Proline dehydrogenase is a positive regulator of cell death in different kingdoms
- Autores
- Cecchini, Nicolas Miguel; Monteoliva, Mariela Inés; Alvarez, Maria Elena
- Año de publicación
- 2011
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Δ1-pyrroline-5-carboxylate (P5C). This is the first of the two enzymatic reactions that convert proline (Pro) into glutamic acid (Glu). The P5C thus produced is non-enzymatically transformed into glutamate semialdehyde (GSA), which acts as a substrate of P5C dehydrogenase (P5CDH) to generate Glu. Activation of ProDH can generate different effects depending on the behaviour of other enzymes of this metabolism. Under different conditions it can generate toxic levels of P5C, alter the cellular redox homeostasis and even produce reactive oxygen species (ROS). Recent studies indicate that in Arabidopsis, the enzyme potentiates the oxidative burst and cell death associated to the Hypersensitive Responses (HR). Interestingly, activation of ProDH can also produce harmful effects in other organisms, suggesting that the enzyme may play a conserved role in the control of cell death.
Fil: Cecchini, Nicolas Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Monteoliva, Mariela Inés. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigaciones Agropecuarias. Unidad de Estudios Agropecuarios - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Unidad de Estudios Agropecuarios; Argentina
Fil: Alvarez, Maria Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina - Materia
-
CELL DEATH
HYPERSENSITIVE RESPONSE (HR)
PROLINE
PROLINE DEHYDROGENASE
REACTIVE OXYGEN SPECIES (ROS) - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/190630
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Proline dehydrogenase is a positive regulator of cell death in different kingdomsCecchini, Nicolas MiguelMonteoliva, Mariela InésAlvarez, Maria ElenaCELL DEATHHYPERSENSITIVE RESPONSE (HR)PROLINEPROLINE DEHYDROGENASEREACTIVE OXYGEN SPECIES (ROS)https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Δ1-pyrroline-5-carboxylate (P5C). This is the first of the two enzymatic reactions that convert proline (Pro) into glutamic acid (Glu). The P5C thus produced is non-enzymatically transformed into glutamate semialdehyde (GSA), which acts as a substrate of P5C dehydrogenase (P5CDH) to generate Glu. Activation of ProDH can generate different effects depending on the behaviour of other enzymes of this metabolism. Under different conditions it can generate toxic levels of P5C, alter the cellular redox homeostasis and even produce reactive oxygen species (ROS). Recent studies indicate that in Arabidopsis, the enzyme potentiates the oxidative burst and cell death associated to the Hypersensitive Responses (HR). Interestingly, activation of ProDH can also produce harmful effects in other organisms, suggesting that the enzyme may play a conserved role in the control of cell death.Fil: Cecchini, Nicolas Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Monteoliva, Mariela Inés. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigaciones Agropecuarias. Unidad de Estudios Agropecuarios - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Unidad de Estudios Agropecuarios; ArgentinaFil: Alvarez, Maria Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaTaylor & Francis2011-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/190630Cecchini, Nicolas Miguel; Monteoliva, Mariela Inés; Alvarez, Maria Elena; Proline dehydrogenase is a positive regulator of cell death in different kingdoms; Taylor & Francis; Plant Signaling and Behavior; 6; 8; 1-8-2011; 1195-11971559-23161559-2324CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.4161/psb.6.8.15791info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.4161/psb.6.8.15791info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:06Zoai:ri.conicet.gov.ar:11336/190630instacron: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 09:34:06.871CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
title |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
spellingShingle |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms Cecchini, Nicolas Miguel CELL DEATH HYPERSENSITIVE RESPONSE (HR) PROLINE PROLINE DEHYDROGENASE REACTIVE OXYGEN SPECIES (ROS) |
title_short |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
title_full |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
title_fullStr |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
title_full_unstemmed |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
title_sort |
Proline dehydrogenase is a positive regulator of cell death in different kingdoms |
dc.creator.none.fl_str_mv |
Cecchini, Nicolas Miguel Monteoliva, Mariela Inés Alvarez, Maria Elena |
author |
Cecchini, Nicolas Miguel |
author_facet |
Cecchini, Nicolas Miguel Monteoliva, Mariela Inés Alvarez, Maria Elena |
author_role |
author |
author2 |
Monteoliva, Mariela Inés Alvarez, Maria Elena |
author2_role |
author author |
dc.subject.none.fl_str_mv |
CELL DEATH HYPERSENSITIVE RESPONSE (HR) PROLINE PROLINE DEHYDROGENASE REACTIVE OXYGEN SPECIES (ROS) |
topic |
CELL DEATH HYPERSENSITIVE RESPONSE (HR) PROLINE PROLINE DEHYDROGENASE REACTIVE OXYGEN SPECIES (ROS) |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Δ1-pyrroline-5-carboxylate (P5C). This is the first of the two enzymatic reactions that convert proline (Pro) into glutamic acid (Glu). The P5C thus produced is non-enzymatically transformed into glutamate semialdehyde (GSA), which acts as a substrate of P5C dehydrogenase (P5CDH) to generate Glu. Activation of ProDH can generate different effects depending on the behaviour of other enzymes of this metabolism. Under different conditions it can generate toxic levels of P5C, alter the cellular redox homeostasis and even produce reactive oxygen species (ROS). Recent studies indicate that in Arabidopsis, the enzyme potentiates the oxidative burst and cell death associated to the Hypersensitive Responses (HR). Interestingly, activation of ProDH can also produce harmful effects in other organisms, suggesting that the enzyme may play a conserved role in the control of cell death. Fil: Cecchini, Nicolas Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Monteoliva, Mariela Inés. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigaciones Agropecuarias. Unidad de Estudios Agropecuarios - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Unidad de Estudios Agropecuarios; Argentina Fil: Alvarez, Maria Elena. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina |
description |
Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Δ1-pyrroline-5-carboxylate (P5C). This is the first of the two enzymatic reactions that convert proline (Pro) into glutamic acid (Glu). The P5C thus produced is non-enzymatically transformed into glutamate semialdehyde (GSA), which acts as a substrate of P5C dehydrogenase (P5CDH) to generate Glu. Activation of ProDH can generate different effects depending on the behaviour of other enzymes of this metabolism. Under different conditions it can generate toxic levels of P5C, alter the cellular redox homeostasis and even produce reactive oxygen species (ROS). Recent studies indicate that in Arabidopsis, the enzyme potentiates the oxidative burst and cell death associated to the Hypersensitive Responses (HR). Interestingly, activation of ProDH can also produce harmful effects in other organisms, suggesting that the enzyme may play a conserved role in the control of cell death. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-08-01 |
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/11336/190630 Cecchini, Nicolas Miguel; Monteoliva, Mariela Inés; Alvarez, Maria Elena; Proline dehydrogenase is a positive regulator of cell death in different kingdoms; Taylor & Francis; Plant Signaling and Behavior; 6; 8; 1-8-2011; 1195-1197 1559-2316 1559-2324 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/190630 |
identifier_str_mv |
Cecchini, Nicolas Miguel; Monteoliva, Mariela Inés; Alvarez, Maria Elena; Proline dehydrogenase is a positive regulator of cell death in different kingdoms; Taylor & Francis; Plant Signaling and Behavior; 6; 8; 1-8-2011; 1195-1197 1559-2316 1559-2324 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.4161/psb.6.8.15791 info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.4161/psb.6.8.15791 |
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 |
dc.publisher.none.fl_str_mv |
Taylor & Francis |
publisher.none.fl_str_mv |
Taylor & Francis |
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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1844613054077075456 |
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13.070432 |