Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse.
Identifieur interne : 000C11 ( Main/Exploration ); précédent : 000C10; suivant : 000C12Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse.
Auteurs : Stefan Löfgren [États-Unis] ; M Rohan Fernando ; Kui-Yi Xing ; Yin Wang ; Charles A. Kuszynski ; Ye-Shih Ho ; Marjorie F. LouSource :
- Investigative ophthalmology & visual science [ 1552-5783 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Apoptose (MeSH), Cellules cultivées (MeSH), Cellules épithéliales (cytologie), Cellules épithéliales (métabolisme), Chaine A de la cristalline alpha (métabolisme), Cristallin (cytologie), Cristallin (métabolisme), Cytométrie en flux (MeSH), Cytosol (MeSH), Glutarédoxines (pharmacologie), Glutarédoxines (physiologie), Glutathion (physiologie), Glyceraldehyde 3-phosphate dehydrogenases (métabolisme), Peroxyde d'hydrogène (toxicité), Prolifération cellulaire (MeSH), Protéines recombinantes (pharmacologie), Souris (MeSH), Souris de lignée C57BL (MeSH), Souris knockout (MeSH), Stress oxydatif (MeSH), Survie cellulaire (MeSH), Technique de Northern (MeSH), Technique de Western (MeSH).
- MESH :
- cytologie : Cellules épithéliales, Cristallin.
- métabolisme : Cellules épithéliales, Chaine A de la cristalline alpha, Cristallin, Glyceraldehyde 3-phosphate dehydrogenases.
- pharmacologie : Glutarédoxines, Protéines recombinantes.
- physiologie : Glutarédoxines, Glutathion.
- toxicité : Peroxyde d'hydrogène.
- Animaux, Apoptose, Cellules cultivées, Cytométrie en flux, Cytosol, Prolifération cellulaire, Souris, Souris de lignée C57BL, Souris knockout, Stress oxydatif, Survie cellulaire, Technique de Northern, Technique de Western.
English descriptors
- KwdEn :
- Animals (MeSH), Apoptosis (MeSH), Blotting, Northern (MeSH), Blotting, Western (MeSH), Cell Proliferation (MeSH), Cell Survival (MeSH), Cells, Cultured (MeSH), Cytosol (MeSH), Epithelial Cells (cytology), Epithelial Cells (metabolism), Flow Cytometry (MeSH), Glutaredoxins (pharmacology), Glutaredoxins (physiology), Glutathione (physiology), Glyceraldehyde-3-Phosphate Dehydrogenases (metabolism), Hydrogen Peroxide (toxicity), Lens, Crystalline (cytology), Lens, Crystalline (metabolism), Mice (MeSH), Mice, Inbred C57BL (MeSH), Mice, Knockout (MeSH), Oxidative Stress (MeSH), Recombinant Proteins (pharmacology), alpha-Crystallin A Chain (metabolism).
- MESH :
- chemical , metabolism : Glyceraldehyde-3-Phosphate Dehydrogenases, alpha-Crystallin A Chain.
- chemical , pharmacology : Glutaredoxins, Recombinant Proteins.
- cytology : Epithelial Cells, Lens, Crystalline.
- metabolism : Epithelial Cells, Lens, Crystalline.
- chemical , physiology : Glutaredoxins, Glutathione.
- chemical , toxicity : Hydrogen Peroxide.
- Animals, Apoptosis, Blotting, Northern, Blotting, Western, Cell Proliferation, Cell Survival, Cells, Cultured, Cytosol, Flow Cytometry, Mice, Mice, Inbred C57BL, Mice, Knockout, Oxidative Stress.
Abstract
PURPOSE
To examine the physiological function of the thioltransferase (TTase)/glutathione (GSH) system in the lens using TTase knockout mouse (TTase(-/-)) lens epithelial cells (LECs) as a model.
