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Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia.

Identifieur interne : 000494 ( Main/Exploration ); précédent : 000493; suivant : 000495

Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia.

Auteurs : Juan Ignacio Romero [Argentine] ; Eva-Maria Hanschmann [Allemagne] ; Manuela Gellert [Allemagne] ; Susanne Eitner [Allemagne] ; Mariana Inés Holubiec [Argentine] ; Eduardo Blanco-Calvo [Espagne] ; Christopher Horst Lillig [Allemagne] ; Francisco Capani [Argentine]

Source :

RBID : pubmed:25735211

Descripteurs français

English descriptors

Abstract

BACKGROUND

Thioredoxin (Trx) family proteins are crucial mediators of cell functions via regulation of the thiol redox state of various key proteins and the levels of the intracellular second messenger hydrogen peroxide. Their expression, localization and functions are altered in various pathologies. Here, we have analyzed the impact of Trx family proteins in neuronal development and recovery, following hypoxia/ischemia and reperfusion.

METHODS

We have analyzed the regulation and potential functions of Trx family proteins during hypoxia/ischemia and reoxygenation of the developing brain in both an animal and a cellular model of perinatal asphyxia. We have analyzed the distribution of 14 Trx family and related proteins in the cerebellum, striatum, and hippocampus, three areas of the rat brain that are especially susceptible to hypoxia. Using SH-SY5Y cells subjected to hypoxia and reoxygenation, we have analyzed the functions of some redoxins suggested by the animal experiment.

RESULTS AND CONCLUSIONS

We have described/discovered a complex, cell-type and tissue-specific expression pattern following the hypoxia/ischemia and reoxygenation. Particularly, Grx2 and Trx1 showed distinct changes during tissue recovery following hypoxia/ischemia and reoxygenation. Silencing of these proteins in SH-SY5Y cells subjected to hypoxia-reoxygenation confirmed that these proteins are required to maintain the normal neuronal phenotype.

GENERAL SIGNIFICANCE

These findings demonstrate the significance of redox signaling in cellular pathways. Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders.


DOI: 10.1016/j.bbagen.2015.02.015
PubMed: 25735211


Affiliations:


