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, D.A., Marmisollé, W.A., Tomasina, F., Demicheli, V., Portela, M., Radi, R., Murgida, D.H.
Formato: JOUR
Materias:
Amino acids
Bins
Cell death
Cell membranes
Lipids
Mitochondria
Oxidation
Phospholipids
Proteins
Activated proteins
Cationic proteins
Membrane components
Methionine oxidation
Mitochondrial membranes
Phosphatidylcholine
Phosphatidylethanolamine
Zwitterionic lipids
C (programming language)
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_20416520_v6_n1_p705_Capdevila
record_format dspace
spelling todo:paper_20416520_v6_n1_p705_Capdevila2023-10-03T16:37:57Z Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis Capdevila, D.A. Marmisollé, W.A. Tomasina, F. Demicheli, V. Portela, M. Radi, R. Murgida, D.H. Amino acids Bins Cell death Cell membranes Lipids Mitochondria Oxidation Phospholipids Proteins Activated proteins Cationic proteins Membrane components Methionine oxidation Mitochondrial membranes Phosphatidylcholine Phosphatidylethanolamine Zwitterionic lipids C (programming language) 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 H 2 O 2 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 H 2 O 2 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. This journal is © The Royal Society of Chemistry. Fil:Capdevila, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marmisollé, W.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Amino acids
Bins
Cell death
Cell membranes
Lipids
Mitochondria
Oxidation
Phospholipids
Proteins
Activated proteins
Cationic proteins
Membrane components
Methionine oxidation
Mitochondrial membranes
Phosphatidylcholine
Phosphatidylethanolamine
Zwitterionic lipids
C (programming language)
spellingShingle Amino acids
Bins
Cell death
Cell membranes
Lipids
Mitochondria
Oxidation
Phospholipids
Proteins
Activated proteins
Cationic proteins
Membrane components
Methionine oxidation
Mitochondrial membranes
Phosphatidylcholine
Phosphatidylethanolamine
Zwitterionic lipids
C (programming language)
Capdevila, D.A.
Marmisollé, W.A.
Tomasina, F.
Demicheli, V.
Portela, M.
Radi, R.
Murgida, D.H.
Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: Potential implications for apoptosis
topic_facet Amino acids
Bins
Cell death
Cell membranes
Lipids
Mitochondria
Oxidation
Phospholipids
Proteins
Activated proteins
Cationic proteins
Membrane components
Methionine oxidation
Mitochondrial membranes
Phosphatidylcholine
Phosphatidylethanolamine
Zwitterionic lipids
C (programming language)
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 H 2 O 2 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 H 2 O 2 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. This journal is © The Royal Society of Chemistry.
format JOUR
author Capdevila, D.A.
Marmisollé, W.A.
Tomasina, F.
Demicheli, V.
Portela, M.
Radi, R.
Murgida, D.H.
author_facet Capdevila, D.A.
Marmisollé, W.A.
Tomasina, F.
Demicheli, V.
Portela, M.
Radi, R.
Murgida, D.H.
author_sort Capdevila, D.A.
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
url http://hdl.handle.net/20.500.12110/paper_20416520_v6_n1_p705_Capdevila
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