The glutaredoxin/S-glutathionylation axis regulates interleukin-17A-induced proinflammatory responses in lung epithelial cells in association with S-glutathionylation of nuclear factor κB family proteins.
Identifieur interne : 000595 ( Main/Exploration ); précédent : 000594; suivant : 000596The glutaredoxin/S-glutathionylation axis regulates interleukin-17A-induced proinflammatory responses in lung epithelial cells in association with S-glutathionylation of nuclear factor κB family proteins.
Auteurs : James D. Nolin [États-Unis] ; Jane E. Tully [États-Unis] ; Sidra M. Hoffman [États-Unis] ; Amy S. Guala [États-Unis] ; Jos L. Van Der Velden [États-Unis] ; Matthew E. Poynter [États-Unis] ; Albert Van Der Vliet [États-Unis] ; Vikas Anathy [États-Unis] ; Yvonne M W. Janssen-Heininger [États-Unis]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2014.
Descripteurs français
- KwdFr :
- Acides sulféniques (métabolisme), Animaux (MeSH), Cellules cultivées (MeSH), Cellules épithéliales (métabolisme), Chimiokine CCL20 (biosynthèse), Facteur de transcription RelA (métabolisme), Facteur de transcription RelB (métabolisme), Glutarédoxines (génétique), Glutathion (composition chimique), I-kappa B Kinase (génétique), I-kappa B Kinase (métabolisme), Inflammation (anatomopathologie), Inflammation (immunologie), Interférence par ARN (MeSH), Interleukine-17 (métabolisme), Interleukine-6 (biosynthèse), Maladies pulmonaires (anatomopathologie), Maturation post-traductionnelle des protéines (MeSH), Muqueuse respiratoire (cytologie), Oxydoréduction (MeSH), Petit ARN interférent (MeSH), Poumon (cytologie), Régulation de l'expression des gènes (MeSH), Souris (MeSH), Souris knockout (MeSH), Trachée (cytologie).
- MESH :
- anatomopathologie : Inflammation, Maladies pulmonaires.
- biosynthèse : Chimiokine CCL20, Interleukine-6.
- composition chimique : Glutathion.
- cytologie : Muqueuse respiratoire, Poumon, Trachée.
- génétique : Glutarédoxines, I-kappa B Kinase.
- immunologie : Inflammation.
- métabolisme : Acides sulféniques, Cellules épithéliales, Facteur de transcription RelA, Facteur de transcription RelB, I-kappa B Kinase, Interleukine-17.
- Animaux, Cellules cultivées, Interférence par ARN, Maturation post-traductionnelle des protéines, Oxydoréduction, Petit ARN interférent, Régulation de l'expression des gènes, Souris, Souris knockout.
English descriptors
- KwdEn :
- Animals (MeSH), Cells, Cultured (MeSH), Chemokine CCL20 (biosynthesis), Epithelial Cells (metabolism), Gene Expression Regulation (MeSH), Glutaredoxins (genetics), Glutathione (chemistry), I-kappa B Kinase (genetics), I-kappa B Kinase (metabolism), Inflammation (immunology), Inflammation (pathology), Interleukin-17 (metabolism), Interleukin-6 (biosynthesis), Lung (cytology), Lung Diseases (pathology), Mice (MeSH), Mice, Knockout (MeSH), Oxidation-Reduction (MeSH), Protein Processing, Post-Translational (MeSH), RNA Interference (MeSH), RNA, Small Interfering (MeSH), Respiratory Mucosa (cytology), Sulfenic Acids (metabolism), Trachea (cytology), Transcription Factor RelA (metabolism), Transcription Factor RelB (metabolism).
- MESH :
- chemical , biosynthesis : Chemokine CCL20, Interleukin-6.
- chemical , chemistry : Glutathione.
- chemical , genetics : Glutaredoxins, I-kappa B Kinase.
- cytology : Lung, Respiratory Mucosa, Trachea.
- immunology : Inflammation.
- metabolism : Epithelial Cells, I-kappa B Kinase, Interleukin-17, Sulfenic Acids, Transcription Factor RelA, Transcription Factor RelB.
- pathology : Inflammation, Lung Diseases.
- Animals, Cells, Cultured, Gene Expression Regulation, Mice, Mice, Knockout, Oxidation-Reduction, Protein Processing, Post-Translational, RNA Interference, RNA, Small Interfering.
