Protein oxidation in Huntington disease
Identifieur interne : 000379 ( Istex/Corpus ); précédent : 000378; suivant : 000380Protein oxidation in Huntington disease
Auteurs : M. Alba Sorolla ; María José Rodríguez-Colman ; Núria Vall-Llaura ; Jordi Tamarit ; Joaquim Ros ; Elisa CabiscolSource :
- BioFactors [ 0951-6433 ] ; 2012-05.
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Abstract
Huntington disease (HD) is an inherited neurodegenerative disorder caused by expansion of CAG repeats in the huntingtin gene, affecting initially the striatum and progressively the cortex. Oxidative stress, and consequent protein oxidation, has been described as important to disease progression. This review focuses on recent advances in the field, with a particular emphasis on the identified target proteins and the role that their oxidation has or might have in the pathophysiology of HD. Oxidation and the resulting inactivation and/or degradation of important proteins can explain the impairment of several metabolic pathways in HD. Oxidation of enzymes involved in ATP synthesis can account for the energy deficiency observed. Impairment of protein folding and degradation can be due to oxidation of several heat shock proteins and Valosin‐containing protein. Oxidation of two enzymes involved in the vitamin B6 metabolism could result in decreased availability of pyridoxal phosphate, which is a necessary cofactor in transaminations, the kynurenine pathway and the synthesis of glutathione, GABA, dopamine and serotonin, all of which have a key role in HD pathology. In addition, protein oxidation often contributes to oxidative stress, aggravating the molecular damage inside the cell.
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DOI: 10.1002/biof.1013
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ISTEX:C1F291B9F24AA548A537FB619CB0BF011412F6ABLe document en format XML
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Alba Sorolla</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation></author><author><name sortKey="Rodriguez Olman, Maria Jose" sort="Rodriguez Olman, Maria Jose" uniqKey="Rodriguez Olman M" first="María José" last="Rodríguez-Colman">María José Rodríguez-Colman</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation></author><author><name sortKey="Vall Laura, Nuria" sort="Vall Laura, Nuria" uniqKey="Vall Laura N" first="Núria" last="Vall-Llaura">Núria Vall-Llaura</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation></author><author><name sortKey="Tamarit, Jordi" sort="Tamarit, Jordi" uniqKey="Tamarit J" first="Jordi" last="Tamarit">Jordi Tamarit</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation></author><author><name sortKey="Ros, Joaquim" sort="Ros, Joaquim" uniqKey="Ros J" first="Joaquim" last="Ros">Joaquim Ros</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation></author><author><name sortKey="Cabiscol, Elisa" sort="Cabiscol, Elisa" uniqKey="Cabiscol E" first="Elisa" last="Cabiscol">Elisa Cabiscol</name><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, C/Montserrat Roig, 2, 25008‐Lleida, Spain</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:C1F291B9F24AA548A537FB619CB0BF011412F6AB</idno><date when="2012" year="2012">2012</date><idno type="doi">10.1002/biof.1013</idno><idno type="url">https://api.istex.fr/document/C1F291B9F24AA548A537FB619CB0BF011412F6AB/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000379</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000379</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Protein oxidation in Huntington disease</title><author><name sortKey="Sorolla, M Alba" sort="Sorolla, M Alba" uniqKey="Sorolla M" first="M. 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Oxidative stress, and consequent protein oxidation, has been described as important to disease progression. This review focuses on recent advances in the field, with a particular emphasis on the identified target proteins and the role that their oxidation has or might have in the pathophysiology of HD. Oxidation and the resulting inactivation and/or degradation of important proteins can explain the impairment of several metabolic pathways in HD. Oxidation of enzymes involved in ATP synthesis can account for the energy deficiency observed. Impairment of protein folding and degradation can be due to oxidation of several heat shock proteins and Valosin‐containing protein. Oxidation of two enzymes involved in the vitamin B6 metabolism could result in decreased availability of pyridoxal phosphate, which is a necessary cofactor in transaminations, the kynurenine pathway and the synthesis of glutathione, GABA, dopamine and serotonin, all of which have a key role in HD pathology. In addition, protein oxidation often contributes to oxidative stress, aggravating the molecular damage inside the cell.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>M. 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Oxidative stress, and consequent protein oxidation, has been described as important to disease progression. This review focuses on recent advances in the field, with a particular emphasis on the identified target proteins and the role that their oxidation has or might have in the pathophysiology of HD. Oxidation and the resulting inactivation and/or degradation of important proteins can explain the impairment of several metabolic pathways in HD. Oxidation of enzymes involved in ATP synthesis can account for the energy deficiency observed. Impairment of protein folding and degradation can be due to oxidation of several heat shock proteins and Valosin‐containing protein. Oxidation of two enzymes involved in the vitamin B6 metabolism could result in decreased availability of pyridoxal phosphate, which is a necessary cofactor in transaminations, the kynurenine pathway and the synthesis of glutathione, GABA, dopamine and serotonin, all of which have a key role in HD pathology. 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Alba</givenNames><familyName>Sorolla</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>María José</givenNames><familyName>Rodríguez‐Colman</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Núria</givenNames><familyName>Vall‐llaura</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Jordi</givenNames><familyName>Tamarit</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Joaquim</givenNames><familyName>Ros</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af1" corresponding="yes" noteRef="#fn1"><personName><givenNames>Elisa</givenNames><familyName>Cabiscol</familyName></personName><contactDetails><email>elisa.cabiscol@cmb.udl.cat</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="ES" type="organization"><unparsedAffiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">Huntington disease</keyword><keyword xml:id="kwd2">protein oxidation</keyword><keyword xml:id="kwd3">oxidative stress</keyword><keyword xml:id="kwd4">energy deficiency</keyword><keyword xml:id="kwd5">pyridoxal 5‐phosphate</keyword></keywordGroup><fundingInfo><fundingAgency>Consolider Ingenio 2010 from Spain's Ministerio de Ciencia e Innovación</fundingAgency><fundingNumber>BFU2010‐17387</fundingNumber><fundingNumber>CSD2007‐20</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Generalitat de Catalunya</fundingAgency><fundingNumber>2009SGR196</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Huntington disease (HD) is an inherited neurodegenerative disorder caused by expansion of CAG repeats in the <i>huntingtin</i> gene, affecting initially the striatum and progressively the cortex. Oxidative stress, and consequent protein oxidation, has been described as important to disease progression. This review focuses on recent advances in the field, with a particular emphasis on the identified target proteins and the role that their oxidation has or might have in the pathophysiology of HD. Oxidation and the resulting inactivation and/or degradation of important proteins can explain the impairment of several metabolic pathways in HD. Oxidation of enzymes involved in ATP synthesis can account for the energy deficiency observed. Impairment of protein folding and degradation can be due to oxidation of several heat shock proteins and Valosin‐containing protein. Oxidation of two enzymes involved in the vitamin B6 metabolism could result in decreased availability of pyridoxal phosphate, which is a necessary cofactor in transaminations, the kynurenine pathway and the synthesis of glutathione, GABA, dopamine and serotonin, all of which have a key role in HD pathology. In addition, protein oxidation often contributes to oxidative stress, aggravating the molecular damage inside the cell.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Tel: +34 973 702281; Fax: 34 973 702426</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Protein oxidation in Huntington disease</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Protein Oxidation in Huntington Disease</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Protein oxidation in Huntington disease</title></titleInfo><name type="personal"><namePart type="given">M. Alba</namePart><namePart type="family">Sorolla</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">María José</namePart><namePart type="family">Rodríguez‐Colman</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Núria</namePart><namePart type="family">Vall‐llaura</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jordi</namePart><namePart type="family">Tamarit</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Joaquim</namePart><namePart type="family">Ros</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Elisa</namePart><namePart type="family">Cabiscol</namePart><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, 25008 Lleida, Spain</affiliation><description>Tel: +34 973 702281; Fax: 34 973 702426</description><affiliation>Department of Basic Medical Sciences, IRBLleida, Universitat de Lleida, C/Montserrat Roig, 2, 25008‐Lleida, Spain</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2012-05</dateIssued><dateCaptured encoding="w3cdtf">2012-01-16</dateCaptured><dateValid encoding="w3cdtf">2012-03-08</dateValid><copyrightDate encoding="w3cdtf">2012</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">2</extent><extent unit="tables">1</extent><extent unit="references">121</extent><extent unit="words">11771</extent></physicalDescription><abstract lang="en">Huntington disease (HD) is an inherited neurodegenerative disorder caused by expansion of CAG repeats in the huntingtin gene, affecting initially the striatum and progressively the cortex. Oxidative stress, and consequent protein oxidation, has been described as important to disease progression. This review focuses on recent advances in the field, with a particular emphasis on the identified target proteins and the role that their oxidation has or might have in the pathophysiology of HD. Oxidation and the resulting inactivation and/or degradation of important proteins can explain the impairment of several metabolic pathways in HD. Oxidation of enzymes involved in ATP synthesis can account for the energy deficiency observed. Impairment of protein folding and degradation can be due to oxidation of several heat shock proteins and Valosin‐containing protein. Oxidation of two enzymes involved in the vitamin B6 metabolism could result in decreased availability of pyridoxal phosphate, which is a necessary cofactor in transaminations, the kynurenine pathway and the synthesis of glutathione, GABA, dopamine and serotonin, all of which have a key role in HD pathology. In addition, protein oxidation often contributes to oxidative stress, aggravating the molecular damage inside the cell.</abstract><note type="funding">Consolider Ingenio 2010 from Spain's Ministerio de Ciencia e Innovación - No. BFU2010‐17387; No. CSD2007‐20; </note><note type="funding">Generalitat de Catalunya - No. 2009SGR196; </note><subject lang="en"><genre>keywords</genre><topic>Huntington disease</topic><topic>protein oxidation</topic><topic>oxidative stress</topic><topic>energy deficiency</topic><topic>pyridoxal 5‐phosphate</topic></subject><relatedItem type="host"><titleInfo><title>BioFactors</title></titleInfo><titleInfo type="abbreviated"><title>BioFactors</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Review Article</topic></subject><identifier type="ISSN">0951-6433</identifier><identifier type="eISSN">1872-8081</identifier><identifier type="DOI">10.1002/(ISSN)1872-8081</identifier><identifier type="PublisherID">BIOF</identifier><part><date>2012</date><detail type="volume"><caption>vol.</caption><number>38</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>173</start><end>185</end><total>13</total></extent></part></relatedItem><identifier type="istex">C1F291B9F24AA548A537FB619CB0BF011412F6AB</identifier><identifier type="DOI">10.1002/biof.1013</identifier><identifier type="ArticleID">BIOF1013</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2012 International Union of Biochemistry and Molecular Biology, 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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