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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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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. |
format | Online Article Text |
id | pubmed-9917916 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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