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Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis

Iron overload caused by hereditary hemochromatosis (HH) increases free reactive oxygen species that, in turn, induce lipid peroxidation. Its 4-hydroxynonenal (HNE) by-product is a well-established marker of lipid peroxidation since it reacts with accessible proteins with deleterious consequences. In...

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Autores principales: Sánchez-Jaut, Sandra, Pérez-Benavente, Susana, Abad, Paloma, Méndez-Cuadro, Darío, Puyet, Antonio, Diez, Amalia, Galicia-Poblet, Gonzalo, Gómez-Domínguez, Elena, Moran-Jiménez, María J., Bautista, José M., Azcárate, Isabel G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9917916/
https://www.ncbi.nlm.nih.gov/pubmed/36769239
http://dx.doi.org/10.3390/ijms24032922
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author Sánchez-Jaut, Sandra
Pérez-Benavente, Susana
Abad, Paloma
Méndez-Cuadro, Darío
Puyet, Antonio
Diez, Amalia
Galicia-Poblet, Gonzalo
Gómez-Domínguez, Elena
Moran-Jiménez, María J.
Bautista, José M.
Azcárate, Isabel G.
author_facet Sánchez-Jaut, Sandra
Pérez-Benavente, Susana
Abad, Paloma
Méndez-Cuadro, Darío
Puyet, Antonio
Diez, Amalia
Galicia-Poblet, Gonzalo
Gómez-Domínguez, Elena
Moran-Jiménez, María J.
Bautista, José M.
Azcárate, Isabel G.
author_sort Sánchez-Jaut, Sandra
collection PubMed
description Iron overload caused by hereditary hemochromatosis (HH) increases free reactive oxygen species that, in turn, induce lipid peroxidation. Its 4-hydroxynonenal (HNE) by-product is a well-established marker of lipid peroxidation since it reacts with accessible proteins with deleterious consequences. Indeed, elevated levels of HNE are often detected in a wide variety of human diseases related to oxidative stress. Here, we evaluated HNE-modified proteins in the membrane of erythrocytes from HH patients and in organs of Hfe(−/−) male and female mice, a mouse model of HH. For this purpose, we used one- and two-dimensional gel electrophoresis, immunoblotting and MALDI-TOF/TOF analysis. We identified cytoskeletal membrane proteins and membrane receptors of erythrocytes bound to HNE exclusively in HH patients. Furthermore, kidney and brain of Hfe(−/−) mice contained more HNE-adducted protein than healthy controls. Our results identified main HNE-modified proteins suggesting that HH favours preferred protein targets for oxidation by HNE.
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spelling pubmed-99179162023-02-11 Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis Sánchez-Jaut, Sandra Pérez-Benavente, Susana Abad, Paloma Méndez-Cuadro, Darío Puyet, Antonio Diez, Amalia Galicia-Poblet, Gonzalo Gómez-Domínguez, Elena Moran-Jiménez, María J. Bautista, José M. Azcárate, Isabel G. Int J Mol Sci Article Iron overload caused by hereditary hemochromatosis (HH) increases free reactive oxygen species that, in turn, induce lipid peroxidation. Its 4-hydroxynonenal (HNE) by-product is a well-established marker of lipid peroxidation since it reacts with accessible proteins with deleterious consequences. Indeed, elevated levels of HNE are often detected in a wide variety of human diseases related to oxidative stress. Here, we evaluated HNE-modified proteins in the membrane of erythrocytes from HH patients and in organs of Hfe(−/−) male and female mice, a mouse model of HH. For this purpose, we used one- and two-dimensional gel electrophoresis, immunoblotting and MALDI-TOF/TOF analysis. We identified cytoskeletal membrane proteins and membrane receptors of erythrocytes bound to HNE exclusively in HH patients. Furthermore, kidney and brain of Hfe(−/−) mice contained more HNE-adducted protein than healthy controls. Our results identified main HNE-modified proteins suggesting that HH favours preferred protein targets for oxidation by HNE. MDPI 2023-02-02 /pmc/articles/PMC9917916/ /pubmed/36769239 http://dx.doi.org/10.3390/ijms24032922 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sánchez-Jaut, Sandra
Pérez-Benavente, Susana
Abad, Paloma
Méndez-Cuadro, Darío
Puyet, Antonio
Diez, Amalia
Galicia-Poblet, Gonzalo
Gómez-Domínguez, Elena
Moran-Jiménez, María J.
Bautista, José M.
Azcárate, Isabel G.
Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title_full Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title_fullStr Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title_full_unstemmed Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title_short Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
title_sort protein susceptibility to peroxidation by 4-hydroxynonenal in hereditary hemochromatosis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9917916/
https://www.ncbi.nlm.nih.gov/pubmed/36769239
http://dx.doi.org/10.3390/ijms24032922
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