Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis

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...

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Autores principales: Capdevila, Daiana Andrea, Marmisollé, Waldemar Alejandro, Tomasina, Florencia, Demicheli, Verónica, Portela, Magdalena, Radi, Rafael, Murgida, Daniel Horacio
Formato: Articulo
Lenguaje:Inglés
Publicado: 2014
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104719
http://hdl.handle.net/11336/5476
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id I19-R120-10915-104719
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Cytochrome c
Apoptosis
Hydrogen peroxide
spellingShingle Química
Cytochrome c
Apoptosis
Hydrogen peroxide
Capdevila, Daiana Andrea
Marmisollé, Waldemar Alejandro
Tomasina, Florencia
Demicheli, Verónica
Portela, Magdalena
Radi, Rafael
Murgida, Daniel Horacio
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis
topic_facet Química
Cytochrome c
Apoptosis
Hydrogen peroxide
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.
format Articulo
Articulo
author Capdevila, Daiana Andrea
Marmisollé, Waldemar Alejandro
Tomasina, Florencia
Demicheli, Verónica
Portela, Magdalena
Radi, Rafael
Murgida, Daniel Horacio
author_facet Capdevila, Daiana Andrea
Marmisollé, Waldemar Alejandro
Tomasina, Florencia
Demicheli, Verónica
Portela, Magdalena
Radi, Rafael
Murgida, Daniel Horacio
author_sort Capdevila, Daiana Andrea
title Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis
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
publishDate 2014
url http://sedici.unlp.edu.ar/handle/10915/104719
http://hdl.handle.net/11336/5476
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