A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.

The β-amyloid precursor protein (APP), which is a key player in Alzheimer's disease, was recently reported to possess an Fe(II) binding site within its E2 domain which exhibits ferroxidase activity [Duce et al. 2010, Cell 142: 857]. The putative ligands of this site were compared to those in th...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Kourosh Honarmand Ebrahimi, Peter-Leon Hagedoorn, Wilfred R Hagen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0324eaafbc6841d6b00be1d9262111e0
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0324eaafbc6841d6b00be1d9262111e0
record_format	dspace
spelling	oai:doaj.org-article:0324eaafbc6841d6b00be1d9262111e02021-11-18T07:08:45ZA synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.1932-620310.1371/journal.pone.0040287https://doaj.org/article/0324eaafbc6841d6b00be1d9262111e02012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22916096/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The β-amyloid precursor protein (APP), which is a key player in Alzheimer's disease, was recently reported to possess an Fe(II) binding site within its E2 domain which exhibits ferroxidase activity [Duce et al. 2010, Cell 142: 857]. The putative ligands of this site were compared to those in the ferroxidase site of ferritin. The activity was indirectly measured using transferrin, which scavenges the Fe(III) product of the reaction. A 22-residue synthetic peptide, named FD1, with the putative ferroxidase site of APP, and the E2 domain of APP were each reported to exhibit 40% of the ferroxidase activity of APP and of ceruloplasmin. It was also claimed that the ferroxidase activity of APP is inhibited by Zn(II) just as in ferritin. We measured the ferroxidase activity indirectly (i) by the incorporation of the Fe(III) product of the ferroxidase reaction into transferrin and directly (ii) by monitoring consumption of the substrate molecular oxygen. The results with the FD1 peptide were compared to the established ferroxidase activities of human H-chain ferritin and of ceruloplasmin. For FD1 we observed no activity above the background of non-enzymatic Fe(II) oxidation by molecular oxygen. Zn(II) binds to transferrin and diminishes its Fe(III) incorporation capacity and rate but it does not specifically bind to a putative ferroxidase site of FD1. Based on these results, and on comparison of the putative ligands of the ferroxidase site of APP with those of ferritin, we conclude that the previously reported results for ferroxidase activity of FD1 and - by implication - of APP should be re-evaluated.Kourosh Honarmand EbrahimiPeter-Leon HagedoornWilfred R HagenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e40287 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kourosh Honarmand Ebrahimi Peter-Leon Hagedoorn Wilfred R Hagen A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
description	The β-amyloid precursor protein (APP), which is a key player in Alzheimer's disease, was recently reported to possess an Fe(II) binding site within its E2 domain which exhibits ferroxidase activity [Duce et al. 2010, Cell 142: 857]. The putative ligands of this site were compared to those in the ferroxidase site of ferritin. The activity was indirectly measured using transferrin, which scavenges the Fe(III) product of the reaction. A 22-residue synthetic peptide, named FD1, with the putative ferroxidase site of APP, and the E2 domain of APP were each reported to exhibit 40% of the ferroxidase activity of APP and of ceruloplasmin. It was also claimed that the ferroxidase activity of APP is inhibited by Zn(II) just as in ferritin. We measured the ferroxidase activity indirectly (i) by the incorporation of the Fe(III) product of the ferroxidase reaction into transferrin and directly (ii) by monitoring consumption of the substrate molecular oxygen. The results with the FD1 peptide were compared to the established ferroxidase activities of human H-chain ferritin and of ceruloplasmin. For FD1 we observed no activity above the background of non-enzymatic Fe(II) oxidation by molecular oxygen. Zn(II) binds to transferrin and diminishes its Fe(III) incorporation capacity and rate but it does not specifically bind to a putative ferroxidase site of FD1. Based on these results, and on comparison of the putative ligands of the ferroxidase site of APP with those of ferritin, we conclude that the previously reported results for ferroxidase activity of FD1 and - by implication - of APP should be re-evaluated.
format	article
author	Kourosh Honarmand Ebrahimi Peter-Leon Hagedoorn Wilfred R Hagen
author_facet	Kourosh Honarmand Ebrahimi Peter-Leon Hagedoorn Wilfred R Hagen
author_sort	Kourosh Honarmand Ebrahimi
title	A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
title_short	A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
title_full	A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
title_fullStr	A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
title_full_unstemmed	A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.
title_sort	synthetic peptide with the putative iron binding motif of amyloid precursor protein (app) does not catalytically oxidize iron.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0324eaafbc6841d6b00be1d9262111e0
work_keys_str_mv	AT kouroshhonarmandebrahimi asyntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron AT peterleonhagedoorn asyntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron AT wilfredrhagen asyntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron AT kouroshhonarmandebrahimi syntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron AT peterleonhagedoorn syntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron AT wilfredrhagen syntheticpeptidewiththeputativeironbindingmotifofamyloidprecursorproteinappdoesnotcatalyticallyoxidizeiron
_version_	1718423832909316096

A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron.

Ejemplares similares