Effect of different metals on protease activity in sunflower cotyledons

Autores
Pena, Liliana Beatriz; Tomaro, Maria Lujan; Gallego, Susana Mabel
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Proteases are crucial for living cells and play a role in plant cell adaptation to environmental conditions. Oxidative stress produced oxidized proteins which are selectively degraded by proteases. To understand the role of proteolysis in response to metal stress, sunflower plants (a plant suitable for phytoremediation) were treated with 100 μM of CdCl2, CuCl2, AlCl3, CoCl2,PbCl2, CrCl3, NiCl2, HgCl2 or ZnCl2. Changes in protease activity, gelatinase profile and protein oxidation were examined in sunflower cotyledons. Our results indicate that this tissue has mainly acid proteases belonging to different classes. Although all metals (except Zn) increased protein oxidation (62, 57, 112, 74, 74, 68, 64 and 40% for Pb, Al, Ni, Cd, Hg, Co, Cr andCu over the control), they altered proteolysis in different ways. Pb, Al and Ni treatment decreased protease activity 22, 28 and 30% respect to control while Cd and Hg increased this activity in 23 and 27%. In Zn, Cu and Co treatments protease activity remained similar to control treatment. These results indicate that different proteases are involved in plant defence againstmetal toxicity. However, the identification of specific oxidized proteins involved in this process and the metal effect on class specific proteases should provide greater information.
Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Tomaro, Maria Lujan. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; 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. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
PROTEASE
HEAVY METALS
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:11336/241980
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Effect of different metals on protease activity in sunflower cotyledonsPena, Liliana BeatrizTomaro, Maria LujanGallego, Susana MabelPROTEASEHEAVY METALShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Proteases are crucial for living cells and play a role in plant cell adaptation to environmental conditions. Oxidative stress produced oxidized proteins which are selectively degraded by proteases. To understand the role of proteolysis in response to metal stress, sunflower plants (a plant suitable for phytoremediation) were treated with 100 μM of CdCl2, CuCl2, AlCl3, CoCl2,PbCl2, CrCl3, NiCl2, HgCl2 or ZnCl2. Changes in protease activity, gelatinase profile and protein oxidation were examined in sunflower cotyledons. Our results indicate that this tissue has mainly acid proteases belonging to different classes. Although all metals (except Zn) increased protein oxidation (62, 57, 112, 74, 74, 68, 64 and 40% for Pb, Al, Ni, Cd, Hg, Co, Cr andCu over the control), they altered proteolysis in different ways. Pb, Al and Ni treatment decreased protease activity 22, 28 and 30% respect to control while Cd and Hg increased this activity in 23 and 27%. In Zn, Cu and Co treatments protease activity remained similar to control treatment. These results indicate that different proteases are involved in plant defence againstmetal toxicity. However, the identification of specific oxidized proteins involved in this process and the metal effect on class specific proteases should provide greater information.Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Tomaro, Maria Lujan. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; 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. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaPontificia Universidad Católica de Valparaíso2006-12info: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/11336/241980Pena, Liliana Beatriz; Tomaro, Maria Lujan; Gallego, Susana Mabel; Effect of different metals on protease activity in sunflower cotyledons; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 12-2006; 258-2620717-3458CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ejbiotechnology.info/index.php/ejbiotechnology/article/view/v9n3-18info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:54:50Zoai:ri.conicet.gov.ar:11336/241980instacron: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 09:54:50.478CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of different metals on protease activity in sunflower cotyledons
title Effect of different metals on protease activity in sunflower cotyledons
spellingShingle Effect of different metals on protease activity in sunflower cotyledons
Pena, Liliana Beatriz
PROTEASE
HEAVY METALS
title_short Effect of different metals on protease activity in sunflower cotyledons
