Oxidative inactivation of the endogenous antioxidant protein DJ-1 by the food contaminants 3-MCPD and 2-MCPD
3-Chloro-1,2-propanediol (3-MCPD) and 2-chloro-1,3-propanediol (2-MCPD) are heat-induced food contaminants being present either as free substances or as fatty acid esters in numerous foods. 3-MCPD was classified to be possibly carcinogenic to humans (category 2B) with kidney and testis being the pri...
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| Veröffentlicht in: | Archives of toxicology 2018-01, Vol.92 (1), p.289-299 |
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| creator | Buhrke, Thorsten Voss, Linn Briese, Anja Stephanowitz, Heike Krause, Eberhard Braeuning, Albert Lampen, Alfonso |
| description | 3-Chloro-1,2-propanediol (3-MCPD) and 2-chloro-1,3-propanediol (2-MCPD) are heat-induced food contaminants being present either as free substances or as fatty acid esters in numerous foods. 3-MCPD was classified to be possibly carcinogenic to humans (category 2B) with kidney and testis being the primary target organs according to animal studies. A previous 28-day oral feeding study with rats revealed that the endogenous antioxidant protein DJ-1 was strongly deregulated at the protein level in kidney, liver, and testis of the experimental animals that had been treated either with 3-MCPD, 2-MCPD or their dipalmitate esters. Here we show that this deregulation is due to the oxidation of a conserved, redox-active cysteine residue (Cys106) of DJ-1 to a cysteine sulfonic acid which is equivalent to loss of function of DJ-1. Irreversible oxidation of DJ-1 is associated with a number of oxidative stress-related diseases such as Parkinson, cancer, and type II diabetes. It is assumed that 3-MCPD or 2-MCPD do not directly oxidize DJ-1, but that these substances induce the formation of reactive oxygen species (ROS) which in turn trigger DJ-1 oxidation. The implications of 3-MCPD/2-MCPD-mediated ROS formation in vivo for the ongoing risk assessment of these compounds as well as the potential of oxidized DJ-1 to serve as a novel effect biomarker for 3-MCPD/2-MCPD toxicity are being discussed. |
| doi_str_mv | 10.1007/s00204-017-2027-5 |
| format | Article |
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A previous 28-day oral feeding study with rats revealed that the endogenous antioxidant protein DJ-1 was strongly deregulated at the protein level in kidney, liver, and testis of the experimental animals that had been treated either with 3-MCPD, 2-MCPD or their dipalmitate esters. Here we show that this deregulation is due to the oxidation of a conserved, redox-active cysteine residue (Cys106) of DJ-1 to a cysteine sulfonic acid which is equivalent to loss of function of DJ-1. Irreversible oxidation of DJ-1 is associated with a number of oxidative stress-related diseases such as Parkinson, cancer, and type II diabetes. It is assumed that 3-MCPD or 2-MCPD do not directly oxidize DJ-1, but that these substances induce the formation of reactive oxygen species (ROS) which in turn trigger DJ-1 oxidation. The implications of 3-MCPD/2-MCPD-mediated ROS formation in vivo for the ongoing risk assessment of these compounds as well as the potential of oxidized DJ-1 to serve as a novel effect biomarker for 3-MCPD/2-MCPD toxicity are being discussed.</description><identifier>ISSN: 0340-5761</identifier><identifier>EISSN: 1432-0738</identifier><identifier>DOI: 10.1007/s00204-017-2027-5</identifier><identifier>PMID: 28707023</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>1,3-Propanediol ; alpha-Chlorohydrin - administration & dosage ; alpha-Chlorohydrin - toxicity ; Animals ; Antioxidants ; Antioxidants - metabolism ; Biocompatibility ; Biomarkers ; Biomedical and Life Sciences ; Biomedicine ; Cancer ; Carcinogens ; Cell Line, Tumor ; Contaminants ; Cysteine ; Cysteine - metabolism ; Deactivation ; Deregulation ; Diabetes mellitus ; Environmental Health ; Esters ; Fatty acids ; Food ; Food Contamination ; Glycerol - administration & dosage ; Glycerol - analogs & derivatives ; Glycerol - toxicity ; Humans ; Inactivation ; Kidney - drug effects ; Kidney - metabolism ; Kidneys ; Liver ; Liver - drug effects ; Liver - metabolism ; Male ; Molecular Toxicology ; Occupational Medicine/Industrial Medicine ; Organs ; Oxidation ; Oxidation-Reduction ; Oxidative stress ; PARK7 protein ; Pharmacology/Toxicology ; Protein Deglycase DJ-1 - genetics ; Protein Deglycase DJ-1 - metabolism ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Processing, Post-Translational ; Proteins ; Rats ; Reactive oxygen species ; Risk assessment ; Sulfonic acid ; Toxicity</subject><ispartof>Archives of toxicology, 2018-01, Vol.92 (1), p.289-299</ispartof><rights>Springer-Verlag GmbH Germany 2017</rights><rights>Archives of Toxicology is a copyright of Springer, (2017). