Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress.
Identifieur interne : 000E09 ( Main/Exploration ); précédent : 000E08; suivant : 000E10Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress.
Auteurs : Sungchur Moon [États-Unis] ; M Rohan Fernando ; Marjorie F. LouSource :
- Investigative ophthalmology & visual science [ 0146-0404 ] ; 2005.
Descripteurs français
- KwdFr :
- ARN messager (métabolisme), Animaux (MeSH), Cataracte (anatomopathologie), Cataracte (enzymologie), Cataracte (induit chimiquement), Cristallin (anatomopathologie), Cristallin (effets des médicaments et des substances chimiques), Cristallin (enzymologie), Glutarédoxines (MeSH), Glutathion (métabolisme), Induction enzymatique (MeSH), Peroxyde d'hydrogène (toxicité), Protein-disulfide reductase (glutathione) (biosynthèse), Protein-disulfide reductase (glutathione) (génétique), RT-PCR (MeSH), Régulation positive (MeSH), Stress oxydatif (MeSH), Suidae (MeSH), Technique de Western (MeSH), Techniques de culture d'organes (MeSH), Thioredoxin-disulfide reductase (biosynthèse), Thioredoxin-disulfide reductase (génétique), Thiorédoxines (biosynthèse), Thiorédoxines (génétique).
- MESH :
- anatomopathologie : Cataracte, Cristallin.
- biosynthèse : Protein-disulfide reductase (glutathione), Thioredoxin-disulfide reductase, Thiorédoxines.
- effets des médicaments et des substances chimiques : Cristallin.
- enzymologie : Cataracte, Cristallin.
- génétique : Protein-disulfide reductase (glutathione), Thioredoxin-disulfide reductase, Thiorédoxines.
- induit chimiquement : Cataracte.
- métabolisme : ARN messager, Glutathion.
- toxicité : Peroxyde d'hydrogène.
- Animaux, Glutarédoxines, Induction enzymatique, RT-PCR, Régulation positive, Stress oxydatif, Suidae, Technique de Western, Techniques de culture d'organes.
English descriptors
- KwdEn :
- Animals (MeSH), Blotting, Western (MeSH), Cataract (chemically induced), Cataract (enzymology), Cataract (pathology), Enzyme Induction (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Hydrogen Peroxide (toxicity), Lens, Crystalline (drug effects), Lens, Crystalline (enzymology), Lens, Crystalline (pathology), Organ Culture Techniques (MeSH), Oxidative Stress (MeSH), Protein Disulfide Reductase (Glutathione) (biosynthesis), Protein Disulfide Reductase (Glutathione) (genetics), RNA, Messenger (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Swine (MeSH), Thioredoxin-Disulfide Reductase (biosynthesis), Thioredoxin-Disulfide Reductase (genetics), Thioredoxins (biosynthesis), Thioredoxins (genetics), Up-Regulation (MeSH).
- MESH :
- chemical , biosynthesis : Protein Disulfide Reductase (Glutathione), Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , genetics : Protein Disulfide Reductase (Glutathione), Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , metabolism : Glutathione, RNA, Messenger.
- chemical , toxicity : Hydrogen Peroxide.
- chemical : Glutaredoxins.
- chemically induced : Cataract.
- drug effects : Lens, Crystalline.
- enzymology : Cataract, Lens, Crystalline.
- pathology : Cataract, Lens, Crystalline.
- Animals, Blotting, Western, Enzyme Induction, Organ Culture Techniques, Oxidative Stress, Reverse Transcriptase Polymerase Chain Reaction, Swine, Up-Regulation.
Abstract
PURPOSE
In view of the important antioxidant roles of thioltransferase (TTase), thioredoxin (Trx), and thioredoxin reductase (TR) in the lens, the present study was conducted to investigate the induction of these cytosolic enzymes in response to H(2)O(2) stress in cultured lenses.
METHODS
Porcine lenses were cultured, exposed to H(2)O(2) for various lengths of time between 0 and 24 hours, and photographed to detect morphologic changes. The lenses were then harvested; dissected into epithelial layer, cortex, and nucleus; and homogenized for the determination of the glutathione (GSH) level. Pooled epithelial layers were used to examine TTase, Trx, and TR protein or mRNA levels.
RESULTS
Treatment of lenses with H(2)O(2) caused distinct morphologic changes. Lower concentrations of H(2)O(2) (0.2 mM) caused the lens to be hazy after 6 hours and to worsen progressively between 12 and 24 hours. Higher levels of H(2)O(2) (0.5 mM) induced similar morphologic changes, but sooner (within 1 hour) and more severe. Both H(2)O(2)-treated groups showed a dramatic and gradual GSH depletion during the 24-hour incubation, but the GSH level at 50% or above appeared to be essential in maintaining lens clarity. However, TTase, Trx, and TR activities, protein expressions, and mRNA transcriptions in the epithelial layers of these lenses were increased, but each enzyme had a distinct pattern. Under mild H(2)O(2) stress, a slow and transient activation of TTase, Trx, and TR was observed. However, under stronger H(2)O(2) stress, all three enzymes showed a very rapid increase and then a steady decline in activity. Western blot and RT-PCR analyses revealed that this increase in activity in all three enzymes was due to the induction of protein and mRNA expression. In the control group (no oxidative stress) all three enzyme activities and their respective expressions remained constant throughout the experimental period.
