| Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome. | |
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MedLine Citation:
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PMID: 22192356 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Under 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. |
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Authors:
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José M García-Heredia; Irene Díaz-Moreno; Antonio Díaz-Quintana; Mar Orzáez; José A Navarro; Manuel Hervás; Miguel A De la Rosa |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-12-16 |
Journal Detail:
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Title: FEBS letters Volume: - ISSN: 1873-3468 ISO Abbreviation: - Publication Date: 2011 Dec |
Date Detail:
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Created Date: 2011-12-23 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier B.V. |
Affiliation:
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Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla-CSIC, Avda. Americo Vespucio 49, Sevilla 41092, Spain. |
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