Amyloid-β peptide binds to cytochrome C oxidase subunit 1.

Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amylo...

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Autores principales:	Luis Fernando Hernandez-Zimbron, Jose Luna-Muñoz, Raul Mena, Ricardo Vazquez-Ramirez, Carlos Kubli-Garfias, David H Cribbs, Karen Manoutcharian, Goar Gevorkian
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fff283e4831e4f22be5c18ec56fddbbe
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spelling	oai:doaj.org-article:fff283e4831e4f22be5c18ec56fddbbe2021-11-18T07:08:08ZAmyloid-β peptide binds to cytochrome C oxidase subunit 1.1932-620310.1371/journal.pone.0042344https://doaj.org/article/fff283e4831e4f22be5c18ec56fddbbe2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22927926/?tool=EBIhttps://doaj.org/toc/1932-6203Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.Luis Fernando Hernandez-ZimbronJose Luna-MuñozRaul MenaRicardo Vazquez-RamirezCarlos Kubli-GarfiasDavid H CribbsKaren ManoutcharianGoar GevorkianPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e42344 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Luis Fernando Hernandez-Zimbron Jose Luna-Muñoz Raul Mena Ricardo Vazquez-Ramirez Carlos Kubli-Garfias David H Cribbs Karen Manoutcharian Goar Gevorkian Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
description	Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.
format	article
author	Luis Fernando Hernandez-Zimbron Jose Luna-Muñoz Raul Mena Ricardo Vazquez-Ramirez Carlos Kubli-Garfias David H Cribbs Karen Manoutcharian Goar Gevorkian
author_facet	Luis Fernando Hernandez-Zimbron Jose Luna-Muñoz Raul Mena Ricardo Vazquez-Ramirez Carlos Kubli-Garfias David H Cribbs Karen Manoutcharian Goar Gevorkian
author_sort	Luis Fernando Hernandez-Zimbron
title	Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
title_short	Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
title_full	Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
title_fullStr	Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
title_full_unstemmed	Amyloid-β peptide binds to cytochrome C oxidase subunit 1.
title_sort	amyloid-β peptide binds to cytochrome c oxidase subunit 1.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fff283e4831e4f22be5c18ec56fddbbe
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Amyloid-β peptide binds to cytochrome C oxidase subunit 1.

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