Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation

Autores
Pena, Liliana Beatriz; Azpilicueta, Claudia Elsa; Gallego, Susana Mabel
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Copper is an essential trace element for living organisms, in excess, can be toxic to the cell because of its capacity to generate reactive oxygen species (ROS). Catalase (CAT) catalyzes the dismutation of hydrogen peroxide into water and dioxygen and in plants it is located in peroxisomes and glyoxysomes. Different metals can induce changes in CAT activity, but the mechanism underlying its changes is unclear. After 4 h of treatment with 5 and 10 μM CuCl2 a decrease in the specific CAT activity was detected in sunflower cotyledons of post-germinative heterotrophic seedlings. At 8 h of treatment, 5 μM Cu2+ produced an induction of CAT activity while only a complete recovery to control values was observed for 10 μM Cu2+ treated seedlings. These activity variations were not related to the level of CAT protein expression, but they did correlate with the oxidative state of the CAT protein. This indicates that the mechanism of CAT inactivation by Cu2+ involves oxidation of the protein structure. The level of the mRNA of CATA3 and CATA4 increased with the presence of the metal after 4 h of exposure. These CAT genes code for the synthesis of CAT subunits less sensitive to oxidation, which would prevent the copper-induced oxidative inactivation of CAT.
Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Azpilicueta, Claudia Elsa. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gallego, Susana Mabel. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Copper
Catalase
Helianthus Annuus L
Sunflower
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:11336/18198
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidationPena, Liliana BeatrizAzpilicueta, Claudia ElsaGallego, Susana MabelCopperCatalaseHelianthus Annuus LSunflowerhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Copper is an essential trace element for living organisms, in excess, can be toxic to the cell because of its capacity to generate reactive oxygen species (ROS). Catalase (CAT) catalyzes the dismutation of hydrogen peroxide into water and dioxygen and in plants it is located in peroxisomes and glyoxysomes. Different metals can induce changes in CAT activity, but the mechanism underlying its changes is unclear. After 4 h of treatment with 5 and 10 μM CuCl2 a decrease in the specific CAT activity was detected in sunflower cotyledons of post-germinative heterotrophic seedlings. At 8 h of treatment, 5 μM Cu2+ produced an induction of CAT activity while only a complete recovery to control values was observed for 10 μM Cu2+ treated seedlings. These activity variations were not related to the level of CAT protein expression, but they did correlate with the oxidative state of the CAT protein. This indicates that the mechanism of CAT inactivation by Cu2+ involves oxidation of the protein structure. The level of the mRNA of CATA3 and CATA4 increased with the presence of the metal after 4 h of exposure. These CAT genes code for the synthesis of CAT subunits less sensitive to oxidation, which would prevent the copper-induced oxidative inactivation of CAT.Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Azpilicueta, Claudia Elsa. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gallego, Susana Mabel. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Gmbh2011-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18198Pena, Liliana Beatriz; Azpilicueta, Claudia Elsa; Gallego, Susana Mabel; Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation; Elsevier Gmbh; Journal of Trace Elements in Medicine and Biology; 25; 3; 7-2011; 125-1290946-672XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0946672X11000708?via%3Dihubinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jtemb.2011.05.001info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:25:53Zoai:ri.conicet.gov.ar:11336/18198instacron: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 14:25:53.419CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
title Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
spellingShingle Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
Pena, Liliana Beatriz
Copper
Catalase
Helianthus Annuus L
Sunflower
title_short Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
title_full Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
title_fullStr Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
title_full_unstemmed Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
title_sort Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation
dc.creator.none.fl_str_mv Pena, Liliana Beatriz
Azpilicueta, Claudia Elsa
Gallego, Susana Mabel
author Pena, Liliana Beatriz
author_facet Pena, Liliana Beatriz
Azpilicueta, Claudia Elsa
Gallego, Susana Mabel
author_role author
author2 Azpilicueta, Claudia Elsa
Gallego, Susana Mabel
author2_role author
author
dc.subject.none.fl_str_mv Copper
Catalase
Helianthus Annuus L
Sunflower
topic Copper
Catalase
Helianthus Annuus L
Sunflower
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Copper is an essential trace element for living organisms, in excess, can be toxic to the cell because of its capacity to generate reactive oxygen species (ROS). Catalase (CAT) catalyzes the dismutation of hydrogen peroxide into water and dioxygen and in plants it is located in peroxisomes and glyoxysomes. Different metals can induce changes in CAT activity, but the mechanism underlying its changes is unclear. After 4 h of treatment with 5 and 10 μM CuCl2 a decrease in the specific CAT activity was detected in sunflower cotyledons of post-germinative heterotrophic seedlings. At 8 h of treatment, 5 μM Cu2+ produced an induction of CAT activity while only a complete recovery to control values was observed for 10 μM Cu2+ treated seedlings. These activity variations were not related to the level of CAT protein expression, but they did correlate with the oxidative state of the CAT protein. This indicates that the mechanism of CAT inactivation by Cu2+ involves oxidation of the protein structure. The level of the mRNA of CATA3 and CATA4 increased with the presence of the metal after 4 h of exposure. These CAT genes code for the synthesis of CAT subunits less sensitive to oxidation, which would prevent the copper-induced oxidative inactivation of CAT.
Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Azpilicueta, Claudia Elsa. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gallego, Susana Mabel. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Copper is an essential trace element for living organisms, in excess, can be toxic to the cell because of its capacity to generate reactive oxygen species (ROS). Catalase (CAT) catalyzes the dismutation of hydrogen peroxide into water and dioxygen and in plants it is located in peroxisomes and glyoxysomes. Different metals can induce changes in CAT activity, but the mechanism underlying its changes is unclear. After 4 h of treatment with 5 and 10 μM CuCl2 a decrease in the specific CAT activity was detected in sunflower cotyledons of post-germinative heterotrophic seedlings. At 8 h of treatment, 5 μM Cu2+ produced an induction of CAT activity while only a complete recovery to control values was observed for 10 μM Cu2+ treated seedlings. These activity variations were not related to the level of CAT protein expression, but they did correlate with the oxidative state of the CAT protein. This indicates that the mechanism of CAT inactivation by Cu2+ involves oxidation of the protein structure. The level of the mRNA of CATA3 and CATA4 increased with the presence of the metal after 4 h of exposure. These CAT genes code for the synthesis of CAT subunits less sensitive to oxidation, which would prevent the copper-induced oxidative inactivation of CAT.
publishDate 2011
dc.date.none.fl_str_mv 2011-07
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/11336/18198
Pena, Liliana Beatriz; Azpilicueta, Claudia Elsa; Gallego, Susana Mabel; Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation; Elsevier Gmbh; Journal of Trace Elements in Medicine and Biology; 25; 3; 7-2011; 125-129
0946-672X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/18198
identifier_str_mv Pena, Liliana Beatriz; Azpilicueta, Claudia Elsa; Gallego, Susana Mabel; Sunflower cotyledons cope with copper stress by inducing catalase subunits less sensitive to oxidation; Elsevier Gmbh; Journal of Trace Elements in Medicine and Biology; 25; 3; 7-2011; 125-129
0946-672X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0946672X11000708?via%3Dihub
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jtemb.2011.05.001
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
dc.publisher.none.fl_str_mv Elsevier Gmbh
publisher.none.fl_str_mv Elsevier Gmbh
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 13.22299

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