Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells.
Identifieur interne : 000453 ( Main/Exploration ); précédent : 000452; suivant : 000454Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells.
Auteurs : Jane T. Jones [États-Unis] ; Xi Qian [États-Unis] ; Jos L J. Van Der Velden [États-Unis] ; Shi Biao Chia [États-Unis] ; David H. Mcmillan [États-Unis] ; Stevenson Flemer [États-Unis] ; Sidra M. Hoffman [États-Unis] ; Karolyn G. Lahue [États-Unis] ; Robert W. Schneider [États-Unis] ; James D. Nolin [États-Unis] ; Vikas Anathy [États-Unis] ; Albert Van Der Vliet [États-Unis] ; Danyelle M. Townsend [États-Unis] ; Kenneth D. Tew [États-Unis] ; Yvonne M W. Janssen-Heininger [États-Unis]Source :
- Redox biology [ 2213-2317 ] ; 2016.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Asthme (anatomopathologie), Asthme (génétique), Asthme (induit chimiquement), Cellules épithéliales (anatomopathologie), Cellules épithéliales (métabolisme), Facteur de transcription NF-kappa B (génétique), Glutarédoxines (métabolisme), Glutathione S-transferase pi (génétique), Glutathione S-transferase pi (métabolisme), Humains (MeSH), I-kappa B Kinase (génétique), I-kappa B Kinase (métabolisme), Inflammation (génétique), Inflammation (métabolisme), Lignée cellulaire (MeSH), Lipopolysaccharides (toxicité), Maturation post-traductionnelle des protéines (génétique), Modèles animaux de maladie humaine (MeSH), Poumon (anatomopathologie), Poumon (métabolisme), Souris (MeSH), Stress oxydatif (génétique), Transduction du signal (MeSH).
- MESH :
- anatomopathologie : Asthme, Cellules épithéliales, Poumon.
- génétique : Asthme, Facteur de transcription NF-kappa B, Glutathione S-transferase pi, I-kappa B Kinase, Inflammation, Maturation post-traductionnelle des protéines, Stress oxydatif.
- induit chimiquement : Asthme.
- métabolisme : Cellules épithéliales, Glutarédoxines, Glutathione S-transferase pi, I-kappa B Kinase, Inflammation, Poumon.
- toxicité : Lipopolysaccharides.
- Animaux, Humains, Lignée cellulaire, Modèles animaux de maladie humaine, Souris, Transduction du signal.
English descriptors
- KwdEn :
- Animals (MeSH), Asthma (chemically induced), Asthma (genetics), Asthma (pathology), Cell Line (MeSH), Disease Models, Animal (MeSH), Epithelial Cells (metabolism), Epithelial Cells (pathology), Glutaredoxins (metabolism), Glutathione S-Transferase pi (genetics), Glutathione S-Transferase pi (metabolism), Humans (MeSH), I-kappa B Kinase (genetics), I-kappa B Kinase (metabolism), Inflammation (genetics), Inflammation (metabolism), Lipopolysaccharides (toxicity), Lung (metabolism), Lung (pathology), Mice (MeSH), NF-kappa B (genetics), Oxidative Stress (genetics), Protein Processing, Post-Translational (genetics), Signal Transduction (MeSH).
- MESH :
- chemical , genetics : Glutathione S-Transferase pi, I-kappa B Kinase, NF-kappa B.
- chemical , metabolism : Glutaredoxins, Glutathione S-Transferase pi, I-kappa B Kinase.
- chemically induced : Asthma.
- genetics : Asthma, Inflammation, Oxidative Stress, Protein Processing, Post-Translational.
- metabolism : Epithelial Cells, Inflammation, Lung.
- pathology : Asthma, Epithelial Cells, Lung.
- chemical , toxicity : Lipopolysaccharides.
- Animals, Cell Line, Disease Models, Animal, Humans, Mice, Signal Transduction.
