Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells.
Identifieur interne : 000947 ( Main/Exploration ); précédent : 000946; suivant : 000948Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells.
Auteurs : Hongli Wu [États-Unis] ; Liren Lin ; Frank Giblin ; Ye-Sheh Ho ; Marjorie F. LouSource :
- Free radical biology & medicine [ 1873-4596 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules épithéliales (effets des médicaments et des substances chimiques), Cellules épithéliales (métabolisme), Cristallin (cytologie), Cristallin (métabolisme), Glutarédoxines (déficit), Glutarédoxines (métabolisme), Peroxyde d'hydrogène (pharmacologie), Souris (MeSH), Souris de lignée C57BL (MeSH), Souris knockout (MeSH), Stress oxydatif (effets des médicaments et des substances chimiques), Survie cellulaire (effets des médicaments et des substances chimiques).
- MESH :
- cytologie : Cristallin.
- déficit : Glutarédoxines.
- effets des médicaments et des substances chimiques : Cellules épithéliales, Stress oxydatif, Survie cellulaire.
- métabolisme : Cellules épithéliales, Cristallin, Glutarédoxines.
- pharmacologie : Peroxyde d'hydrogène.
- Animaux, Souris, Souris de lignée C57BL, Souris knockout.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Survival (drug effects), Epithelial Cells (drug effects), Epithelial Cells (metabolism), Glutaredoxins (deficiency), Glutaredoxins (metabolism), Hydrogen Peroxide (pharmacology), Lens, Crystalline (cytology), Lens, Crystalline (metabolism), Mice (MeSH), Mice, Inbred C57BL (MeSH), Mice, Knockout (MeSH), Oxidative Stress (drug effects).
- MESH :
- chemical , deficiency : Glutaredoxins.
- cytology : Lens, Crystalline.
- drug effects : Cell Survival, Epithelial Cells, Oxidative Stress.
- metabolism : Epithelial Cells, Glutaredoxins, Lens, Crystalline.
- chemical , pharmacology : Hydrogen Peroxide.
- Animals, Mice, Mice, Inbred C57BL, Mice, Knockout.
Abstract
Glutaredoxin belongs to the oxidoreductase family, with cytosolic glutaredoxin 1 (Grx1) and mitochondrial glutaredoxin 2 (Grx2) isoforms. Of the two isozymes, the function of Grx2 is not well understood. This paper describes the effects of Grx2 deletion on cellular function using primary lens epithelial cell cultures isolated from Grx2 gene knockout (KO) and wild-type (WT) mice. We found that both cell types showed similar growth patterns and morphology and comparable mitochondrial glutathione pool and complex I activity. Cells with deleted Grx2 did not show affected Grx1 or thioredoxin expression but exhibited high sensitivity to oxidative stress. Under treatment with H(2)O(2), the KO cells showed less viability, higher membrane leakage, enhanced ATP loss and complex I inactivation, and weakened ability to detoxify H(2)O(2) in comparison with the WT cells. The KO cells had higher glutathionylation in the mitochondrial proteins, particularly the 75-kDa subunit of complex I. Recombinant Grx2 deglutathionylated complex I and restored most of its activity. We conclude that Grx2 has a function that protects cells against H(2)O(2)-induced injury via its peroxidase and dethiolase activities; particularly, Grx2 prevents complex I inactivation and preserves mitochondrial function.
