Thioredoxin induced antioxidant gene expressions in human lens epithelial cells.
Identifieur interne : 000D02 ( Main/Exploration ); précédent : 000D01; suivant : 000D03Thioredoxin induced antioxidant gene expressions in human lens epithelial cells.
Auteurs : Svitlana Yegorova [États-Unis] ; Oleg Yegorov ; Marjorie F. LouSource :
- Experimental eye research [ 0014-4835 ] ; 2006.
Descripteurs français
- KwdFr :
- Antioxydants (métabolisme), Cellules cultivées (MeSH), Cellules épithéliales (effets des médicaments et des substances chimiques), Cellules épithéliales (enzymologie), Cristallin (effets des médicaments et des substances chimiques), Cristallin (enzymologie), Glutarédoxines (MeSH), Humains (MeSH), Oxidoreductases (biosynthèse), Oxidoreductases (génétique), Oxydoréduction (MeSH), Peroxidases (biosynthèse), Peroxidases (génétique), Peroxirédoxines (MeSH), Protein-disulfide reductase (glutathione) (biosynthèse), Protein-disulfide reductase (glutathione) (génétique), Protéines recombinantes (pharmacologie), RT-PCR (méthodes), Régulation de l'expression des gènes codant pour des enzymes (effets des médicaments et des substances chimiques), Stress oxydatif (MeSH), Superoxide dismutase (biosynthèse), Superoxide dismutase (génétique), Thiorédoxines (pharmacologie).
- MESH :
- biosynthèse : Oxidoreductases, Peroxidases, Protein-disulfide reductase (glutathione), Superoxide dismutase.
- effets des médicaments et des substances chimiques : Cellules épithéliales, Cristallin, Régulation de l'expression des gènes codant pour des enzymes.
- enzymologie : Cellules épithéliales, Cristallin.
- génétique : Oxidoreductases, Peroxidases, Protein-disulfide reductase (glutathione), Superoxide dismutase.
- métabolisme : Antioxydants.
- méthodes : RT-PCR.
- pharmacologie : Protéines recombinantes, Thiorédoxines.
- Cellules cultivées, Glutarédoxines, Humains, Oxydoréduction, Peroxirédoxines, Stress oxydatif.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Cells, Cultured (MeSH), Epithelial Cells (drug effects), Epithelial Cells (enzymology), Gene Expression Regulation, Enzymologic (drug effects), Glutaredoxins (MeSH), Humans (MeSH), Lens, Crystalline (drug effects), Lens, Crystalline (enzymology), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (biosynthesis), Oxidoreductases (genetics), Peroxidases (biosynthesis), Peroxidases (genetics), Peroxiredoxins (MeSH), Protein Disulfide Reductase (Glutathione) (biosynthesis), Protein Disulfide Reductase (Glutathione) (genetics), Recombinant Proteins (pharmacology), Reverse Transcriptase Polymerase Chain Reaction (methods), Superoxide Dismutase (biosynthesis), Superoxide Dismutase (genetics), Thioredoxins (pharmacology).
- MESH :
- chemical , biosynthesis : Oxidoreductases, Peroxidases, Protein Disulfide Reductase (Glutathione), Superoxide Dismutase.
- chemical , genetics : Oxidoreductases, Peroxidases, Protein Disulfide Reductase (Glutathione), Superoxide Dismutase.
- chemical , metabolism : Antioxidants.
- drug effects : Epithelial Cells, Gene Expression Regulation, Enzymologic, Lens, Crystalline.
- enzymology : Epithelial Cells, Lens, Crystalline.
- methods : Reverse Transcriptase Polymerase Chain Reaction.
- chemical , pharmacology : Recombinant Proteins, Thioredoxins.
- Cells, Cultured, Glutaredoxins, Humans, Oxidation-Reduction, Oxidative Stress, Peroxiredoxins.
Abstract
Thioredoxin (Trx) is one of the major redox-regulating proteins. It catalyzes dithiol/disulfide exchange reactions and displays many unique intracellular and extracellular activities thereby controlling multiple mammalian cell functions. In the present study we examine the effect of exogenous Trx on the expression of several antioxidant genes in human lens epithelial (HLE B3) cells. mRNA levels for gene expression were monitored by RT-PCR and real-time PCR while protein levels were measured by western blot analysis. We have found that recombinant human Trx (hTrx)-treated HLE B3 cells have a simultaneous increase in mRNA expressions of mitochondrial manganese superoxide dismutase (MnSOD), thioltranferase 1 (TTase 1) or glutaredoxin 1 (Grx1), mitochondrial thioltransferase (TTase 2) or glutaredoxin 2 (Grx2), and thioredoxin peroxidase IV (Prx IV). The increased MnSOD and TTase 1 mRNA expressions were accompanied with their respective increases in protein levels. Other antioxidant genes, including Cu/ZnSOD, catalase, glutathione peroxidase 1 (GPx1), thioredoxin reductase 1 (TrxR1), thioredoxin peroxidase III (Prx III), and gamma-glutamyl cysteine synthetase were not affected. The ability of Trx to induce selectively these antioxidant genes in the absence of oxidative stress suggest a cytokine/growth factor-like new physiological role of hTrx in HLE B3 cells. Our data also provide evidence of a strong antioxidant defense system in HLE B3 cells that can be activated by extracellular hTrx, as well as of a possible link between the thioredoxin (Trx) and glutathione (GSH) redox regulating systems in these cells.