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Le document en format XML

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<term>Animals (MeSH)</term>
<term>Asphyxia Neonatorum (enzymology)</term>
<term>Asphyxia Neonatorum (pathology)</term>
<term>Brain (enzymology)</term>
<term>Brain (pathology)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Disease Models, Animal (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Hypoxia-Ischemia, Brain (enzymology)</term>
<term>Hypoxia-Ischemia, Brain (pathology)</term>
<term>Male (MeSH)</term>
<term>Neurons (enzymology)</term>
<term>Neurons (pathology)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxygen (metabolism)</term>
<term>Phenotype (MeSH)</term>
<term>RNA Interference (MeSH)</term>
<term>Rats, Sprague-Dawley (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Thioredoxins (genetics)</term>
<term>Thioredoxins (metabolism)</term>
<term>Time Factors (MeSH)</term>
<term>Transfection (MeSH)</term>
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<term>Animaux (MeSH)</term>
<term>Asphyxie néonatale (anatomopathologie)</term>
<term>Asphyxie néonatale (enzymologie)</term>
<term>Encéphale (anatomopathologie)</term>
<term>Encéphale (enzymologie)</term>
<term>Facteurs temps (MeSH)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Hypoxie-ischémie du cerveau (anatomopathologie)</term>
<term>Hypoxie-ischémie du cerveau (enzymologie)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Modèles animaux de maladie humaine (MeSH)</term>
<term>Mâle (MeSH)</term>
<term>Neurones (anatomopathologie)</term>
<term>Neurones (enzymologie)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Oxygène (métabolisme)</term>
<term>Phénotype (MeSH)</term>
<term>Rat Sprague-Dawley (MeSH)</term>
<term>Thiorédoxines (génétique)</term>
<term>Thiorédoxines (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transfection (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Glutaredoxins</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr">
<term>Asphyxie néonatale</term>
<term>Encéphale</term>
<term>Hypoxie-ischémie du cerveau</term>
<term>Neurones</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Asphyxie néonatale</term>
<term>Encéphale</term>
<term>Hypoxie-ischémie du cerveau</term>
<term>Neurones</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Asphyxia Neonatorum</term>
<term>Brain</term>
<term>Hypoxia-Ischemia, Brain</term>
<term>Neurons</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Glutarédoxines</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Glutaredoxins</term>
<term>Oxygen</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Glutarédoxines</term>
<term>Oxygène</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en">
<term>Asphyxia Neonatorum</term>
<term>Brain</term>
<term>Hypoxia-Ischemia, Brain</term>
<term>Neurons</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Animals</term>
<term>Cell Line, Tumor</term>
<term>Disease Models, Animal</term>
<term>Humans</term>
<term>Male</term>
<term>Oxidation-Reduction</term>
<term>Phenotype</term>
<term>RNA Interference</term>
<term>Rats, Sprague-Dawley</term>
<term>Signal Transduction</term>
<term>Time Factors</term>
<term>Transfection</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Animaux</term>
<term>Facteurs temps</term>
<term>Humains</term>
<term>Interférence par ARN</term>
<term>Lignée cellulaire tumorale</term>
<term>Modèles animaux de maladie humaine</term>
<term>Mâle</term>
<term>Oxydoréduction</term>
<term>Phénotype</term>
<term>Rat Sprague-Dawley</term>
<term>Transduction du signal</term>
<term>Transfection</term>
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<front>
<div type="abstract" xml:lang="en">
<p>
<b>BACKGROUND</b>
</p>
<p>Thioredoxin (Trx) family proteins are crucial mediators of cell functions via regulation of the thiol redox state of various key proteins and the levels of the intracellular second messenger hydrogen peroxide. Their expression, localization and functions are altered in various pathologies. Here, we have analyzed the impact of Trx family proteins in neuronal development and recovery, following hypoxia/ischemia and reperfusion.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>METHODS</b>
</p>
<p>We have analyzed the regulation and potential functions of Trx family proteins during hypoxia/ischemia and reoxygenation of the developing brain in both an animal and a cellular model of perinatal asphyxia. We have analyzed the distribution of 14 Trx family and related proteins in the cerebellum, striatum, and hippocampus, three areas of the rat brain that are especially susceptible to hypoxia. Using SH-SY5Y cells subjected to hypoxia and reoxygenation, we have analyzed the functions of some redoxins suggested by the animal experiment.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>RESULTS AND CONCLUSIONS</b>
</p>