Abstract
Nuclear Factor kappa B (NF-κB) is a transcription factor family critical in the activation of pro- inflammatory responses. The NF-κB pathway is regulated by oxidant-induced post-translational modifications. Protein S-glutathionylation, or the conjugation of the antioxidant molecule, glutathione to reactive cysteines inhibits the activity of inhibitory kappa B kinase beta (IKKβ), among other NF-κB proteins. Glutathione S-transferase Pi (GSTP) is an enzyme that has been shown to catalyze protein S-glutathionylation (PSSG) under conditions of oxidative stress. The objective of the present study was to determine whether GSTP regulates NF-κB signaling, S-glutathionylation of IKK, and subsequent pro-inflammatory signaling. We demonstrated that, in unstimulated cells, GSTP associated with the inhibitor of NF-κB, IκBα. However, exposure to LPS resulted in a rapid loss of association between IκBα and GSTP, and instead led to a protracted association between IKKβ and GSTP. LPS exposure also led to increases in the S-glutathionylation of IKKβ. SiRNA-mediated knockdown of GSTP decreased IKKβ-SSG, and enhanced NF-κB nuclear translocation, transcriptional activity, and pro-inflammatory cytokine production in response to lipopolysaccharide (LPS). TLK117, an isotype-selective inhibitor of GSTP, also enhanced LPS-induced NF-κB transcriptional activity and pro-inflammatory cytokine production, suggesting that the catalytic activity of GSTP is important in repressing NF-κB activation. Expression of both wild-type and catalytically-inactive Y7F mutant GSTP significantly attenuated LPS- or IKKβ-induced production of GM-CSF. These studies indicate a complex role for GSTP in modulating NF-κB, which may involve S-glutathionylation of IKK proteins, and interaction with NF-κB family members. Our findings suggest that targeting GSTP is a potential avenue for regulating the activity of this prominent pro-inflammatory and immunomodulatory transcription factor.
DOI: 10.1016/j.redox.2016.03.005
PubMed: 27058114
PubMed Central: PMC4827796
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells.</title>
<author><name sortKey="Jones, Jane T" sort="Jones, Jane T" uniqKey="Jones J" first="Jane T" last="Jones">Jane T. Jones</name>
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<author><name sortKey="Qian, Xi" sort="Qian, Xi" uniqKey="Qian X" first="Xi" last="Qian">Xi Qian</name>
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<author><name sortKey="Van Der Velden, Jos L J" sort="Van Der Velden, Jos L J" uniqKey="Van Der Velden J" first="Jos L J" last="Van Der Velden">Jos L J. Van Der Velden</name>
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<author><name sortKey="Chia, Shi Biao" sort="Chia, Shi Biao" uniqKey="Chia S" first="Shi Biao" last="Chia">Shi Biao Chia</name>
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<author><name sortKey="Mcmillan, David H" sort="Mcmillan, David H" uniqKey="Mcmillan D" first="David H" last="Mcmillan">David H. Mcmillan</name>
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<author><name sortKey="Flemer, Stevenson" sort="Flemer, Stevenson" uniqKey="Flemer S" first="Stevenson" last="Flemer">Stevenson Flemer</name>
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<country xml:lang="fr">États-Unis</country>
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<author><name sortKey="Hoffman, Sidra M" sort="Hoffman, Sidra M" uniqKey="Hoffman S" first="Sidra M" last="Hoffman">Sidra M. Hoffman</name>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
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<author><name sortKey="Lahue, Karolyn G" sort="Lahue, Karolyn G" uniqKey="Lahue K" first="Karolyn G" last="Lahue">Karolyn G. Lahue</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
<placeName><region type="state">Vermont</region>
</placeName>
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<author><name sortKey="Schneider, Robert W" sort="Schneider, Robert W" uniqKey="Schneider R" first="Robert W" last="Schneider">Robert W. Schneider</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
<placeName><region type="state">Vermont</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Nolin, James D" sort="Nolin, James D" uniqKey="Nolin J" first="James D" last="Nolin">James D. Nolin</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
<placeName><region type="state">Vermont</region>
</placeName>
</affiliation>
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<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 and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</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 and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
<placeName><region type="state">Vermont</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Townsend, Danyelle M" sort="Townsend, Danyelle M" uniqKey="Townsend D" first="Danyelle M" last="Townsend">Danyelle M. Townsend</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, SC, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, SC</wicri:regionArea>
<placeName><region type="state">Caroline du Sud</region>
<settlement type="city">Columbia (Caroline du Sud)</settlement>
</placeName>
