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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| Veröffentlicht in: | International journal of molecular sciences 2023-02, Vol.24 (3), p.2922 |
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| creator | 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 |
| 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. |
| doi_str_mv | 10.3390/ijms24032922 |
| format | Article |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms24032922</identifier><identifier>PMID: 36769239</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>4-Hydroxynonenal ; Aldehydes - metabolism ; Animals ; Apoptosis ; Cardiovascular disease ; Cell cycle ; Cell division ; Cytoskeleton ; Diabetes ; Electrophoresis ; Erythrocytes ; Female ; Females ; Gel electrophoresis ; Glycoproteins ; Heart ; Hemochromatosis ; Hemochromatosis - genetics ; Hemochromatosis Protein - genetics ; Hemochromatosis Protein - metabolism ; Hemoglobin ; Homeostasis ; Humans ; Immunoblotting ; Iron ; Iron Overload ; Lipid Peroxidation ; Lipids ; Liver ; Male ; Males ; Membrane proteins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Mice ; Mutation ; Oxidation ; Oxidative stress ; Parkinson's disease ; Patients ; Peptides ; Proteins ; Reactive oxygen species ; Toxicity</subject><ispartof>International journal of molecular sciences, 2023-02, Vol.24 (3), p.2922</ispartof><rights>2023 by the authors. 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/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-60a76626e84ae29b17332298e21c09a2189bf0868896bf7c750dc8a4b71a2f463</citedby><cites>FETCH-LOGICAL-c412t-60a76626e84ae29b17332298e21c09a2189bf0868896bf7c750dc8a4b71a2f463</cites><orcidid>0000-0002-0072-459X ; 0000-0001-9369-6139 ; 0000-0003-4545-1254 ; 0000-0001-8926-881X ; 0000-0002-3905-6859</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9917916/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9917916/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27915,27916,53782,53784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36769239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sánchez-Jaut, Sandra</creatorcontrib><creatorcontrib>Pérez-Benavente, Susana</creatorcontrib><creatorcontrib>Abad, Paloma</creatorcontrib><creatorcontrib>Méndez-Cuadro, Darío</creatorcontrib><creatorcontrib>Puyet, Antonio</creatorcontrib><creatorcontrib>Diez, Amalia</creatorcontrib><creatorcontrib>Galicia-Poblet, Gonzalo</creatorcontrib><creatorcontrib>Gómez-Domínguez, Elena</creatorcontrib><creatorcontrib>Moran-Jiménez, María J</creatorcontrib><creatorcontrib>Bautista, José M</creatorcontrib><creatorcontrib>Azcárate, Isabel G</creatorcontrib><title>Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><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.</description><subject>4-Hydroxynonenal</subject><subject>Aldehydes - metabolism</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Cardiovascular disease</subject><subject>Cell cycle</subject><subject>Cell division</subject><subject>Cytoskeleton</subject><subject>Diabetes</subject><subject>Electrophoresis</subject><subject>Erythrocytes</subject><subject>Female</subject><subject>Females</subject><subject>Gel electrophoresis</subject><subject>Glycoproteins</subject><subject>Heart</subject><subject>Hemochromatosis</subject><subject>Hemochromatosis - genetics</subject><subject>Hemochromatosis Protein - genetics</subject><subject>Hemochromatosis Protein - metabolism</subject><subject>Hemoglobin</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Iron</subject><subject>Iron Overload</subject><subject>Lipid Peroxidation</subject><subject>Lipids</subject><subject>Liver</subject><subject>Male</subject><subject>Males</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Mice</subject><subject>Mutation</subject><subject>Oxidation</subject><subject>Oxidative stress</subject><subject>Parkinson's disease</subject><subject>Patients</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Reactive oxygen species</subject><subject>Toxicity</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkU1LxDAQhoMofqzePEvBiweryaSbNBdBFnWFBQUVvIW0TTVL26xJKvbfG3VdVk8zzDzzMjMvQocEn1Eq8LmZtx4yTEEAbKBdkgGkGDO-uZbvoD3v5xgDhbHYRjuUcSaAil30fO9s0KZLHnpf6kUwhWlMGJJgk3vt7IepVDC2S4ohydLpUMXS0NlOd6pJ4tRUO12ZoNwQ09aWr862Klhv_D7aqlXj9cEyjtDT9dXjZJrO7m5uJ5eztMwIhJRhxRkDpvNMaRAF4ZQCiFwDKbFQQHJR1DhneS5YUfOSj3FV5iorOFFQZ4yO0MWP7qIvWl2VugtONXLhTBu3klYZ-bfTmVf5Yt-lEIQL8iVwshRw9q3XPsjWxFc0jeq07b0EzscMxoRDRI__oXPbu_iKbyqLarngkTr9oUpnvXe6Xi1DsPyyTK5bFvGj9QNW8K9H9BMhjZMr</recordid><startdate>20230202</startdate><enddate>20230202</enddate><creator>Sánchez-Jaut, Sandra</creator><creator>Pérez-Benavente, Susana</creator><creator>Abad, Paloma</creator><creator>Méndez-Cuadro, Darío</creator><creator>Puyet, Antonio</creator><creator>Diez, Amalia</creator><creator>Galicia-Poblet, Gonzalo</creator><creator>Gómez-Domínguez, Elena</creator><creator>Moran-Jiménez, María