Abstract
Interleukin-17A (IL-17A) is a newly emerging player in the pathogenesis of chronic lung diseases that amplifies inflammatory responses and promotes tissue remodeling. Stimulation of lung epithelial cells with IL-17A leads to activation of the transcription factor nuclear factor κB (NF-κB), a key player in the orchestration of lung inflammation. We have previously demonstrated the importance of the redox-dependent posttranslational modification S-glutathionylation in limiting activation of NF-κB and downstream gene induction. Under physiological conditions, the enzyme glutaredoxin 1 (Grx1) acts to deglutathionylate NF-κB proteins, which restores functional activity. In this study, we sought to determine the impact of S-glutathionylation on IL-17A-induced NF-κB activation and expression of proinflammatory mediators. C10 mouse lung alveolar epithelial cells or primary mouse tracheal epithelial cells exposed to IL-17A show rapid activation of NF-κB and the induction of proinflammatory genes. Upon IL-17A exposure, sulfenic acid formation and S-glutathionylated proteins increased. Assessment of S-glutathionylation of NF-κB pathway components revealed S-glutathionylation of RelA (RelA-SSG) and inhibitory κB kinase α (IKKα-SSG) after stimulation with IL-17A. SiRNA-mediated ablation of Grx1 increased both RelA-SSG and IKKα-SSG and acutely increased nuclear content of RelA and tended to decrease nuclear RelB. SiRNA-mediated ablation or genetic ablation of Glrx1 decreased the expression of the NF-κB-regulated genes KC and CCL20 in response to IL-17A, but conversely increased the expression of IL-6. Last, siRNA-mediated ablation of IKKα attenuated nuclear RelA and RelB content and decreased expression of KC and CCL20 in response to IL-17A. Together, these data demonstrate a critical role for the S-glutathionylation/Grx1 redox axis in regulating IKKα and RelA S-glutathionylation and the responsiveness of epithelial cells to IL-17A.
DOI: 10.1016/j.freeradbiomed.2014.04.028
PubMed: 24816292
PubMed Central: PMC4111997
Affiliations:
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Janssen-Heininger</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA. 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Nolin</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Tully, Jane E" sort="Tully, Jane E" uniqKey="Tully J" first="Jane E" last="Tully">Jane E. Tully</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Hoffman, Sidra M" sort="Hoffman, Sidra M" uniqKey="Hoffman S" first="Sidra M" last="Hoffman">Sidra M. Hoffman</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Guala, Amy S" sort="Guala, Amy S" uniqKey="Guala A" first="Amy S" last="Guala">Amy S. Guala</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Van Der Velden, Jos L" sort="Van Der Velden, Jos L" uniqKey="Van Der Velden J" first="Jos L" last="Van Der Velden">Jos L. Van Der Velden</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Poynter, Matthew E" sort="Poynter, Matthew E" uniqKey="Poynter M" first="Matthew E" last="Poynter">Matthew E. Poynter</name><affiliation wicri:level="2"><nlm:affiliation>Department of Medicine, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author><author><name sortKey="Janssen Heininger, Yvonne M W" sort="Janssen Heininger, Yvonne M W" uniqKey="Janssen Heininger Y" first="Yvonne M W" last="Janssen-Heininger">Yvonne M W. Janssen-Heininger</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA. Electronic address: yvonne.janssen@uvm.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405</wicri:regionArea><placeName><region type="state">Vermont</region></placeName></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Chemokine CCL20 (biosynthesis)</term><term>Epithelial Cells (metabolism)</term><term>Gene Expression Regulation (MeSH)</term><term>Glutaredoxins (genetics)</term><term>Glutathione (chemistry)</term><term>I-kappa B Kinase (genetics)</term><term>I-kappa B Kinase (metabolism)</term><term>Inflammation (immunology)</term><term>Inflammation (pathology)</term><term>Interleukin-17 (metabolism)</term><term>Interleukin-6 (biosynthesis)</term><term>Lung (cytology)</term><term>Lung Diseases (pathology)</term><term>Mice (MeSH)</term><term>Mice, Knockout (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>RNA Interference (MeSH)</term><term>RNA, Small Interfering (MeSH)</term><term>Respiratory Mucosa (cytology)</term><term>Sulfenic Acids (metabolism)</term><term>Trachea (cytology)</term><term>Transcription Factor RelA (metabolism)</term><term>Transcription Factor RelB (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulféniques (métabolisme)</term><term>Animaux (MeSH)</term><term>Cellules cultivées (MeSH)</term><term>Cellules épithéliales (métabolisme)</term><term>Chimiokine CCL20 (biosynthèse)</term><term>Facteur de transcription RelA (métabolisme)</term><term>Facteur de transcription RelB (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutathion (composition chimique)</term><term>I-kappa B Kinase (génétique)</term><term>I-kappa B Kinase (métabolisme)</term><term>Inflammation (anatomopathologie)</term><term>Inflammation (immunologie)</term><term>Interférence par ARN (MeSH)</term><term>Interleukine-17 (métabolisme)</term><term>Interleukine-6 (biosynthèse)</term><term>Maladies pulmonaires (anatomopathologie)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Muqueuse respiratoire (cytologie)</term><term>Oxydoréduction (MeSH)</term><term>Petit ARN interférent (MeSH)</term><term>Poumon (cytologie)</term><term>Régulation de