English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/95810
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 18 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome

Autor García-Heredia, José M. ; Díaz-Moreno, Irene ; Díaz-Quintana, Antonio; Orzáez, Mar; Navarro, José A. ; Hervás, Manuel ; Rosa, Miguel A. de la
Palabras clave Mitochondrial respiration
Electron transfer
Cytochrome c oxidase
Tyrosine nitration
Caspase-9 activation
Post-translational modification
RNOS
Cytochrome c
Apoptosome
Fecha de publicación 2012
EditorElsevier
Citación FEBS Letters 586: 154- 158 (2012)
ResumenUnder nitroxidative stress, a minor fraction of cytochrome c can be modified by tyrosine nitration. Here we analyze the specific effect of nitration of tyrosines 46 and 48 on the dual role of cytochrome c in cell survival and cell death. Our findings reveal that nitration of these two solvent-exposed residues has a negligible effect on the rate of electron transfer from cytochrome c to cytochrome c oxidase, but impairs the ability of the heme protein to activate caspase-9 by assembling a non-functional apoptosome. It seems that cytochrome c nitration under cellular stress counteracts apoptosis in light of the small amount of modified protein. We conclude that other changes such as increased peroxidase activity prevail and allow the execution of apoptosis. © 2011 Elsevier Ltd. All rights reserved.
URI http://hdl.handle.net/10261/95810
DOI10.1016/j.febslet.2011.12.007
Identificadoresdoi: 10.1016/j.febslet.2011.12.007
issn: 0014-5793
Aparece en las colecciones: (IBVF) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
1-s2.0-S0014579311008787-main.pdf423,91 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.