METHODS
Primary LEC cultures were obtained from wild-type (TTase(+/+)) and TTase(-/-) mice. Characterization and validation of the cells were determined by immunoblotting for TTase and alpha-crystallin proteins and by immunohistochemistry for glutathionylated proteins. Cell proliferation was examined by 3-(4,5-dimethyl-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium and BrdU analysis, and cell apoptosis after H(2)O(2) stress was assessed by fluorescence-activated cell sorter analysis. Reloading of TTase protein into the TTase(-/-) cells was achieved with reagent.
RESULTS
Primary LEC cultures obtained from wild-type (TTase(+/+)) and TTase(-/-) mice were characterized and found to contain lens-specific alpha-crystallin protein. Western blot analysis confirmed the absence of TTase protein in the TTase(-/-) cells and its presence in the wild-type cells. TTase(-/-) LECs had significantly lower levels of glutathione (GSH) and protein thiols with extensive elevation of glutathionylated proteins, and they exhibited less resistance to oxidative stress than did TTase(+/+) cells. These cells were less viable and more apoptotic, and they had a reduced ability to remove H(2)O(2) after challenge with low levels of H(2)O(2). Reloading of purified TTase into the TTase(-/-) cells restored the antioxidant function in TTase(-/-) cells to a near normal state.
CONCLUSIONS
These findings confirm the importance of TTase in regulating redox homeostasis and suggest a new physiological function in controlling cell proliferation in the lens epithelial cells.
DOI: 10.1167/iovs.07-1404
PubMed: 18586881
Affiliations:
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Kuszynski</name></author><author><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18586881</idno><idno type="pmid">18586881</idno><idno type="doi">10.1167/iovs.07-1404</idno><idno type="wicri:Area/Main/Corpus">000B77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B77</idno><idno type="wicri:Area/Main/Curation">000B77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B77</idno><idno type="wicri:Area/Main/Exploration">000B77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse.</title><author><name sortKey="Lofgren, Stefan" sort="Lofgren, Stefan" uniqKey="Lofgren S" first="Stefan" last="Löfgren">Stefan Löfgren</name><affiliation wicri:level="1"><nlm:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0905, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0905</wicri:regionArea><wicri:noRegion>Nebraska 68583-0905</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="Xing, Kui Yi" sort="Xing, Kui Yi" uniqKey="Xing K" first="Kui-Yi" last="Xing">Kui-Yi Xing</name></author><author><name sortKey="Wang, Yin" sort="Wang, Yin" uniqKey="Wang Y" first="Yin" last="Wang">Yin Wang</name></author><author><name sortKey="Kuszynski, Charles A" sort="Kuszynski, Charles A" uniqKey="Kuszynski C" first="Charles A" last="Kuszynski">Charles A. Kuszynski</name></author><author><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</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="eISSN">1552-5783</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Apoptosis (MeSH)</term><term>Blotting, Northern (MeSH)</term><term>Blotting, Western (MeSH)</term><term>Cell Proliferation (MeSH)</term><term>Cell Survival (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Cytosol (MeSH)</term><term>Epithelial Cells (cytology)</term><term>Epithelial Cells (metabolism)</term><term>Flow Cytometry (MeSH)</term><term>Glutaredoxins (pharmacology)</term><term>Glutaredoxins (physiology)</term><term>Glutathione (physiology)</term><term>Glyceraldehyde-3-Phosphate Dehydrogenases (metabolism)</term><term>Hydrogen Peroxide (toxicity)</term><term>Lens, Crystalline (cytology)</term><term>Lens, Crystalline (metabolism)</term><term>Mice (MeSH)</term><term>Mice, Inbred C57BL (MeSH)</term><term>Mice, Knockout (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Recombinant Proteins (pharmacology)</term><term>alpha-Crystallin A Chain (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Apoptose (MeSH)</term><term>Cellules cultivées (MeSH)</term><term>Cellules épithéliales (cytologie)</term><term>Cellules épithéliales (métabolisme)</term><term>Chaine A de la cristalline alpha (métabolisme)</term><term>Cristallin (cytologie)</term><term>Cristallin (métabolisme)</term><term>Cytométrie en flux (MeSH)</term><term>Cytosol (MeSH)</term><term>Glutarédoxines (pharmacologie)</term><term>Glutarédoxines (physiologie)</term><term>Glutathion (physiologie)</term><term>Glyceraldehyde 3-phosphate dehydrogenases (métabolisme)</term><term>Peroxyde d'hydrogène (toxicité)</term><term>Prolifération cellulaire (MeSH)</term><term>Protéines recombinantes (pharmacologie)</term><term>Souris (MeSH)</term><term>Souris de lignée C57BL (MeSH)</term><term>Souris knockout (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Survie cellulaire (MeSH)</term><term>Technique de Northern (MeSH)</term><term>Technique de Western (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glyceraldehyde-3-Phosphate Dehydrogenases</term><term>alpha-Crystallin A Chain</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glutaredoxins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules épithéliales</term><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Epithelial Cells</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules épithéliales</term><term>Chaine A de la cristalline alpha</term><term>Cristallin</term><term>Glyceraldehyde 3-phosphate dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Hydrogen Peroxide</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>Apoptosis</term><term>Blotting, Northern</term><term>Blotting, Western</term><term>Cell Proliferation</term><term>Cell Survival</term><term>Cells, Cultured</term><term>Cytosol</term><term>Flow Cytometry</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Apoptose</term><term>Cellules cultivées</term><term>Cytométrie en flux</term><term>Cytosol</term><term>Prolifération cellulaire</term><term>Souris</term><term>Souris de lignée C57BL</term><term>Souris knockout</term><term>Stress oxydatif</term><term>Survie cellulaire</term><term>Technique de Northern</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>PURPOSE</b></p><p>To examine the physiological function of the thioltransferase (TTase)/glutathione (GSH) system in the lens using TTase knockout mouse (TTase(-/-)) lens epithelial cells (LECs) as a model.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>Primary LEC cultures were obtained from wild-type (TTase(+/+)) and TTase(-/-) mice. Characterization and validation of the cells were determined by immunoblotting for TTase and alpha-crystallin proteins and by immunohistochemistry for glutathionylated proteins. Cell proliferation was examined by 3-(4,5-dimethyl-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium and BrdU analysis, and cell apoptosis after H(2)O(2) stress was assessed by fluorescence-activated cell sorter analysis. Reloading of TTase protein into the TTase(-/-) cells was achieved with reagent.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Primary LEC cultures obtained from wild-type (TTase(+/+)) and TTase(-/-) mice were characterized and found to contain lens-specific alpha-crystallin protein. Western blot analysis confirmed the absence of TTase protein in the TTase(-/-) cells and its presence in the wild-type cells. TTase(-/-) LECs had significantly lower levels of glutathione (GSH) and protein thiols with extensive elevation of glutathionylated proteins, and they exhibited less resistance to oxidative stress than did TTase(+/+) cells. These cells were less viable and more apoptotic, and they had a reduced ability to remove H(2)O(2) after challenge with low levels of H(2)O(2). Reloading of purified TTase into the TTase(-/-) cells restored the antioxidant function in TTase(-/-) cells to a near normal state.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>These findings confirm the importance of TTase in regulating redox homeostasis and suggest a new physiological function in controlling cell proliferation in the lens epithelial cells.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18586881</PMID><DateCompleted><Year>2008</Year><Month>10</Month><Day>10</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1552-5783</ISSN><JournalIssue CitedMedium="Internet"><Volume>49</Volume><Issue>10</Issue><PubDate><Year>2008</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Investigative ophthalmology & visual science</Title><ISOAbbreviation>Invest Ophthalmol Vis Sci</ISOAbbreviation></Journal><ArticleTitle>Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse.</ArticleTitle><Pagination><MedlinePgn>4497-505</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1167/iovs.07-1404</ELocationID><Abstract><AbstractText Label="PURPOSE" NlmCategory="OBJECTIVE">To examine the physiological function of the thioltransferase (TTase)/glutathione (GSH) system in the lens using TTase knockout mouse (TTase(-/-)) lens epithelial cells (LECs) as a model.