CONCLUSIONS
The data show that TTase, Trx, and TR activity and expression are induced in lens cells under oxidative stress, probably to protect and maintain the health of the lens.
DOI: 10.1167/iovs.05-0237
PubMed: 16186363
Affiliations:
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Lou</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16186363</idno><idno type="pmid">16186363</idno><idno type="doi">10.1167/iovs.05-0237</idno><idno type="wicri:Area/Main/Corpus">000D88</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D88</idno><idno type="wicri:Area/Main/Curation">000D88</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D88</idno><idno type="wicri:Area/Main/Exploration">000D88</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress.</title><author><name sortKey="Moon, Sungchur" sort="Moon, Sungchur" uniqKey="Moon S" first="Sungchur" last="Moon">Sungchur Moon</name><affiliation wicri:level="1"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 68583, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 68583</wicri:regionArea><wicri:noRegion>68583</wicri:noRegion></affiliation></author><author><name sortKey="Fernando, M Rohan" sort="Fernando, M Rohan" uniqKey="Fernando M" first="M Rohan" last="Fernando">M Rohan Fernando</name></author><author><name sortKey="Lou, Marjorie F" sort="Lou, Marjorie F" uniqKey="Lou M" first="Marjorie F" last="Lou">Marjorie F. Lou</name></author></analytic><series><title level="j">Investigative ophthalmology & visual science</title><idno type="ISSN">0146-0404</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Blotting, Western (MeSH)</term><term>Cataract (chemically induced)</term><term>Cataract (enzymology)</term><term>Cataract (pathology)</term><term>Enzyme Induction (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Hydrogen Peroxide (toxicity)</term><term>Lens, Crystalline (drug effects)</term><term>Lens, Crystalline (enzymology)</term><term>Lens, Crystalline (pathology)</term><term>Organ Culture Techniques (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (biosynthesis)</term><term>Protein Disulfide Reductase (Glutathione) (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Swine (MeSH)</term><term>Thioredoxin-Disulfide Reductase (biosynthesis)</term><term>Thioredoxin-Disulfide Reductase (genetics)</term><term>Thioredoxins (biosynthesis)</term><term>Thioredoxins (genetics)</term><term>Up-Regulation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term><term>Animaux (MeSH)</term><term>Cataracte (anatomopathologie)</term><term>Cataracte (enzymologie)</term><term>Cataracte (induit chimiquement)</term><term>Cristallin (anatomopathologie)</term><term>Cristallin (effets des médicaments et des substances chimiques)</term><term>Cristallin (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Induction enzymatique (MeSH)</term><term>Peroxyde d'hydrogène (toxicité)</term><term>Protein-disulfide reductase (glutathione) (biosynthèse)</term><term>Protein-disulfide reductase (glutathione) (génétique)</term><term>RT-PCR (MeSH)</term><term>Régulation positive (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Suidae (MeSH)</term><term>Technique de Western (MeSH)</term><term>Techniques de culture d'organes (MeSH)</term><term>Thioredoxin-disulfide reductase (biosynthèse)</term><term>Thioredoxin-disulfide reductase (génétique)</term><term>Thiorédoxines (biosynthèse)</term><term>Thiorédoxines (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Protein Disulfide Reductase (Glutathione)</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein Disulfide Reductase (Glutathione)</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Cataracte</term><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="chemically induced" xml:lang="en"><term>Cataract</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cataracte</term><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cataract</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="induit chimiquement" xml:lang="fr"><term>Cataracte</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Cataract</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Enzyme Induction</term><term>Organ Culture Techniques</term><term>Oxidative Stress</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Swine</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glutarédoxines</term><term>Induction enzymatique</term><term>RT-PCR</term><term>Régulation positive</term><term>Stress oxydatif</term><term>Suidae</term><term>Technique de Western</term><term>Techniques de culture d'organes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>PURPOSE</b></p><p>In view of the important antioxidant roles of thioltransferase (TTase), thioredoxin (Trx), and thioredoxin reductase (TR) in the lens, the present study was conducted to investigate the induction of these cytosolic enzymes in response to H(2)O(2) stress in cultured lenses.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>Porcine lenses were cultured, exposed to H(2)O(2) for various lengths of time between 0 and 24 hours, and photographed to detect morphologic changes. The lenses were then harvested; dissected into epithelial layer, cortex, and nucleus; and homogenized for the determination of the glutathione (GSH) level. Pooled epithelial layers were used to examine TTase, Trx, and TR protein or mRNA levels.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Treatment of lenses with H(2)O(2) caused distinct morphologic changes. Lower concentrations of H(2)O(2) (0.2 mM) caused the lens to be hazy after 6 hours and to worsen progressively between 12 and 24 hours. Higher levels of H(2)O(2) (0.5 mM) induced similar morphologic changes, but sooner (within 1 hour) and more severe. Both H(2)O(2)-treated groups showed a dramatic and gradual GSH depletion during the 24-hour incubation, but the GSH level at 50% or above appeared to be essential in maintaining lens clarity. However, TTase, Trx, and TR activities, protein expressions, and mRNA transcriptions in the epithelial layers of these lenses were increased, but each enzyme had a distinct pattern. Under mild H(2)O(2) stress, a slow and transient activation of TTase, Trx, and TR was observed. However, under stronger H(2)O(2) stress, all three enzymes showed a very rapid increase and then a steady decline in activity. Western blot and RT-PCR analyses revealed that this increase in activity in all three enzymes was due to the induction of protein and mRNA expression. In the control group (no oxidative stress) all three enzyme activities and their respective expressions remained constant throughout the experimental period.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>The data show that TTase, Trx, and TR activity and expression are induced in lens cells under oxidative stress, probably to protect and maintain the health of the lens.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16186363</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>21</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0146-0404</ISSN><JournalIssue CitedMedium="Print"><Volume>46</Volume><Issue>10</Issue><PubDate><Year>2005</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Investigative ophthalmology & visual science</Title><ISOAbbreviation>Invest Ophthalmol Vis Sci</ISOAbbreviation></Journal><ArticleTitle>Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress.</ArticleTitle><Pagination><MedlinePgn>3783-9</MedlinePgn></Pagination><Abstract><AbstractText Label="PURPOSE" NlmCategory="OBJECTIVE">In view of the important antioxidant roles of thioltransferase (TTase), thioredoxin (Trx), and thioredoxin reductase (TR) in the lens, the present study was conducted to investigate the induction of these cytosolic enzymes in response to H(2)O(2) stress in cultured lenses.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">Porcine lenses were cultured, exposed to H(2)O(2) for various lengths of time between 0 and 24 hours, and photographed to detect morphologic changes. The lenses were then harvested; dissected into epithelial layer, cortex, and nucleus; and homogenized for the determination of the glutathione (GSH) level. Pooled epithelial layers were used to examine TTase, Trx, and TR protein or mRNA levels.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Treatment of lenses with H(2)O(2) caused distinct morphologic changes. Lower concentrations of H(2)O(2) (0.2 mM) caused the lens to be hazy after 6 hours and to worsen progressively between 12 and 24 hours. Higher levels of H(2)O(2) (0.5 mM) induced similar morphologic changes, but sooner (within 1 hour) and more severe. Both H(2)O(2)-treated groups showed a dramatic and gradual GSH depletion during the 24-hour incubation, but the GSH level at 50% or above appeared to be essential in maintaining lens clarity. However, TTase, Trx, and TR activities, protein expressions, and mRNA transcriptions in the epithelial layers of these lenses were increased, but each enzyme had a distinct pattern. Under mild H(2)O(2) stress, a slow and transient activation of TTase, Trx, and TR was observed. However, under stronger H(2)O(2) stress, all three enzymes showed a very rapid increase and then a steady decline in activity. Western blot and RT-PCR analyses revealed that this increase in activity in all three enzymes was due to the induction of protein and mRNA expression. In the control group (no oxidative stress) all three enzyme activities and their respective expressions remained constant throughout the experimental period.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">The data show that TTase, Trx, and TR activity and expression are induced in lens cells under oxidative stress, probably to protect and maintain the health of the lens.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moon</LastName><ForeName>Sungchur</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 68583, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernando</LastName><ForeName>M Rohan</ForeName><Initials>MR</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><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Invest Ophthalmol Vis Sci</MedlineTA><NlmUniqueID>7703701</NlmUniqueID><ISSNLinking>0146-0404</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002386" MajorTopicYN="N">Cataract</DescriptorName><QualifierName UI="Q000139" MajorTopicYN="N">chemically induced</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004790" MajorTopicYN="N">Enzyme Induction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007908" MajorTopicYN="N">Lens, Crystalline</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009924" MajorTopicYN="N">Organ Culture Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015854" MajorTopicYN="N">Up-Regulation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>9</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>12</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>9</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16186363</ArticleId><ArticleId IdType="pii">46/10/3783</ArticleId><ArticleId IdType="doi">10.1167/iovs.05-0237</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Fernando, M Rohan" sort="Fernando, M Rohan" uniqKey="Fernando M" first="M Rohan" last="Fernando">M Rohan Fernando</name><name sortKey="Lou, Marjorie F" sort="Lou, Marjorie F" uniqKey="Lou M" first="Marjorie F" last="Lou">Marjorie F. Lou</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Moon, Sungchur" sort="Moon, Sungchur" uniqKey="Moon S" first="Sungchur" last="Moon">Sungchur Moon</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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