<orgName type="university">Université de Caroline du Sud</orgName>
</affiliation>
</author>
<author><name sortKey="Tew, Kenneth D" sort="Tew, Kenneth D" uniqKey="Tew K" first="Kenneth D" last="Tew">Kenneth D. Tew</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC</wicri:regionArea>
<placeName><region type="state">Caroline du Sud</region>
<settlement type="city">Columbia (Caroline du Sud)</settlement>
</placeName>
<orgName type="university">Université de Caroline du Sud</orgName>
</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 and Laboratory Medicine, The University of Vermont, Burlington, VT, United States. Electronic address: yvonne.janssen@uvm.edu.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT</wicri:regionArea>
<placeName><region type="state">Vermont</region>
</placeName>
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<series><title level="j">Redox biology</title>
<idno type="eISSN">2213-2317</idno>
<imprint><date when="2016" type="published">2016</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Asthma (chemically induced)</term>
<term>Asthma (genetics)</term>
<term>Asthma (pathology)</term>
<term>Cell Line (MeSH)</term>
<term>Disease Models, Animal (MeSH)</term>
<term>Epithelial Cells (metabolism)</term>
<term>Epithelial Cells (pathology)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione S-Transferase pi (genetics)</term>
<term>Glutathione S-Transferase pi (metabolism)</term>
<term>Humans (MeSH)</term>
<term>I-kappa B Kinase (genetics)</term>
<term>I-kappa B Kinase (metabolism)</term>
<term>Inflammation (genetics)</term>
<term>Inflammation (metabolism)</term>
<term>Lipopolysaccharides (toxicity)</term>
<term>Lung (metabolism)</term>
<term>Lung (pathology)</term>
<term>Mice (MeSH)</term>
<term>NF-kappa B (genetics)</term>
<term>Oxidative Stress (genetics)</term>
<term>Protein Processing, Post-Translational (genetics)</term>
<term>Signal Transduction (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Asthme (anatomopathologie)</term>
<term>Asthme (génétique)</term>
<term>Asthme (induit chimiquement)</term>
<term>Cellules épithéliales (anatomopathologie)</term>
<term>Cellules épithéliales (métabolisme)</term>
<term>Facteur de transcription NF-kappa B (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathione S-transferase pi (génétique)</term>
<term>Glutathione S-transferase pi (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>I-kappa B Kinase (génétique)</term>
<term>I-kappa B Kinase (métabolisme)</term>
<term>Inflammation (génétique)</term>
<term>Inflammation (métabolisme)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Lipopolysaccharides (toxicité)</term>
<term>Maturation post-traductionnelle des protéines (génétique)</term>
<term>Modèles animaux de maladie humaine (MeSH)</term>
<term>Poumon (anatomopathologie)</term>
<term>Poumon (métabolisme)</term>
<term>Souris (MeSH)</term>
<term>Stress oxydatif (génétique)</term>
<term>Transduction du signal (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione S-Transferase pi</term>
<term>I-kappa B Kinase</term>
<term>NF-kappa B</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione S-Transferase pi</term>
<term>I-kappa B Kinase</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Asthme</term>
<term>Cellules épithéliales</term>
<term>Poumon</term>
</keywords>
<keywords scheme="MESH" qualifier="chemically induced" xml:lang="en"><term>Asthma</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Asthma</term>
<term>Inflammation</term>
<term>Oxidative Stress</term>
<term>Protein Processing, Post-Translational</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Asthme</term>
<term>Facteur de transcription NF-kappa B</term>
<term>Glutathione S-transferase pi</term>
<term>I-kappa B Kinase</term>
<term>Inflammation</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Stress oxydatif</term>
</keywords>
<keywords scheme="MESH" qualifier="induit chimiquement" xml:lang="fr"><term>Asthme</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term>
<term>Inflammation</term>
<term>Lung</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules épithéliales</term>
<term>Glutarédoxines</term>
<term>Glutathione S-transferase pi</term>
<term>I-kappa B Kinase</term>
<term>Inflammation</term>
<term>Poumon</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Asthma</term>
<term>Epithelial Cells</term>
<term>Lung</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Lipopolysaccharides</term>
</keywords>
<keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Lipopolysaccharides</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Disease Models, Animal</term>
<term>Humans</term>
<term>Mice</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Modèles animaux de maladie humaine</term>
<term>Souris</term>