DOI: 10.1016/j.exer.2006.03.018
PubMed: 16712839
Affiliations:
Links toward previous steps (curation, corpus...)
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Lou</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16712839</idno><idno type="pmid">16712839</idno><idno type="doi">10.1016/j.exer.2006.03.018</idno><idno type="wicri:Area/Main/Corpus">000D48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D48</idno><idno type="wicri:Area/Main/Curation">000D48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D48</idno><idno type="wicri:Area/Main/Exploration">000D48</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thioredoxin induced antioxidant gene expressions in human lens epithelial cells.</title><author><name sortKey="Yegorova, Svitlana" sort="Yegorova, Svitlana" uniqKey="Yegorova S" first="Svitlana" last="Yegorova">Svitlana Yegorova</name><affiliation wicri:level="1"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 134 VBS, Fair St./East Campus Loop, 68583-0905, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 134 VBS, Fair St./East Campus Loop, 68583-0905</wicri:regionArea><wicri:noRegion>68583-0905</wicri:noRegion></affiliation></author><author><name sortKey="Yegorov, Oleg" sort="Yegorov, Oleg" uniqKey="Yegorov O" first="Oleg" last="Yegorov">Oleg Yegorov</name></author><author><name sortKey="Lou, Marjorie F" sort="Lou, Marjorie F" uniqKey="Lou M" first="Marjorie F" last="Lou">Marjorie F. 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(biosynthesis)</term><term>Protein Disulfide Reductase (Glutathione) (genetics)</term><term>Recombinant Proteins (pharmacology)</term><term>Reverse Transcriptase Polymerase Chain Reaction (methods)</term><term>Superoxide Dismutase (biosynthesis)</term><term>Superoxide Dismutase (genetics)</term><term>Thioredoxins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (métabolisme)</term><term>Cellules cultivées (MeSH)</term><term>Cellules épithéliales (effets des médicaments et des substances chimiques)</term><term>Cellules épithéliales (enzymologie)</term><term>Cristallin (effets des médicaments et des substances chimiques)</term><term>Cristallin (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Oxidoreductases (biosynthèse)</term><term>Oxidoreductases (génétique)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (biosynthèse)</term><term>Peroxidases (génétique)</term><term>Peroxirédoxines (MeSH)</term><term>Protein-disulfide reductase (glutathione) (biosynthèse)</term><term>Protein-disulfide reductase (glutathione) (génétique)</term><term>Protéines recombinantes (pharmacologie)</term><term>RT-PCR (méthodes)</term><term>Régulation de l'expression des gènes codant pour des enzymes (effets des médicaments et des substances chimiques)</term><term>Stress oxydatif (MeSH)</term><term>Superoxide dismutase (biosynthèse)</term><term>Superoxide dismutase (génétique)</term><term>Thiorédoxines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Oxidoreductases</term><term>Peroxidases</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term><term>Peroxidases</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Oxidoreductases</term><term>Peroxidases</term><term>Protein-disulfide reductase (glutathione)</term><term>Superoxide dismutase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Epithelial Cells</term><term>Gene Expression Regulation, Enzymologic</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cellules épithéliales</term><term>Cristallin</term><term>Régulation de l'expression des gènes codant pour des enzymes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cellules épithéliales</term><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Epithelial Cells</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term><term>Peroxidases</term><term>Protein-disulfide reductase (glutathione)</term><term>Superoxide dismutase</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Reverse Transcriptase Polymerase Chain Reaction</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>RT-PCR</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cells, Cultured</term><term>Glutaredoxins</term><term>Humans</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules cultivées</term><term>Glutarédoxines</term><term>Humains</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin (Trx) is one of the major redox-regulating proteins. It catalyzes dithiol/disulfide exchange reactions and displays many unique intracellular and extracellular activities thereby controlling multiple mammalian cell functions. In the present study we examine the effect of exogenous Trx on the expression of several antioxidant genes in human lens epithelial (HLE B3) cells. mRNA levels for gene expression were monitored by RT-PCR and real-time PCR while protein levels were measured by western blot analysis. We have found that recombinant human Trx (hTrx)-treated HLE B3 cells have a simultaneous increase in mRNA expressions of mitochondrial manganese superoxide dismutase (MnSOD), thioltranferase 1 (TTase 1) or glutaredoxin 1 (Grx1), mitochondrial