Sánchez-Jaut, SandraPérez-Benavente, SusanaAbad, PalomaMéndez-Cuadro, DaríoPuyet, AntonioDiez, AmaliaGalicia-Poblet, GonzaloGómez-Domínguez, ElenaMoran-Jiménez, María JBautista, José MAzcárate, Isabel G2024-01-312024-01-312023-02-02Sánchez-Jaut S, Pérez-Benavente S, Abad P, Méndez-Cuadro D, Puyet A, Diez A, Galicia-Poblet G, Gómez-Domínguez E, Moran-Jiménez MJ, Bautista JM, Azcárate IG. Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis. Int J Mol Sci. 2023 Feb 2;24(3):2922. doi: 10.3390/ijms24032922. PMID: 36769239; PMCID: PMC9917916.1661-6596https://hdl.handle.net/10115/29339Iron 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.engAtribución 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/4-hydroxynonenal (HNE)Hfe−/− mouseerythrocyte membrane proteinshemochromatosislipid peroxidationoxidative stressprotein modificationinfo:eu-repo/semantics/article10.3390/ijms24032922.info:eu-repo/semantics/openAccess