%0 Journal Article
%A Sánchez-Jaut, Sandra 
%A Pérez-Benavente, Susana 
%A Abad, Paloma 
%A Méndez Cuadro, Darío 
%A Puyet Catalina, Antonio
%A Díez Martín, Amalia
%A Galicia Poblet, Gonzalo 
%A Gómez Domínguez, Elena 
%A Moran Jiménez, María J. 
%A Bautista Santa Cruz, José Manuel
%A Azcárate, Isabel G. 
%T Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis
%D 2023
%@ 1422-0067
%U https://hdl.handle.net/20.500.14352/94131
%X 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.
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