title_full Effect of different metals on protease activity in sunflower cotyledons
title_fullStr Effect of different metals on protease activity in sunflower cotyledons
title_full_unstemmed Effect of different metals on protease activity in sunflower cotyledons
title_sort Effect of different metals on protease activity in sunflower cotyledons
dc.creator.none.fl_str_mv Pena, Liliana Beatriz
Tomaro, Maria Lujan
Gallego, Susana Mabel
author Pena, Liliana Beatriz
author_facet Pena, Liliana Beatriz
Tomaro, Maria Lujan
Gallego, Susana Mabel
author_role author
author2 Tomaro, Maria Lujan
Gallego, Susana Mabel
author2_role author
author
dc.subject.none.fl_str_mv PROTEASE
HEAVY METALS
topic PROTEASE
HEAVY METALS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Proteases are crucial for living cells and play a role in plant cell adaptation to environmental conditions. Oxidative stress produced oxidized proteins which are selectively degraded by proteases. To understand the role of proteolysis in response to metal stress, sunflower plants (a plant suitable for phytoremediation) were treated with 100 μM of CdCl2, CuCl2, AlCl3, CoCl2,PbCl2, CrCl3, NiCl2, HgCl2 or ZnCl2. Changes in protease activity, gelatinase profile and protein oxidation were examined in sunflower cotyledons. Our results indicate that this tissue has mainly acid proteases belonging to different classes. Although all metals (except Zn) increased protein oxidation (62, 57, 112, 74, 74, 68, 64 and 40% for Pb, Al, Ni, Cd, Hg, Co, Cr andCu over the control), they altered proteolysis in different ways. Pb, Al and Ni treatment decreased protease activity 22, 28 and 30% respect to control while Cd and Hg increased this activity in 23 and 27%. In Zn, Cu and Co treatments protease activity remained similar to control treatment. These results indicate that different proteases are involved in plant defence againstmetal toxicity. However, the identification of specific oxidized proteins involved in this process and the metal effect on class specific proteases should provide greater information.
Fil: Pena, Liliana Beatriz. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Tomaro, Maria Lujan. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Biológica. Cátedra de Química Biológica Vegetal; 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. Cátedra de Química Biológica Vegetal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Proteases are crucial for living cells and play a role in plant cell adaptation to environmental conditions. Oxidative stress produced oxidized proteins which are selectively degraded by proteases. To understand the role of proteolysis in response to metal stress, sunflower plants (a plant suitable for phytoremediation) were treated with 100 μM of CdCl2, CuCl2, AlCl3, CoCl2,PbCl2, CrCl3, NiCl2, HgCl2 or ZnCl2. Changes in protease activity, gelatinase profile and protein oxidation were examined in sunflower cotyledons. Our results indicate that this tissue has mainly acid proteases belonging to different classes. Although all metals (except Zn) increased protein oxidation (62, 57, 112, 74, 74, 68, 64 and 40% for Pb, Al, Ni, Cd, Hg, Co, Cr andCu over the control), they altered proteolysis in different ways. Pb, Al and Ni treatment decreased protease activity 22, 28 and 30% respect to control while Cd and Hg increased this activity in 23 and 27%. In Zn, Cu and Co treatments protease activity remained similar to control treatment. These results indicate that different proteases are involved in plant defence againstmetal toxicity. However, the identification of specific oxidized proteins involved in this process and the metal effect on class specific proteases should provide greater information.
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/11336/241980
Pena, Liliana Beatriz; Tomaro, Maria Lujan; Gallego, Susana Mabel; Effect of different metals on protease activity in sunflower cotyledons; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 12-2006; 258-262
0717-3458
CONICET Digital
CONICET
url http://hdl.handle.net/11336/241980
identifier_str_mv Pena, Liliana Beatriz; Tomaro, Maria Lujan; Gallego, Susana Mabel; Effect of different metals on protease activity in sunflower cotyledons; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 12-2006; 258-262
0717-3458
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.ejbiotechnology.info/index.php/ejbiotechnology/article/view/v9n3-18
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Pontificia Universidad Católica de Valparaíso
publisher.none.fl_str_mv Pontificia Universidad Católica de Valparaíso
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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