l'expression des gènes (MeSH)</term><term>Souris (MeSH)</term><term>Souris knockout (MeSH)</term><term>Trachée (cytologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Chemokine CCL20</term><term>Interleukin-6</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>I-kappa B Kinase</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Inflammation</term><term>Maladies pulmonaires</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Chimiokine CCL20</term><term>Interleukine-6</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathion</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Muqueuse respiratoire</term><term>Poumon</term><term>Trachée</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Lung</term><term>Respiratory Mucosa</term><term>Trachea</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>I-kappa B Kinase</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Inflammation</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Inflammation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term><term>I-kappa B Kinase</term><term>Interleukin-17</term><term>Sulfenic Acids</term><term>Transcription Factor RelA</term><term>Transcription Factor RelB</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sulféniques</term><term>Cellules épithéliales</term><term>Facteur de transcription RelA</term><term>Facteur de transcription RelB</term><term>I-kappa B Kinase</term><term>Interleukine-17</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Inflammation</term><term>Lung Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Gene Expression Regulation</term><term>Mice</term><term>Mice, Knockout</term><term>Oxidation-Reduction</term><term>Protein Processing, Post-Translational</term><term>RNA Interference</term><term>RNA, Small Interfering</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Interférence par ARN</term><term>Maturation post-traductionnelle des protéines</term><term>Oxydoréduction</term><term>Petit ARN interférent</term><term>Régulation de l'expression des gènes</term><term>Souris</term><term>Souris knockout</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Interleukin-17A (IL-17A) is a newly emerging player in the pathogenesis of chronic lung diseases that amplifies inflammatory responses and promotes tissue remodeling. Stimulation of lung epithelial cells with IL-17A leads to activation of the transcription factor nuclear factor κB (NF-κB), a key player in the orchestration of lung inflammation. We have previously demonstrated the importance of the redox-dependent posttranslational modification S-glutathionylation in limiting activation of NF-κB and downstream gene induction. Under physiological conditions, the enzyme glutaredoxin 1 (Grx1) acts to deglutathionylate NF-κB proteins, which restores functional activity. In this study, we sought to determine the impact of S-glutathionylation on IL-17A-induced NF-κB activation and expression of proinflammatory mediators. C10 mouse lung alveolar epithelial cells or primary mouse tracheal epithelial cells exposed to IL-17A show rapid activation of NF-κB and the induction of proinflammatory genes. Upon IL-17A exposure, sulfenic acid formation and S-glutathionylated proteins increased. Assessment of S-glutathionylation of NF-κB pathway components revealed S-glutathionylation of RelA (RelA-SSG) and inhibitory κB kinase α (IKKα-SSG) after stimulation with IL-17A. SiRNA-mediated ablation of Grx1 increased both RelA-SSG and IKKα-SSG and acutely increased nuclear content of RelA and tended to decrease nuclear RelB. SiRNA-mediated ablation or genetic ablation of Glrx1 decreased the expression of the NF-κB-regulated genes KC and CCL20 in response to IL-17A, but conversely increased the expression of IL-6. Last, siRNA-mediated ablation of IKKα attenuated nuclear RelA and RelB content and decreased expression of KC and CCL20 in response to IL-17A. Together, these data demonstrate a critical role for the S-glutathionylation/Grx1 redox axis in regulating IKKα and RelA S-glutathionylation and the responsiveness of epithelial cells to IL-17A. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24816292</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>11</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>73</Volume><PubDate><Year>2014</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>The glutaredoxin/S-glutathionylation axis regulates interleukin-17A-induced proinflammatory responses in lung epithelial cells in association with S-glutathionylation of nuclear factor κB family proteins.</ArticleTitle><Pagination><MedlinePgn>143-53</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2014.04.028</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(14)00200-7</ELocationID><Abstract><AbstractText>Interleukin-17A (IL-17A) is a newly emerging player in the pathogenesis of chronic lung diseases that amplifies inflammatory responses and promotes tissue remodeling. Stimulation of lung epithelial cells with IL-17A leads to activation of the transcription factor nuclear factor κB (NF-κB), a key player in the orchestration of lung inflammation. We have previously demonstrated the importance of the redox-dependent posttranslational modification S-glutathionylation in limiting activation of NF-κB and downstream gene induction. Under physiological conditions, the enzyme glutaredoxin 1 (Grx1) acts to deglutathionylate NF-κB proteins, which restores functional activity. In this study, we sought to determine the impact of S-glutathionylation on IL-17A-induced NF-κB activation