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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MDPI AG
2023-02-01
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author | Sandra Sánchez-Jaut Susana Pérez-Benavente Paloma Abad Darío Méndez-Cuadro Antonio Puyet Amalia Diez Gonzalo Galicia-Poblet Elena Gómez-Domínguez María J. Moran-Jiménez José M. Bautista Isabel G. Azcárate |
author_facet | Sandra Sánchez-Jaut Susana Pérez-Benavente Paloma Abad Darío Méndez-Cuadro Antonio Puyet Amalia Diez Gonzalo Galicia-Poblet Elena Gómez-Domínguez María J. Moran-Jiménez José M. Bautista Isabel G. Azcárate |
author_sort | Sandra Sánchez-Jaut |
collection | DOAJ |
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<sup>−/−</sup> 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<sup>−/−</sup> 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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issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-11T09:39:38Z |
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spelling | doaj.art-2b79ecf09184442ea410407afce789352023-11-16T17:04:19ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-02-01243292210.3390/ijms24032922Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary HemochromatosisSandra Sánchez-Jaut0Susana Pérez-Benavente1Paloma Abad2Darío Méndez-Cuadro3Antonio Puyet4Amalia Diez5Gonzalo Galicia-Poblet6Elena Gómez-Domínguez7María J. Moran-Jiménez8José M. Bautista9Isabel G. Azcárate10Department of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainDepartment of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainDepartment of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainAnalytical Chemistry and Biomedicine Group, School of Exact and Natural Sciences, San Pablo Campus, University of Cartagena, Cartagena 130014, ColombiaDepartment of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainDepartment of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainPediatric Digestive Service, Guadalajara University Hospital, 19002 Guadalajara, SpainResearch Institute Hospital 12 de Octubre, 28041 Madrid, SpainResearch Institute Hospital 12 de Octubre, 28041 Madrid, SpainDepartment of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, SpainDepartment of Medical Specialties and Public Health, Rey Juan Carlos University, 28922 Madrid, SpainIron 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<sup>−/−</sup> 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<sup>−/−</sup> 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.https://www.mdpi.com/1422-0067/24/3/2922hemochromatosisoxidative stresslipid peroxidation4-hydroxynonenal (HNE)Hfe<sup>−/−</sup> mouseerythrocyte membrane proteins |
spellingShingle | Sandra Sánchez-Jaut Susana Pérez-Benavente Paloma Abad Darío Méndez-Cuadro Antonio Puyet Amalia Diez Gonzalo Galicia-Poblet Elena Gómez-Domínguez María J. Moran-Jiménez José M. Bautista Isabel G. Azcárate Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis International Journal of Molecular Sciences hemochromatosis oxidative stress lipid peroxidation 4-hydroxynonenal (HNE) Hfe<sup>−/−</sup> mouse erythrocyte membrane proteins |
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 | hemochromatosis oxidative stress lipid peroxidation 4-hydroxynonenal (HNE) Hfe<sup>−/−</sup> mouse erythrocyte membrane proteins |
url | https://www.mdpi.com/1422-0067/24/3/2922 |
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