1. Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
- Author
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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, Puyet Catalina, Antonio, 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, and Puyet Catalina, Antonio
- Abstract
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 wellestablished 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., Ramón Areces Foundation., Depto. de Bioquímica y Biología Molecular, Fac. de Veterinaria, TRUE, pub
- Published
- 2024