Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis
- Autores
- Capdevila, Daiana Andrea; Marmisollé, Waldemar Alejandro; Tomasina, Florencia; Demicheli, Verónica; Portela, Magdalena; Radi, Rafael; Murgida, Daniel Horacio
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore,in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H2O2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H2O2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL.
Fil: Capdevila, Daiana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; Argentina
Fil: Marmisollé, Waldemar Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; Argentina
Fil: Tomasina, Florencia. Universidad de la Republica. Facultad de Medicina; Uruguay
Fil: Demicheli, Verónica. Universidad de la Republica. Facultad de Química y Facultad de Ciencias; Uruguay
Fil: Portela, Magdalena . Instituto Pasteur de Montevideo; Uruguay
Fil: Radi, Rafael . Universidad de la Republica. Facultad de Química y Facultad de Ciencias; Uruguay
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina - Materia
-
CYTOCHROME C
APOPTOSIS
HYDROGEN PEROXIDE - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/5476
Ver los metadatos del registro completo
id |
CONICETDig_711b672e3945d6430e449d2ea72483df |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/5476 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosisCapdevila, Daiana AndreaMarmisollé, Waldemar AlejandroTomasina, FlorenciaDemicheli, VerónicaPortela, Magdalena Radi, Rafael Murgida, Daniel HoracioCYTOCHROME CAPOPTOSISHYDROGEN PEROXIDEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore,in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H2O2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H2O2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL.Fil: Capdevila, Daiana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; ArgentinaFil: Marmisollé, Waldemar Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; ArgentinaFil: Tomasina, Florencia. Universidad de la Republica. Facultad de Medicina; UruguayFil: Demicheli, Verónica. Universidad de la Republica. Facultad de Química y Facultad de Ciencias; UruguayFil: Portela, Magdalena . Instituto Pasteur de Montevideo; UruguayFil: Radi, Rafael . Universidad de la Republica. Facultad de Química y Facultad de Ciencias; UruguayFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; ArgentinaRoyal Society of Chemistry2014-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/5476Capdevila, Daiana Andrea; Marmisollé, Waldemar Alejandro; Tomasina, Florencia; Demicheli, Verónica; Portela, Magdalena ; et al.; Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis; Royal Society of Chemistry; Chemical Science; 6; 1; 1-9-2014; 705-7132041-6520enginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/SC/c4sc02181ainfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1039/c4sc02181ainfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:53:08Zoai:ri.conicet.gov.ar:11336/5476instacron: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 09:53:08.766CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
title |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
spellingShingle |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis Capdevila, Daiana Andrea CYTOCHROME C APOPTOSIS HYDROGEN PEROXIDE |
title_short |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
title_full |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
title_fullStr |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
title_full_unstemmed |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
title_sort |
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis |
dc.creator.none.fl_str_mv |
Capdevila, Daiana Andrea Marmisollé, Waldemar Alejandro Tomasina, Florencia Demicheli, Verónica Portela, Magdalena Radi, Rafael Murgida, Daniel Horacio |
author |
Capdevila, Daiana Andrea |
author_facet |
Capdevila, Daiana Andrea Marmisollé, Waldemar Alejandro Tomasina, Florencia Demicheli, Verónica Portela, Magdalena Radi, Rafael Murgida, Daniel Horacio |
author_role |
author |
author2 |
Marmisollé, Waldemar Alejandro Tomasina, Florencia Demicheli, Verónica Portela, Magdalena Radi, Rafael Murgida, Daniel Horacio |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
CYTOCHROME C APOPTOSIS HYDROGEN PEROXIDE |
topic |
CYTOCHROME C APOPTOSIS HYDROGEN PEROXIDE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore,in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H2O2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H2O2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL. Fil: Capdevila, Daiana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; Argentina Fil: Marmisollé, Waldemar Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Departamento de Ciencias Exactas; Argentina Fil: Tomasina, Florencia. Universidad de la Republica. Facultad de Medicina; Uruguay Fil: Demicheli, Verónica. Universidad de la Republica. Facultad de Química y Facultad de Ciencias; Uruguay Fil: Portela, Magdalena . Instituto Pasteur de Montevideo; Uruguay Fil: Radi, Rafael . Universidad de la Republica. Facultad de Química y Facultad de Ciencias; Uruguay Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina |
description |
Cytochrome c (Cyt-c) has been previously shown to participate in cardiolipin (CL) oxidation and, therefore,in mitochondrial membrane permeabilization during the early events of apoptosis. The gain in this function has been ascribed to specific CL/Cyt-c interactions. Here we report that the cationic protein Cyt-c is also able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE), through the mediation of phosphate anions that bind specifically to amino groups in the surfaces of protein and model membranes. In these complexes, Cyt-c reacts efficiently with H2O2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. The modified protein is stable and presents significantly enhanced peroxidatic activity. Based on these results, we postulate that the rise of H2O2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. As the activated protein is a chemically stable species, it can potentially bind and oxidize important targets, such as CL. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-09-01 |
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/11336/5476 Capdevila, Daiana Andrea; Marmisollé, Waldemar Alejandro; Tomasina, Florencia; Demicheli, Verónica; Portela, Magdalena ; et al.; Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis; Royal Society of Chemistry; Chemical Science; 6; 1; 1-9-2014; 705-713 2041-6520 |
url |
http://hdl.handle.net/11336/5476 |
identifier_str_mv |
Capdevila, Daiana Andrea; Marmisollé, Waldemar Alejandro; Tomasina, Florencia; Demicheli, Verónica; Portela, Magdalena ; et al.; Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis; Royal Society of Chemistry; Chemical Science; 6; 1; 1-9-2014; 705-713 2041-6520 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/SC/c4sc02181a info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.1039/c4sc02181a |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Royal Society of Chemistry |
publisher.none.fl_str_mv |
Royal Society of Chemistry |
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_ |
1844613626217889792 |
score |
13.070432 |