Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences

The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modifica...

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Detalles Bibliográficos
Autores: Martínez Ruiz, Antonio, Lamas, Santiago
Tipo de recurso: artículo
Fecha de publicación:2007
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/102745
Acceso en línea:https://hdl.handle.net/20.500.14352/102745
Access Level:acceso abierto
Palabra clave:577.1
577.2
Nitric oxide
Post-translational modifications
Oxidative stress
Glutathione
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
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oai_identifier_str oai:docta.ucm.es:20.500.14352/102745
network_acronym_str ES
network_name_str España
repository_id_str
spelling Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergencesMartínez Ruiz, AntonioLamas, Santiago577.1577.2Nitric oxidePost-translational modificationsOxidative stressGlutathioneBioquímica (Farmacia)Biología molecular (Farmacia)2302 BioquímicaThe role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modification of cysteine residues has been shown to be of particular importance due to the functional relevance of many of them. In this review, we focus on the modification of the cysteine thiol by incorporation of a NO moiety (S-nitrosylation) or of a glutathione moiety (S-glutathionylation). Both modifications are produced by different reactions induced by nitric oxide-related species. We discuss the differences and similarities of both modifications, and their relationships, in regard to the biochemical mechanisms that produce them, including the enzymatic activities that may catalyze some of them and their subcellular compartmentalization. Even when biochemical knowledge is one step ahead of the demonstration of their pathophysiological relevance, we also describe the potential role of both modifications in several processes in which both post-translational modifications are involved. © 2007 European Society of Cardiology. Published by Elsevier B.V. All rights reserved.Universidad Complutense de Madrid20072007-07-1520072007-07-15journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/102745reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1027452026-06-02T12:44:21Z
dc.title.none.fl_str_mv Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
title Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
spellingShingle Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
Martínez Ruiz, Antonio
577.1
577.2
Nitric oxide
Post-translational modifications
Oxidative stress
Glutathione
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
title_short Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
title_full Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
title_fullStr Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
title_full_unstemmed Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
title_sort Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
dc.creator.none.fl_str_mv Martínez Ruiz, Antonio
Lamas, Santiago
author Martínez Ruiz, Antonio
author_facet Martínez Ruiz, Antonio
Lamas, Santiago
author_role author
author2 Lamas, Santiago
author2_role author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
577.2
Nitric oxide
Post-translational modifications
Oxidative stress
Glutathione
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
topic 577.1
577.2
Nitric oxide
Post-translational modifications
Oxidative stress
Glutathione
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
description The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modification of cysteine residues has been shown to be of particular importance due to the functional relevance of many of them. In this review, we focus on the modification of the cysteine thiol by incorporation of a NO moiety (S-nitrosylation) or of a glutathione moiety (S-glutathionylation). Both modifications are produced by different reactions induced by nitric oxide-related species. We discuss the differences and similarities of both modifications, and their relationships, in regard to the biochemical mechanisms that produce them, including the enzymatic activities that may catalyze some of them and their subcellular compartmentalization. Even when biochemical knowledge is one step ahead of the demonstration of their pathophysiological relevance, we also describe the potential role of both modifications in several processes in which both post-translational modifications are involved. © 2007 European Society of Cardiology. Published by Elsevier B.V. All rights reserved.
publishDate 2007
dc.date.none.fl_str_mv 2007
2007-07-15
2007
2007-07-15
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/102745
url https://hdl.handle.net/20.500.14352/102745
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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