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-3150c37061db1c7beb43fc4fe44172b97aa1154ba0449eba04879cf4fb112a033</citedby><cites>FETCH-LOGICAL-c438t-3150c37061db1c7beb43fc4fe44172b97aa1154ba0449eba04879cf4fb112a033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00204-017-2027-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00204-017-2027-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28707023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Buhrke, Thorsten</creatorcontrib><creatorcontrib>Voss, Linn</creatorcontrib><creatorcontrib>Briese, Anja</creatorcontrib><creatorcontrib>Stephanowitz, Heike</creatorcontrib><creatorcontrib>Krause, Eberhard</creatorcontrib><creatorcontrib>Braeuning, Albert</creatorcontrib><creatorcontrib>Lampen, Alfonso</creatorcontrib><title>Oxidative inactivation of the endogenous antioxidant protein DJ-1 by the food contaminants 3-MCPD and 2-MCPD</title><title>Archives of toxicology</title><addtitle>Arch Toxicol</addtitle><addtitle>Arch Toxicol</addtitle><description>3-Chloro-1,2-propanediol (3-MCPD) and 2-chloro-1,3-propanediol (2-MCPD) are heat-induced food contaminants being present either as free substances or as fatty acid esters in numerous foods. 3-MCPD was classified to be possibly carcinogenic to humans (category 2B) with kidney and testis being the primary target organs according to animal studies. A previous 28-day oral feeding study with rats revealed that the endogenous antioxidant protein DJ-1 was strongly deregulated at the protein level in kidney, liver, and testis of the experimental animals that had been treated either with 3-MCPD, 2-MCPD or their dipalmitate esters. Here we show that this deregulation is due to the oxidation of a conserved, redox-active cysteine residue (Cys106) of DJ-1 to a cysteine sulfonic acid which is equivalent to loss of function of DJ-1. Irreversible oxidation of DJ-1 is associated with a number of oxidative stress-related diseases such as Parkinson, cancer, and type II diabetes. It is assumed that 3-MCPD or 2-MCPD do not directly oxidize DJ-1, but that these substances induce the formation of reactive oxygen species (ROS) which in turn trigger DJ-1 oxidation. The implications of 3-MCPD/2-MCPD-mediated ROS formation in vivo for the ongoing risk assessment of these compounds as well as the potential of oxidized DJ-1 to serve as a novel effect biomarker for 3-MCPD/2-MCPD toxicity are being discussed.</description><subject>1,3-Propanediol</subject><subject>alpha-Chlorohydrin - administration & dosage</subject><subject>alpha-Chlorohydrin - toxicity</subject><subject>Animals</subject><subject>Antioxidants</subject><subject>Antioxidants - metabolism</subject><subject>Biocompatibility</subject><subject>Biomarkers</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer</subject><subject>Carcinogens</subject><subject>Cell Line, Tumor</subject><subject>Contaminants</subject><subject>Cysteine</subject><subject>Cysteine - metabolism</subject><subject>Deactivation</subject><subject>Deregulation</subject><subject>Diabetes mellitus</subject><subject>Environmental Health</subject><subject>Esters</subject><subject>Fatty acids</subject><subject>Food</subject><subject>Food Contamination</subject><subject>Glycerol - administration & dosage</subject><subject>Glycerol - analogs & derivatives</subject><subject>Glycerol - toxicity</subject><subject>Humans</subject><subject>Inactivation</subject><subject>Kidney - drug effects</subject><subject>Kidney - metabolism</subject><subject>Kidneys</subject><subject>Liver</subject><subject>Liver - drug effects</subject><subject>Liver - metabolism</subject><subject>Male</subject><subject>Molecular Toxicology</subject><subject>Occupational Medicine/Industrial Medicine</subject><subject>Organs</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidative stress</subject><subject>PARK7 protein</subject><subject>Pharmacology/Toxicology</subject><subject>Protein Deglycase DJ-1 - genetics</subject><subject>Protein Deglycase DJ-1 - metabolism</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Rats</subject><subject>Reactive oxygen species</subject><subject>Risk assessment</subject><subject>Sulfonic acid</subject><subject>Toxicity</subject><issn>0340-5761</issn><issn>1432-0738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</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>eNp1kE1PwzAMhiMEYmPwA7igSJwDdpIu3RFtfGpoHOAcpW06Om3JaFrE_j3pNuDEyY78-HX0EHKOcIUA6joAcJAMUDEOXLHkgPRRCs5AifSQ9EFIYIkaYo-chLAAQJ6OxDHp8VSBAi76ZDn7qgrTVJ-WVs7ksYkP76gvafNuqXWFn1vn20CNi4MOdg1d176xlaOTJ4Y022zR0vuC5t41ZhWTXBOoYM_jl0lcLCjftqfkqDTLYM_2dUDe7m5fxw9sOrt_HN9MWS5F2jCBCeRCwRCLDHOV2UyKMpellRIVz0bKGMREZgakHNmupGqUl7LMELkBIQbkcpcb__nR2tDohW9rF09qjhhNpUp2FO6ovPYh1LbU67pamXqjEXTnV-_86uhXd351Encu9slttrLF78aP0AjwHRDiyM1t_Xf6_9RvV1mD8w</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Buhrke, Thorsten</creator><creator>Voss, Linn</creator><creator>Briese, Anja</creator><creator>Stephanowitz, Heike</creator><creator>Krause, Eberhard</creator><creator>Braeuning, Albert</creator><creator>Lampen, Alfonso</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>7T2</scope><scope>7TK</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>MBDVC</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PYCSY</scope><scope>Q9U</scope></search><sort><creationdate>20180101</creationdate><title>Oxidative inactivation of the endogenous antioxidant protein DJ-1 by the food contaminants 3-MCPD and 2-MCPD</title><author>Buhrke, Thorsten ; Voss, Linn ; Briese, Anja ; Stephanowitz, Heike ; Krause, Eberhard ; Braeuning, Albert ; Lampen, Alfonso</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-3150c37061db1c7beb43fc4fe44172b97aa1154ba0449eba04879cf4fb112a033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>1,3-Propanediol</topic><topic>alpha-Chlorohydrin - administration & dosage</topic><topic>alpha-Chlorohydrin - toxicity</topic><topic>Animals</topic><topic>Antioxidants</topic><topic>Antioxidants - metabolism</topic><topic>Biocompatibility</topic><topic>Biomarkers</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer</topic><topic>Carcinogens</topic><topic>Cell Line, Tumor</topic><topic>Contaminants</topic><topic>Cysteine</topic><topic>Cysteine - metabolism</topic><topic>Deactivation</topic><topic>Deregulation</topic><topic>Diabetes mellitus</topic><topic>Environmental Health</topic><topic>Esters</topic><topic>Fatty acids</topic><topic>Food</topic><topic>Food Contamination</topic><topic>Glycerol - administration & dosage</topic><topic>Glycerol - analogs & derivatives</topic><topic>Glycerol - toxicity</topic><topic>Humans</topic><topic>Inactivation</topic><topic>Kidney - drug effects</topic><topic>Kidney - metabolism</topic><topic>Kidneys</topic><topic>Liver</topic><topic>Liver - drug effects</topic><topic>Liver - 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A previous 28-day oral feeding study with rats revealed that the endogenous antioxidant protein DJ-1 was strongly deregulated at the protein level in kidney, liver, and testis of the experimental animals that had been treated either with 3-MCPD, 2-MCPD or their dipalmitate esters. Here we show that this deregulation is due to the oxidation of a conserved, redox-active cysteine residue (Cys106) of DJ-1 to a cysteine sulfonic acid which is equivalent to loss of function of DJ-1. Irreversible oxidation of DJ-1 is associated with a number of oxidative stress-related diseases such as Parkinson, cancer, and type II diabetes. It is assumed that 3-MCPD or 2-MCPD do not directly oxidize DJ-1, but that these substances induce the formation of reactive oxygen species (ROS) which in turn trigger DJ-1 oxidation. The implications of 3-MCPD/2-MCPD-mediated ROS formation in vivo for the ongoing risk assessment of these compounds as well as the potential of oxidized DJ-1 to serve as a novel effect biomarker for 3-MCPD/2-MCPD toxicity are being discussed.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>28707023</pmid><doi>10.1007/s00204-017-2027-5</doi><tpages>11</tpages></addata></record> |
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| ispartof | Archives of toxicology, 2018-01, Vol.92 (1), p.289-299 |
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| subjects | 1,3-Propanediol alpha-Chlorohydrin - administration & dosage alpha-Chlorohydrin - toxicity Animals Antioxidants Antioxidants - metabolism Biocompatibility Biomarkers Biomedical and Life Sciences Biomedicine Cancer Carcinogens Cell Line, Tumor Contaminants Cysteine Cysteine - metabolism Deactivation Deregulation Diabetes mellitus Environmental Health Esters Fatty acids Food Food Contamination Glycerol - administration & dosage Glycerol - analogs & derivatives Glycerol - toxicity Humans Inactivation Kidney - drug effects Kidney - metabolism Kidneys Liver Liver - drug effects Liver - metabolism Male Molecular Toxicology Occupational Medicine/Industrial Medicine Organs Oxidation Oxidation-Reduction Oxidative stress PARK7 protein Pharmacology/Toxicology Protein Deglycase DJ-1 - genetics Protein Deglycase DJ-1 - metabolism Protein Isoforms - genetics Protein Isoforms - metabolism Protein Processing, Post-Translational Proteins Rats Reactive oxygen species Risk assessment Sulfonic acid Toxicity |
| title | Oxidative inactivation of the endogenous antioxidant protein DJ-1 by the food contaminants 3-MCPD and 2-MCPD |
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