and expression of proinflammatory mediators. C10 mouse lung alveolar epithelial cells or primary mouse tracheal epithelial cells exposed to IL-17A show rapid activation of NF-κB and the induction of proinflammatory genes. Upon IL-17A exposure, sulfenic acid formation and S-glutathionylated proteins increased. Assessment of S-glutathionylation of NF-κB pathway components revealed S-glutathionylation of RelA (RelA-SSG) and inhibitory κB kinase α (IKKα-SSG) after stimulation with IL-17A. SiRNA-mediated ablation of Grx1 increased both RelA-SSG and IKKα-SSG and acutely increased nuclear content of RelA and tended to decrease nuclear RelB. SiRNA-mediated ablation or genetic ablation of Glrx1 decreased the expression of the NF-κB-regulated genes KC and CCL20 in response to IL-17A, but conversely increased the expression of IL-6. Last, siRNA-mediated ablation of IKKα attenuated nuclear RelA and RelB content and decreased expression of KC and CCL20 in response to IL-17A. Together, these data demonstrate a critical role for the S-glutathionylation/Grx1 redox axis in regulating IKKα and RelA S-glutathionylation and the responsiveness of epithelial cells to IL-17A. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nolin</LastName><ForeName>James D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tully</LastName><ForeName>Jane E</ForeName><Initials>JE</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hoffman</LastName><ForeName>Sidra M</ForeName><Initials>SM</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guala</LastName><ForeName>Amy S</ForeName><Initials>AS</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>van der Velden</LastName><ForeName>Jos L</ForeName><Initials>JL</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Poynter</LastName><ForeName>Matthew E</ForeName><Initials>ME</Initials><AffiliationInfo><Affiliation>Department of Medicine, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>van der Vliet</LastName><ForeName>Albert</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Anathy</LastName><ForeName>Vikas</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Janssen-Heininger</LastName><ForeName>Yvonne M W</ForeName><Initials>YM</Initials><AffiliationInfo><Affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, VT 05405, USA. Electronic address: yvonne.janssen@uvm.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 HL060014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32ES007122-30</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL107291</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01HL060014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL085646</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32HL076122</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 ES021476</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH 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MajorTopicYN="N">Chemokine CCL20</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051550" MajorTopicYN="N">I-kappa B Kinase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007249" MajorTopicYN="N">Inflammation</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020381" MajorTopicYN="N">Interleukin-17</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015850" MajorTopicYN="N">Interleukin-6</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008171" MajorTopicYN="N">Lung Diseases</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018345" MajorTopicYN="N">Mice, Knockout</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020545" MajorTopicYN="N">Respiratory Mucosa</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013434" MajorTopicYN="N">Sulfenic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014132" MajorTopicYN="N">Trachea</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051996" MajorTopicYN="N">Transcription Factor RelA</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051841" MajorTopicYN="N">Transcription Factor RelB</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Free radicals</Keyword><Keyword MajorTopicYN="N">Glutaredoxin-1</Keyword><Keyword MajorTopicYN="N">Inhibitory κB kinase α</Keyword><Keyword MajorTopicYN="N">Interleukin-17A</Keyword><Keyword MajorTopicYN="N">Nuclear factor κB</Keyword><Keyword MajorTopicYN="N">Protein S-glutathionylation</Keyword><Keyword 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Nolin</name></region><name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name><name sortKey="Guala, Amy S" sort="Guala, Amy S" uniqKey="Guala A" first="Amy S" last="Guala">Amy S. Guala</name><name sortKey="Hoffman, Sidra M" sort="Hoffman, Sidra M" uniqKey="Hoffman S" first="Sidra M" last="Hoffman">Sidra M. Hoffman</name><name sortKey="Janssen Heininger, Yvonne M W" sort="Janssen Heininger, Yvonne M W" uniqKey="Janssen Heininger Y" first="Yvonne M W" last="Janssen-Heininger">Yvonne M W. Janssen-Heininger</name><name sortKey="Poynter, Matthew E" sort="Poynter, Matthew E" uniqKey="Poynter M" first="Matthew E" last="Poynter">Matthew E. Poynter</name><name sortKey="Tully, Jane E" sort="Tully, Jane E" uniqKey="Tully J" first="Jane E" last="Tully">Jane E. Tully</name><name sortKey="Van Der Velden, Jos L" sort="Van Der Velden, Jos L" uniqKey="Van Der Velden J" first="Jos L" last="Van Der Velden">Jos L. Van Der Velden</name><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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}}
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:24816292" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |