, Gerardo Daniel
author2_role author
author
dc.subject.none.fl_str_mv Glycine Max Phospholipase A2
Auxin Stimulation
Interfacial Catalysis
Soybean Spla2s
Indole-3-Propionic Acid
Indole-3-Acetic Acid
topic Glycine Max Phospholipase A2
Auxin Stimulation
Interfacial Catalysis
Soybean Spla2s
Indole-3-Propionic Acid
Indole-3-Acetic Acid
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces. The effect of IAA and IPA auxins over the activity of recombinant sPLA2 isoforms from Glycine max was studied using membrane model systems including mixed micelles and Langmuir lipid monolayers. Both phytohormones stimulate the activity of both plant sPLA2 using DLPC/Triton mixed micelles as substrate. To elucidate the mechanism of action of the phytohormones, we showed that both auxins are able to self-penetrate lipid monolayers and cause an increment in surface pressure and an expansion of lipid/phytohormone mixed interfaces. The stimulating effect of auxins over phospholipase A2 activity was still present when using Langmuir mixed monolayers as organized substrate regardless of sPLA2 source (plant or animal). All the data suggest that the stimulating effect of auxins over sPLA2 is due to a more favorable interfacial environment rather to a direct effect over the enzyme.
Fil: Mariani, Maria Elisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Fil: Madoery, Ricardo Román. Universidad Nacional de Cordoba. Facultad de Cs.agropecuarias. Departamento de Fundamentacion Biologica; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
description Secretory phospholipase A2 (sPLA2) are soluble enzymes that catalyze the conversion of phospholipids to lysophospholipids and free fatty acids at membrane interfaces. The effect of IAA and IPA auxins over the activity of recombinant sPLA2 isoforms from Glycine max was studied using membrane model systems including mixed micelles and Langmuir lipid monolayers. Both phytohormones stimulate the activity of both plant sPLA2 using DLPC/Triton mixed micelles as substrate. To elucidate the mechanism of action of the phytohormones, we showed that both auxins are able to self-penetrate lipid monolayers and cause an increment in surface pressure and an expansion of lipid/phytohormone mixed interfaces. The stimulating effect of auxins over phospholipase A2 activity was still present when using Langmuir mixed monolayers as organized substrate regardless of sPLA2 source (plant or animal). All the data suggest that the stimulating effect of auxins over sPLA2 is due to a more favorable interfacial environment rather to a direct effect over the enzyme.
publishDate 2015
dc.date.none.fl_str_mv 2015-07
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/11336/10627
Mariani, Maria Elisa; Madoery, Ricardo Román; Fidelio, Gerardo Daniel; Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones; Elsevier Ireland; Chemistry And Physics Of Lipids; 189; 7-2015; 1-6
0009-3084
url http://hdl.handle.net/11336/10627
identifier_str_mv Mariani, Maria Elisa; Madoery, Ricardo Román; Fidelio, Gerardo Daniel; Auxins action on Glycine max secretory phospholipase A2 is mediated by the interfacial properties imposed by the phytohormones; Elsevier Ireland; Chemistry And Physics Of Lipids; 189; 7-2015; 1-6
0009-3084
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.chemphyslip.2015.05.003
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0009308415000328
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv 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_ 1846782620791209984
score 12.982451

Publicaciones similares