J</creator><creator>Bautista, José M</creator><creator>Azcárate, Isabel G</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0072-459X</orcidid><orcidid>https://orcid.org/0000-0001-9369-6139</orcidid><orcidid>https://orcid.org/0000-0003-4545-1254</orcidid><orcidid>https://orcid.org/0000-0001-8926-881X</orcidid><orcidid>https://orcid.org/0000-0002-3905-6859</orcidid></search><sort><creationdate>20230202</creationdate><title>Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis</title><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></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-60a76626e84ae29b17332298e21c09a2189bf0868896bf7c750dc8a4b71a2f463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>4-Hydroxynonenal</topic><topic>Aldehydes - metabolism</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Cardiovascular disease</topic><topic>Cell cycle</topic><topic>Cell division</topic><topic>Cytoskeleton</topic><topic>Diabetes</topic><topic>Electrophoresis</topic><topic>Erythrocytes</topic><topic>Female</topic><topic>Females</topic><topic>Gel electrophoresis</topic><topic>Glycoproteins</topic><topic>Heart</topic><topic>Hemochromatosis</topic><topic>Hemochromatosis - genetics</topic><topic>Hemochromatosis Protein - genetics</topic><topic>Hemochromatosis Protein - metabolism</topic><topic>Hemoglobin</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Iron</topic><topic>Iron Overload</topic><topic>Lipid Peroxidation</topic><topic>Lipids</topic><topic>Liver</topic><topic>Male</topic><topic>Males</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Mice</topic><topic>Mutation</topic><topic>Oxidation</topic><topic>Oxidative stress</topic><topic>Parkinson's disease</topic><topic>Patients</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Reactive oxygen species</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sánchez-Jaut, Sandra</creatorcontrib><creatorcontrib>Pérez-Benavente, Susana</creatorcontrib><creatorcontrib>Abad, Paloma</creatorcontrib><creatorcontrib>Méndez-Cuadro, Darío</creatorcontrib><creatorcontrib>Puyet, Antonio</creatorcontrib><creatorcontrib>Diez, Amalia</creatorcontrib><creatorcontrib>Galicia-Poblet, Gonzalo</creatorcontrib><creatorcontrib>Gómez-Domínguez, Elena</creatorcontrib><creatorcontrib>Moran-Jiménez, María J</creatorcontrib><creatorcontrib>Bautista, José M</creatorcontrib><creatorcontrib>Azcárate, Isabel G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sánchez-Jaut, Sandra</au><au>Pérez-Benavente, Susana</au><au>Abad, Paloma</au><au>Méndez-Cuadro, Darío</au><au>Puyet, Antonio</au><au>Diez, Amalia</au><au>Galicia-Poblet, Gonzalo</au><au>Gómez-Domínguez, Elena</au><au>Moran-Jiménez, María J</au><au>Bautista, José M</au><au>Azcárate, Isabel G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2023-02-02</date><risdate>2023</risdate><volume>24</volume><issue>3</issue><spage>2922</spage><pages>2922-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><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 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.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36769239</pmid><doi>10.3390/ijms24032922</doi><orcidid>https://orcid.org/0000-0002-0072-459X</orcidid><orcidid>https://orcid.org/0000-0001-9369-6139</orcidid><orcidid>https://orcid.org/0000-0003-4545-1254</orcidid><orcidid>https://orcid.org/0000-0001-8926-881X</orcidid><orcidid>https://orcid.org/0000-0002-3905-6859</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 4-Hydroxynonenal Aldehydes - metabolism Animals Apoptosis Cardiovascular disease Cell cycle Cell division Cytoskeleton Diabetes Electrophoresis Erythrocytes Female Females Gel electrophoresis Glycoproteins Heart Hemochromatosis Hemochromatosis - genetics Hemochromatosis Protein - genetics Hemochromatosis Protein - metabolism Hemoglobin Homeostasis Humans Immunoblotting Iron Iron Overload Lipid Peroxidation Lipids Liver Male Males Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Mice Mutation Oxidation Oxidative stress Parkinson's disease Patients Peptides Proteins Reactive oxygen species Toxicity |
| title | Protein Susceptibility to Peroxidation by 4-Hydroxynonenal in Hereditary Hemochromatosis |
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