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">Primary LEC cultures were obtained from wild-type (TTase(+/+)) and TTase(-/-) mice. Characterization and validation of the cells were determined by immunoblotting for TTase and alpha-crystallin proteins and by immunohistochemistry for glutathionylated proteins. Cell proliferation was examined by 3-(4,5-dimethyl-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium and BrdU analysis, and cell apoptosis after H(2)O(2) stress was assessed by fluorescence-activated cell sorter analysis. Reloading of TTase protein into the TTase(-/-) cells was achieved with reagent.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Primary LEC cultures obtained from wild-type (TTase(+/+)) and TTase(-/-) mice were characterized and found to contain lens-specific alpha-crystallin protein. Western blot analysis confirmed the absence of TTase protein in the TTase(-/-) cells and its presence in the wild-type cells. TTase(-/-) LECs had significantly lower levels of glutathione (GSH) and protein thiols with extensive elevation of glutathionylated proteins, and they exhibited less resistance to oxidative stress than did TTase(+/+) cells. These cells were less viable and more apoptotic, and they had a reduced ability to remove H(2)O(2) after challenge with low levels of H(2)O(2). Reloading of purified TTase into the TTase(-/-) cells restored the antioxidant function in TTase(-/-) cells to a near normal state.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">These findings confirm the importance of TTase in regulating redox homeostasis and suggest a new physiological function in controlling cell proliferation in the lens epithelial cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Löfgren</LastName><ForeName>Stefan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0905, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernando</LastName><ForeName>M Rohan</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Xing</LastName><ForeName>Kui-Yi</ForeName><Initials>KY</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yin</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kuszynski</LastName><ForeName>Charles A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Ye-Shih</ForeName><Initials>YS</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>R01 EY10595</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="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>06</Month><Day>27</Day></ArticleDate></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="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D038202">alpha-Crystallin A Chain</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.-</RegistryNumber><NameOfSubstance UI="D005987">Glyceraldehyde-3-Phosphate Dehydrogenases</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="D017209" MajorTopicYN="N">Apoptosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015152" MajorTopicYN="N">Blotting, Northern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049109" MajorTopicYN="Y">Cell Proliferation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005434" MajorTopicYN="N">Flow Cytometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005987" MajorTopicYN="N">Glyceraldehyde-3-Phosphate Dehydrogenases</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="Q000166" MajorTopicYN="Y">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018345" MajorTopicYN="N">Mice, Knockout</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D038202" MajorTopicYN="N">alpha-Crystallin A Chain</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>7</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>10</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>7</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18586881</ArticleId><ArticleId IdType="pii">iovs.07-1404</ArticleId><ArticleId IdType="doi">10.1167/iovs.07-1404</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="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</name><name sortKey="Kuszynski, Charles A" sort="Kuszynski, Charles A" uniqKey="Kuszynski C" first="Charles A" last="Kuszynski">Charles A. Kuszynski</name><name sortKey="Lou, Marjorie F" sort="Lou, Marjorie F" uniqKey="Lou M" first="Marjorie F" last="Lou">Marjorie F. Lou</name><name sortKey="Wang, Yin" sort="Wang, Yin" uniqKey="Wang Y" first="Yin" last="Wang">Yin Wang</name><name sortKey="Xing, Kui Yi" sort="Xing, Kui Yi" uniqKey="Xing K" first="Kui-Yi" last="Xing">Kui-Yi Xing</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Lofgren, Stefan" sort="Lofgren, Stefan" uniqKey="Lofgren S" first="Stefan" last="Löfgren">Stefan Löfgren</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|clé= pubmed:18586881
|texte= Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:18586881" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |