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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/190630
Acceder
id CONICETDig_589de1adc0bccef28edc678edfe55132
oai_identifier_str oai:ri.conicet.gov.ar:11336/190630
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:02:10Zoai: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:34982025-10-22 11:02:10.844CONICET 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
_version_ 1846781222927204352
score 12.982451

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