thioltransferase (TTase 2) or glutaredoxin 2 (Grx2), and thioredoxin peroxidase IV (Prx IV). The increased MnSOD and TTase 1 mRNA expressions were accompanied with their respective increases in protein levels. Other antioxidant genes, including Cu/ZnSOD, catalase, glutathione peroxidase 1 (GPx1), thioredoxin reductase 1 (TrxR1), thioredoxin peroxidase III (Prx III), and gamma-glutamyl cysteine synthetase were not affected. The ability of Trx to induce selectively these antioxidant genes in the absence of oxidative stress suggest a cytokine/growth factor-like new physiological role of hTrx in HLE B3 cells. Our data also provide evidence of a strong antioxidant defense system in HLE B3 cells that can be activated by extracellular hTrx, as well as of a possible link between the thioredoxin (Trx) and glutathione (GSH) redox regulating systems in these cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16712839</PMID><DateCompleted><Year>2006</Year><Month>11</Month><Day>09</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-4835</ISSN><JournalIssue CitedMedium="Print"><Volume>83</Volume><Issue>4</Issue><PubDate><Year>2006</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Experimental eye research</Title><ISOAbbreviation>Exp Eye Res</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin induced antioxidant gene expressions in human lens epithelial cells.</ArticleTitle><Pagination><MedlinePgn>783-92</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin (Trx) is one of the major redox-regulating proteins. It catalyzes dithiol/disulfide exchange reactions and displays many unique intracellular and extracellular activities thereby controlling multiple mammalian cell functions. In the present study we examine the effect of exogenous Trx on the expression of several antioxidant genes in human lens epithelial (HLE B3) cells. mRNA levels for gene expression were monitored by RT-PCR and real-time PCR while protein levels were measured by western blot analysis. We have found that recombinant human Trx (hTrx)-treated HLE B3 cells have a simultaneous increase in mRNA expressions of mitochondrial manganese superoxide dismutase (MnSOD), thioltranferase 1 (TTase 1) or glutaredoxin 1 (Grx1), mitochondrial thioltransferase (TTase 2) or glutaredoxin 2 (Grx2), and thioredoxin peroxidase IV (Prx IV). The increased MnSOD and TTase 1 mRNA expressions were accompanied with their respective increases in protein levels. Other antioxidant genes, including Cu/ZnSOD, catalase, glutathione peroxidase 1 (GPx1), thioredoxin reductase 1 (TrxR1), thioredoxin peroxidase III (Prx III), and gamma-glutamyl cysteine synthetase were not affected. The ability of Trx to induce selectively these antioxidant genes in the absence of oxidative stress suggest a cytokine/growth factor-like new physiological role of hTrx in HLE B3 cells. Our data also provide evidence of a strong antioxidant defense system in HLE B3 cells that can be activated by extracellular hTrx, as well as of a possible link between the thioredoxin (Trx) and glutathione (GSH) redox regulating systems in these cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yegorova</LastName><ForeName>Svitlana</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 134 VBS, Fair St./East Campus Loop, 68583-0905, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yegorov</LastName><ForeName>Oleg</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Lou</LastName><ForeName>Marjorie F</ForeName><Initials>MF</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01EY10595</GrantID><Acronym>EY</Acronym><Agency>NEI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>05</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Exp Eye Res</MedlineTA><NlmUniqueID>0370707</NlmUniqueID><ISSNLinking>0014-4835</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.15.1.1</RegistryNumber><NameOfSubstance UI="D013482">Superoxide Dismutase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007908" MajorTopicYN="N">Lens, Crystalline</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013482" MajorTopicYN="N">Superoxide Dismutase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>01</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>03</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>03</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>11</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16712839</ArticleId><ArticleId IdType="pii">S0014-4835(06)00203-X</ArticleId><ArticleId IdType="doi">10.1016/j.exer.2006.03.018</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Lou, Marjorie F" sort="Lou, Marjorie F" uniqKey="Lou M" first="Marjorie F" last="Lou">Marjorie F. Lou</name><name sortKey="Yegorov, Oleg" sort="Yegorov, Oleg" uniqKey="Yegorov O" first="Oleg" last="Yegorov">Oleg Yegorov</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Yegorova, Svitlana" sort="Yegorova, Svitlana" uniqKey="Yegorova S" first="Svitlana" last="Yegorova">Svitlana Yegorova</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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