DOI: 10.1016/j.freeradbiomed.2011.09.011
PubMed: 21983434
PubMed Central: PMC3235406
Affiliations:
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Lou</name></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cell Survival (drug effects)</term><term>Epithelial Cells (drug effects)</term><term>Epithelial Cells (metabolism)</term><term>Glutaredoxins (deficiency)</term><term>Glutaredoxins (metabolism)</term><term>Hydrogen Peroxide (pharmacology)</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 (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules épithéliales (effets des médicaments et des substances chimiques)</term><term>Cellules épithéliales (métabolisme)</term><term>Cristallin (cytologie)</term><term>Cristallin (métabolisme)</term><term>Glutarédoxines (déficit)</term><term>Glutarédoxines (métabolisme)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Souris (MeSH)</term><term>Souris de lignée C57BL (MeSH)</term><term>Souris knockout (MeSH)</term><term>Stress oxydatif (effets des médicaments et des substances chimiques)</term><term>Survie cellulaire (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cristallin</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Survival</term><term>Epithelial Cells</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cellules épithéliales</term><term>Stress oxydatif</term><term>Survie cellulaire</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term><term>Glutaredoxins</term><term>Lens, Crystalline</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules épithéliales</term><term>Cristallin</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Souris</term><term>Souris de lignée C57BL</term><term>Souris knockout</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin belongs to the oxidoreductase family, with cytosolic glutaredoxin 1 (Grx1) and mitochondrial glutaredoxin 2 (Grx2) isoforms. Of the two isozymes, the function of Grx2 is not well understood. This paper describes the effects of Grx2 deletion on cellular function using primary lens epithelial cell cultures isolated from Grx2 gene knockout (KO) and wild-type (WT) mice. We found that both cell types showed similar growth patterns and morphology and comparable mitochondrial glutathione pool and complex I activity. Cells with deleted Grx2 did not show affected Grx1 or thioredoxin expression but exhibited high sensitivity to oxidative stress. Under treatment with H(2)O(2), the KO cells showed less viability, higher membrane leakage, enhanced ATP loss and complex I inactivation, and weakened ability to detoxify H(2)O(2) in comparison with the WT cells. The KO cells had higher glutathionylation in the mitochondrial proteins, particularly the 75-kDa subunit of complex I. Recombinant Grx2 deglutathionylated complex I and restored most of its activity. We conclude that Grx2 has a function that protects cells against H(2)O(2)-induced injury via its peroxidase and dethiolase activities; particularly, Grx2 prevents complex I inactivation and preserves mitochondrial function.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21983434</PMID><DateCompleted><Year>2012</Year><Month>03</Month><Day>28</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>51</Volume><Issue>11</Issue><PubDate><Year>2011</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells.</ArticleTitle><Pagination><MedlinePgn>2108-17</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2011.09.011</ELocationID><Abstract><AbstractText>Glutaredoxin belongs to the oxidoreductase family, with cytosolic glutaredoxin 1 (Grx1) and mitochondrial glutaredoxin 2 (Grx2) isoforms. Of the two isozymes, the function of Grx2 is not well understood. This paper describes the effects of Grx2 deletion on cellular function using primary lens epithelial cell cultures isolated from Grx2 gene knockout (KO) and wild-type (WT) mice. We found that both cell types showed similar growth patterns and morphology and comparable mitochondrial glutathione pool and complex I activity. Cells with deleted Grx2 did not show affected Grx1 or thioredoxin expression but exhibited high sensitivity to oxidative stress. Under treatment with H(2)O(2), the KO cells showed less viability, higher membrane leakage, enhanced ATP loss and complex I inactivation, and weakened ability to detoxify H(2)O(2) in comparison with the WT cells. The KO cells had higher glutathionylation in the mitochondrial proteins, particularly the 75-kDa subunit of complex I. Recombinant Grx2 deglutathionylated complex I and restored most of its activity. We conclude that Grx2 has a function that protects cells against H(2)O(2)-induced injury via its peroxidase and dethiolase activities; particularly, Grx2 prevents complex I inactivation and preserves mitochondrial function.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>HongLi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Center of Redox Biology and School of Veterinary Medicine and Biomedical Sciences, University of Nebraska at Lincoln, NE 68583, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>LiRen</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Giblin</LastName><ForeName>Frank</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Ye-Sheh</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 EY010595</GrantID><Acronym>EY</Acronym><Agency>NEI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 EY010595-17</GrantID><Acronym>EY</Acronym><Agency>NEI NIH HHS</Agency><Country>United States</Country></Grant><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>2011</Year><Month>09</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516009">Glrx2 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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IdType="pubmed">10998251</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Nebraska</li></region></list><tree><noCountry><name sortKey="Giblin, Frank" sort="Giblin, Frank" uniqKey="Giblin F" first="Frank" last="Giblin">Frank Giblin</name><name sortKey="Ho, Ye Sheh" sort="Ho, Ye Sheh" uniqKey="Ho Y" first="Ye-Sheh" last="Ho">Ye-Sheh Ho</name><name sortKey="Lin, Liren" sort="Lin, Liren" uniqKey="Lin L" first="Liren" last="Lin">Liren Lin</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"><region name="Nebraska"><name sortKey="Wu, Hongli" sort="Wu, Hongli" uniqKey="Wu H" first="Hongli" last="Wu">Hongli Wu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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