Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members
Identifieur interne : 000E07 ( Istex/Corpus ); précédent : 000E06; suivant : 000E08Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members
Auteurs : Chayma Bouaziz ; Ossama Sharaf El Dein ; Cécile Martel ; Emna El Golli ; Salwa Abid-Essefi ; Catherine Brenner ; Christophe Lemaire ; Hassen BachaSource :
- Environmental Toxicology [ 1520-4081 ] ; 2011-11.
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Abstract
In this study, we looked for the role of the mitochondrion in the cytotoxicity of ochratoxin A (OTA), which is one of the most abundant food‐contaminating mycotoxins in the world. In different human carcinoma cell lines, OTA triggered a mitochondria‐dependent apoptotic process, which is characterized by opening of the mitochondrial permeability transition pore (PTPC), loss of mitochondrial transmembrane potential (ΔΨm), increase in O2[chemp]– production, mitochondrial relocalization of Bax, release of cytochrome c, and caspase activation. However, studies performed on purified organelles suggested that OTA does not directly target the mitochondrion. In addition, we showed that mitochondrial alterations induced by this mycotoxin are favored by the proapoptotic protein Bax, but not Bak. These alterations are prevented by the antiapoptotic proteins, Bcl‐2 and to a lesser degree by Bcl‐XL. Taken together, these data indicate that although mitochondria, PTPC members and proteins of Bcl‐2 family play a pivotal role in OTA‐induced apoptosis, they do not constitute real targets to overcome its toxicity. © 2010 Wiley Periodicals, Inc. Environ Toxicol, 2011.
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DOI: 10.1002/tox.20581
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ISTEX:905E9896B93FA4DBDE6CDD1090A91A6AAB260050Le document en format XML
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In different human carcinoma cell lines, OTA triggered a mitochondria‐dependent apoptotic process, which is characterized by opening of the mitochondrial permeability transition pore (PTPC), loss of mitochondrial transmembrane potential (ΔΨm), increase in O2[chemp]– production, mitochondrial relocalization of Bax, release of cytochrome c, and caspase activation. However, studies performed on purified organelles suggested that OTA does not directly target the mitochondrion. In addition, we showed that mitochondrial alterations induced by this mycotoxin are favored by the proapoptotic protein Bax, but not Bak. These alterations are prevented by the antiapoptotic proteins, Bcl‐2 and to a lesser degree by Bcl‐XL. Taken together, these data indicate that although mitochondria, PTPC members and proteins of Bcl‐2 family play a pivotal role in OTA‐induced apoptosis, they do not constitute real targets to overcome its toxicity. © 2010 Wiley Periodicals, Inc. 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No. DGRST/CNRS 04/R 0803;</note><note>Ministère Tunisien de l'enseignement Supérieur</note><note>de la Recherche Scientifique et de la Technologie through the Laboratoire de Recherche sur les Substances Biologiquement Compatibles: LRSBC</note><note>La Direction Générale de la Recherche Scientifique et de la Rénovation Technologique: DGRST et le Centre National de la Recherche Scientique: CNRS</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members</title><author xml:id="author-1"><persName><forename type="first">Chayma</forename><surname>Bouaziz</surname></persName><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation></author><author xml:id="author-2"><persName><forename type="first">Ossama</forename><surname>Sharaf el dein</surname></persName><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Cécile</forename><surname>Martel</surname></persName><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Emna El</forename><surname>Golli</surname></persName><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation></author><author xml:id="author-5"><persName><forename type="first">Salwa</forename><surname>Abid‐Essefi</surname></persName><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation></author><author xml:id="author-6"><persName><forename type="first">Catherine</forename><surname>Brenner</surname></persName><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation></author><author xml:id="author-7"><persName><forename type="first">Christophe</forename><surname>Lemaire</surname></persName><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation></author><author xml:id="author-8"><persName><forename type="first">Hassen</forename><surname>Bacha</surname></persName><note type="correspondence"><p>Correspondence: Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</p></note><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation></author></analytic><monogr><title level="j">Environmental Toxicology</title><title level="j" type="abbrev">Environ. 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ownership="publisher">Copyright © 2010 Wiley Periodicals, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2009-07-22"></event><event type="manuscriptRevised" date="2010-02-03"></event><event type="manuscriptAccepted" date="2010-02-04"></event><event type="firstOnline" date="2010-04-12"></event><event type="publishedOnlineAcceptedOrEarlyUnpaginated" date="2010-04-12"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.10 mode:FullText" date="2011-11-04"></event><event type="publishedOnlineFinalForm" date="2011-11-04"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-10"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-16"></event></eventGroup><numberingGroup><numbering type="pageFirst">579</numbering><numbering type="pageLast">590</numbering></numberingGroup><correspondenceTo>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:TOX.TOX20581.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="9"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="44"></count><count type="wordTotal" number="6773"></count></countGroup><titleGroup><title type="main" xml:lang="en">Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members</title><title type="short" xml:lang="en">Mechanisms of Ochratoxin A toxicity <fi>in Vitro</fi></title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Chayma</givenNames><familyName>Bouaziz</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Ossama</givenNames><familyName>Sharaf el dein</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Cécile</givenNames><familyName>Martel</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Emna El</givenNames><familyName>Golli</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Salwa</givenNames><familyName>Abid‐Essefi</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Catherine</givenNames><familyName>Brenner</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Christophe</givenNames><familyName>Lemaire</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Hassen</givenNames><familyName>Bacha</familyName></personName><contactDetails><email>hassen.bacha@fmdm.rnu.tn</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="TN" type="organization"><unparsedAffiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="FR" type="organization"><unparsedAffiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">ochratoxin A</keyword><keyword xml:id="kwd2">mitochondria</keyword><keyword xml:id="kwd3">apoptosis</keyword><keyword xml:id="kwd4">PTPC</keyword><keyword xml:id="kwd5">Bcl‐2</keyword><keyword xml:id="kwd6">ROS</keyword></keywordGroup><fundingInfo><fundingAgency>Action d'Echanges Tuniso‐Française</fundingAgency><fundingNumber>DGRST/CNRS 04/R 0803</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Ministère Tunisien de l'enseignement Supérieur</fundingAgency></fundingInfo><fundingInfo><fundingAgency>de la Recherche Scientifique et de la Technologie through the Laboratoire de Recherche sur les Substances Biologiquement Compatibles: LRSBC</fundingAgency></fundingInfo><fundingInfo><fundingAgency>La Direction Générale de la Recherche Scientifique et de la Rénovation Technologique: DGRST et le Centre National de la Recherche Scientique: CNRS</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>In this study, we looked for the role of the mitochondrion in the cytotoxicity of ochratoxin A (OTA), which is one of the most abundant food‐contaminating mycotoxins in the world. In different human carcinoma cell lines, OTA triggered a mitochondria‐dependent apoptotic process, which is characterized by opening of the mitochondrial permeability transition pore (PTPC), loss of mitochondrial transmembrane potential (ΔΨ<sub>m</sub>), increase in O<sub>2</sub>[chemp]<sup>–</sup> production, mitochondrial relocalization of Bax, release of cytochrome c, and caspase activation. However, studies performed on purified organelles suggested that OTA does not directly target the mitochondrion. In addition, we showed that mitochondrial alterations induced by this mycotoxin are favored by the proapoptotic protein Bax, but not Bak. These alterations are prevented by the antiapoptotic proteins, Bcl‐2 and to a lesser degree by Bcl‐X<sub>L</sub>. Taken together, these data indicate that although mitochondria, PTPC members and proteins of Bcl‐2 family play a pivotal role in OTA‐induced apoptosis, they do not constitute real targets to overcome its toxicity. © 2010 Wiley Periodicals, Inc. Environ Toxicol, 2011.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Mechanisms of Ochratoxin A toxicity in Vitro</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Molecular events involved in ochratoxin A induced mitochondrial pathway of apoptosis, modulation by Bcl‐2 family members</title></titleInfo><name type="personal"><namePart type="given">Chayma</namePart><namePart type="family">Bouaziz</namePart><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ossama</namePart><namePart type="family">Sharaf el dein</namePart><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Cécile</namePart><namePart type="family">Martel</namePart><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Emna El</namePart><namePart type="family">Golli</namePart><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Salwa</namePart><namePart type="family">Abid‐Essefi</namePart><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine</namePart><namePart type="family">Brenner</namePart><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christophe</namePart><namePart type="family">Lemaire</namePart><affiliation>Laboratoire de Génétique et Biologie Cellulaire, CNRS UMR 8159, Université de Versaille/SQY, 45 Avenue des Etats‐Unis, Versailles 78035, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hassen</namePart><namePart type="family">Bacha</namePart><affiliation>Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</affiliation><description>Correspondence: Laboratory of Research on Biologically Compatible Compounds, Faculty of Dentistry, Rue Avicenne, Monastir 5000, Tunisia</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2011-11</dateIssued><dateCaptured encoding="w3cdtf">2009-07-22</dateCaptured><dateValid encoding="w3cdtf">2010-02-04</dateValid><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">9</extent><extent unit="references">44</extent><extent unit="words">6773</extent></physicalDescription><abstract lang="en">In this study, we looked for the role of the mitochondrion in the cytotoxicity of ochratoxin A (OTA), which is one of the most abundant food‐contaminating mycotoxins in the world. In different human carcinoma cell lines, OTA triggered a mitochondria‐dependent apoptotic process, which is characterized by opening of the mitochondrial permeability transition pore (PTPC), loss of mitochondrial transmembrane potential (ΔΨm), increase in O2[chemp]– production, mitochondrial relocalization of Bax, release of cytochrome c, and caspase activation. However, studies performed on purified organelles suggested that OTA does not directly target the mitochondrion. In addition, we showed that mitochondrial alterations induced by this mycotoxin are favored by the proapoptotic protein Bax, but not Bak. These alterations are prevented by the antiapoptotic proteins, Bcl‐2 and to a lesser degree by Bcl‐XL. Taken together, these data indicate that although mitochondria, PTPC members and proteins of Bcl‐2 family play a pivotal role in OTA‐induced apoptosis, they do not constitute real targets to overcome its toxicity. © 2010 Wiley Periodicals, Inc. Environ Toxicol, 2011.</abstract><note type="funding">Action d'Echanges Tuniso‐Française - No. DGRST/CNRS 04/R 0803; </note><note type="funding">Ministère Tunisien de l'enseignement Supérieur</note><note type="funding">de la Recherche Scientifique et de la Technologie through the Laboratoire de Recherche sur les Substances Biologiquement Compatibles: LRSBC</note><note type="funding">La Direction Générale de la Recherche Scientifique et de la Rénovation Technologique: DGRST et le Centre National de la Recherche Scientique: CNRS</note><subject lang="en"><genre>keywords</genre><topic>ochratoxin A</topic><topic>mitochondria</topic><topic>apoptosis</topic><topic>PTPC</topic><topic>Bcl‐2</topic><topic>ROS</topic></subject><relatedItem type="host"><titleInfo><title>Environmental Toxicology</title></titleInfo><titleInfo type="abbreviated"><title>Environ. Toxicol.</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">1520-4081</identifier><identifier type="eISSN">1522-7278</identifier><identifier type="DOI">10.1002/(ISSN)1522-7278</identifier><identifier type="PublisherID">TOX</identifier><part><date>2011</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>579</start><end>590</end><total>12</total></extent></part></relatedItem><relatedItem type="preceding"><titleInfo><title>Environmental Toxicology and Water Quality</title></titleInfo><identifier type="ISSN">1053-4725</identifier><identifier type="ISSN">1098-2256</identifier><part><date point="end">1998</date><detail type="volume"><caption>last vol.</caption><number>13</number></detail><detail type="issue"><caption>last no.</caption><number>4</number></detail></part></relatedItem><identifier type="istex">905E9896B93FA4DBDE6CDD1090A91A6AAB260050</identifier><identifier type="DOI">10.1002/tox.20581</identifier><identifier type="ArticleID">TOX20581</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2010 Wiley Periodicals, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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