<p>We have described/discovered a complex, cell-type and tissue-specific expression pattern following the hypoxia/ischemia and reoxygenation. Particularly, Grx2 and Trx1 showed distinct changes during tissue recovery following hypoxia/ischemia and reoxygenation. Silencing of these proteins in SH-SY5Y cells subjected to hypoxia-reoxygenation confirmed that these proteins are required to maintain the normal neuronal phenotype.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>GENERAL SIGNIFICANCE</b>
</p>
<p>These findings demonstrate the significance of redox signaling in cellular pathways. Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders.</p>
</div>
</front>
</TEI>
<pubmed>
<MedlineCitation Status="MEDLINE" Owner="NLM">
<PMID Version="1">25735211</PMID>
<DateCompleted>
<Year>2015</Year>
<Month>08</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised>
<Year>2016</Year>
<Month>11</Month>
<Day>26</Day>
</DateRevised>
<Article PubModel="Print-Electronic">
<Journal>
<ISSN IssnType="Print">0006-3002</ISSN>
<JournalIssue CitedMedium="Print">
<Volume>1850</Volume>
<Issue>6</Issue>
<PubDate>
<Year>2015</Year>
<Month>Jun</Month>
</PubDate>
</JournalIssue>
<Title>Biochimica et biophysica acta</Title>
<ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation>
</Journal>
<ArticleTitle>Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia.</ArticleTitle>
<Pagination>
<MedlinePgn>1274-85</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2015.02.015</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S0304-4165(15)00077-X</ELocationID>
<Abstract>
<AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Thioredoxin (Trx) family proteins are crucial mediators of cell functions via regulation of the thiol redox state of various key proteins and the levels of the intracellular second messenger hydrogen peroxide. Their expression, localization and functions are altered in various pathologies. Here, we have analyzed the impact of Trx family proteins in neuronal development and recovery, following hypoxia/ischemia and reperfusion.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">We have analyzed the regulation and potential functions of Trx family proteins during hypoxia/ischemia and reoxygenation of the developing brain in both an animal and a cellular model of perinatal asphyxia. We have analyzed the distribution of 14 Trx family and related proteins in the cerebellum, striatum, and hippocampus, three areas of the rat brain that are especially susceptible to hypoxia. Using SH-SY5Y cells subjected to hypoxia and reoxygenation, we have analyzed the functions of some redoxins suggested by the animal experiment.</AbstractText>
<AbstractText Label="RESULTS AND CONCLUSIONS" NlmCategory="CONCLUSIONS">We have described/discovered a complex, cell-type and tissue-specific expression pattern following the hypoxia/ischemia and reoxygenation. Particularly, Grx2 and Trx1 showed distinct changes during tissue recovery following hypoxia/ischemia and reoxygenation. Silencing of these proteins in SH-SY5Y cells subjected to hypoxia-reoxygenation confirmed that these proteins are required to maintain the normal neuronal phenotype.</AbstractText>
<AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">These findings demonstrate the significance of redox signaling in cellular pathways. Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders.</AbstractText>
<CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Romero</LastName>
<ForeName>Juan Ignacio</ForeName>
<Initials>JI</Initials>
<AffiliationInfo>
<Affiliation>Instituto de Investigaciones Cardiológicas "Prof. Dr. Alberto C. Taquini" (ININCA), Facultad de Medicina, UBA-CONICET, Marcelo T. de Alvear 2270, C1122AAJ, Ciudad de Buenos Aires, Argentina.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Hanschmann</LastName>
<ForeName>Eva-Maria</ForeName>
<Initials>EM</Initials>
<AffiliationInfo>
<Affiliation>Institute for Medical Biochemistry and Molecular Biology, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität Greifswald, 17475 Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Gellert</LastName>
<ForeName>Manuela</ForeName>
<Initials>M</Initials>
<AffiliationInfo>
<Affiliation>Institute for Medical Biochemistry and Molecular Biology, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität Greifswald, 17475 Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Eitner</LastName>
<ForeName>Susanne</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>Institute for Medical Biochemistry and Molecular Biology, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität Greifswald, 17475 Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Holubiec</LastName>
<ForeName>Mariana Inés</ForeName>
<Initials>MI</Initials>
<AffiliationInfo>
<Affiliation>Instituto de Investigaciones Cardiológicas "Prof. Dr. Alberto C. Taquini" (ININCA), Facultad de Medicina, UBA-CONICET, Marcelo T. de Alvear 2270, C1122AAJ, Ciudad de Buenos Aires, Argentina.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Blanco-Calvo</LastName>
<ForeName>Eduardo</ForeName>
<Initials>E</Initials>
<AffiliationInfo>
<Affiliation>Instituto de Investigaciones Cardiológicas "Prof. Dr. Alberto C. Taquini" (ININCA), Facultad de Medicina, UBA-CONICET, Marcelo T. de Alvear 2270, C1122AAJ, Ciudad de Buenos Aires, Argentina; Facultat d'Educació, Psicologia i Treball Social Universitat de Lleida Av. de l'Estudi General, 4, 25001 Lleida, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Lillig</LastName>
<ForeName>Christopher Horst</ForeName>
<Initials>CH</Initials>
<AffiliationInfo>
<Affiliation>Institute for Medical Biochemistry and Molecular Biology, Universitätsmedizin Greifswald, Ernst-Moritz-Arndt-Universität Greifswald, 17475 Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Capani</LastName>
<ForeName>Francisco</ForeName>
<Initials>F</Initials>
<AffiliationInfo>
<Affiliation>Instituto de Investigaciones Cardiológicas "Prof. Dr. Alberto C. Taquini" (ININCA), Facultad de Medicina, UBA-CONICET, Marcelo T. de Alvear 2270, C1122AAJ, Ciudad de Buenos Aires, Argentina; Departamento de Biología, UAJFK, C1197AAR, Ciudad de Buenos Aires, Argentina. Electronic address: franciscocapani@hotmail.com.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2015</Year>
<Month>02</Month>
<Day>28</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>Netherlands</Country>
<MedlineTA>Biochim Biophys Acta</MedlineTA>
<NlmUniqueID>0217513</NlmUniqueID>
<ISSNLinking>0006-3002</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516010">Glrx2 protein, rat</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C491203">TXN protein, human</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C495697">Txn1 protein, rat</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>S88TT14065</RegistryNumber>
<NameOfSubstance UI="D010100">Oxygen</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001238" MajorTopicYN="N">Asphyxia Neonatorum</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D020925" MajorTopicYN="N">Hypoxia-Ischemia, Brain</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D017207" MajorTopicYN="N">Rats, Sprague-Dawley</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="N">Common carotid artery occlusion</Keyword>
<Keyword MajorTopicYN="N">Hypoxia</Keyword>
<Keyword MajorTopicYN="N">Perinatal asphyxia</Keyword>
<Keyword MajorTopicYN="N">Reoxygenation</Keyword>
<Keyword MajorTopicYN="N">Thioredoxin family of proteins</Keyword>
</KeywordList>
</MedlineCitation>
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<Year>2014</Year>
<Month>08</Month>
<Day>11</Day>
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<PubMedPubDate PubStatus="revised">
<Year>2015</Year>
<Month>02</Month>
<Day>14</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2015</Year>
<Month>02</Month>
<Day>24</Day>
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<Year>2015</Year>
<Month>3</Month>
<Day>5</Day>
<Hour>6</Hour>
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<PubMedPubDate PubStatus="pubmed">
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<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline">
<Year>2015</Year>
<Month>9</Month>
<Day>1</Day>
<Hour>6</Hour>
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<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">25735211</ArticleId>
<ArticleId IdType="pii">S0304-4165(15)00077-X</ArticleId>
<ArticleId IdType="doi">10.1016/j.bbagen.2015.02.015</ArticleId>
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<list>
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<li>Allemagne</li>
<li>Argentine</li>
<li>Espagne</li>
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<li>Catalogne</li>
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<noRegion>
<name sortKey="Romero, Juan Ignacio" sort="Romero, Juan Ignacio" uniqKey="Romero J" first="Juan Ignacio" last="Romero">Juan Ignacio Romero</name>
</noRegion>
<name sortKey="Capani, Francisco" sort="Capani, Francisco" uniqKey="Capani F" first="Francisco" last="Capani">Francisco Capani</name>
<name sortKey="Holubiec, Mariana Ines" sort="Holubiec, Mariana Ines" uniqKey="Holubiec M" first="Mariana Inés" last="Holubiec">Mariana Inés Holubiec</name>
</country>
<country name="Allemagne">
<noRegion>
<name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name>
</noRegion>
<name sortKey="Eitner, Susanne" sort="Eitner, Susanne" uniqKey="Eitner S" first="Susanne" last="Eitner">Susanne Eitner</name>
<name sortKey="Gellert, Manuela" sort="Gellert, Manuela" uniqKey="Gellert M" first="Manuela" last="Gellert">Manuela Gellert</name>
<name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name>
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<country name="Espagne">
<region name="Catalogne">
<name sortKey="Blanco Calvo, Eduardo" sort="Blanco Calvo, Eduardo" uniqKey="Blanco Calvo E" first="Eduardo" last="Blanco-Calvo">Eduardo Blanco-Calvo</name>
</region>
</country>
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