<term>Transduction du signal</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Nuclear Factor kappa B (NF-κB) is a transcription factor family critical in the activation of pro- inflammatory responses. The NF-κB pathway is regulated by oxidant-induced post-translational modifications. Protein S-glutathionylation, or the conjugation of the antioxidant molecule, glutathione to reactive cysteines inhibits the activity of inhibitory kappa B kinase beta (IKKβ), among other NF-κB proteins. Glutathione S-transferase Pi (GSTP) is an enzyme that has been shown to catalyze protein S-glutathionylation (PSSG) under conditions of oxidative stress. The objective of the present study was to determine whether GSTP regulates NF-κB signaling, S-glutathionylation of IKK, and subsequent pro-inflammatory signaling. We demonstrated that, in unstimulated cells, GSTP associated with the inhibitor of NF-κB, IκBα. However, exposure to LPS resulted in a rapid loss of association between IκBα and GSTP, and instead led to a protracted association between IKKβ and GSTP. LPS exposure also led to increases in the S-glutathionylation of IKKβ. SiRNA-mediated knockdown of GSTP decreased IKKβ-SSG, and enhanced NF-κB nuclear translocation, transcriptional activity, and pro-inflammatory cytokine production in response to lipopolysaccharide (LPS). TLK117, an isotype-selective inhibitor of GSTP, also enhanced LPS-induced NF-κB transcriptional activity and pro-inflammatory cytokine production, suggesting that the catalytic activity of GSTP is important in repressing NF-κB activation. Expression of both wild-type and catalytically-inactive Y7F mutant GSTP significantly attenuated LPS- or IKKβ-induced production of GM-CSF. These studies indicate a complex role for GSTP in modulating NF-κB, which may involve S-glutathionylation of IKK proteins, and interaction with NF-κB family members. Our findings suggest that targeting GSTP is a potential avenue for regulating the activity of this prominent pro-inflammatory and immunomodulatory transcription factor.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27058114</PMID>
<DateCompleted><Year>2017</Year>
<Month>11</Month>
<Day>20</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2213-2317</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>8</Volume>
<PubDate><Year>2016</Year>
<Month>08</Month>
</PubDate>
</JournalIssue>
<Title>Redox biology</Title>
<ISOAbbreviation>Redox Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells.</ArticleTitle>
<Pagination><MedlinePgn>375-82</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.redox.2016.03.005</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S2213-2317(16)30024-6</ELocationID>
<Abstract><AbstractText>Nuclear Factor kappa B (NF-κB) is a transcription factor family critical in the activation of pro- inflammatory responses. The NF-κB pathway is regulated by oxidant-induced post-translational modifications. Protein S-glutathionylation, or the conjugation of the antioxidant molecule, glutathione to reactive cysteines inhibits the activity of inhibitory kappa B kinase beta (IKKβ), among other NF-κB proteins. Glutathione S-transferase Pi (GSTP) is an enzyme that has been shown to catalyze protein S-glutathionylation (PSSG) under conditions of oxidative stress. The objective of the present study was to determine whether GSTP regulates NF-κB signaling, S-glutathionylation of IKK, and subsequent pro-inflammatory signaling. We demonstrated that, in unstimulated cells, GSTP associated with the inhibitor of NF-κB, IκBα. However, exposure to LPS resulted in a rapid loss of association between IκBα and GSTP, and instead led to a protracted association between IKKβ and GSTP. LPS exposure also led to increases in the S-glutathionylation of IKKβ. SiRNA-mediated knockdown of GSTP decreased IKKβ-SSG, and enhanced NF-κB nuclear translocation, transcriptional activity, and pro-inflammatory cytokine production in response to lipopolysaccharide (LPS). TLK117, an isotype-selective inhibitor of GSTP, also enhanced LPS-induced NF-κB transcriptional activity and pro-inflammatory cytokine production, suggesting that the catalytic activity of GSTP is important in repressing NF-κB activation. Expression of both wild-type and catalytically-inactive Y7F mutant GSTP significantly attenuated LPS- or IKKβ-induced production of GM-CSF. These studies indicate a complex role for GSTP in modulating NF-κB, which may involve S-glutathionylation of IKK proteins, and interaction with NF-κB family members. Our findings suggest that targeting GSTP is a potential avenue for regulating the activity of this prominent pro-inflammatory and immunomodulatory transcription factor.</AbstractText>
<CopyrightInformation>Copyright © 2016 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jones</LastName>
<ForeName>Jane T</ForeName>
<Initials>JT</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qian</LastName>
<ForeName>Xi</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van der Velden</LastName>
<ForeName>Jos L J</ForeName>
<Initials>JL</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chia</LastName>
<ForeName>Shi Biao</ForeName>
<Initials>SB</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McMillan</LastName>
<ForeName>David H</ForeName>
<Initials>DH</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Flemer</LastName>
<ForeName>Stevenson</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hoffman</LastName>
<ForeName>Sidra M</ForeName>
<Initials>SM</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lahue</LastName>
<ForeName>Karolyn G</ForeName>
<Initials>KG</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Schneider</LastName>
<ForeName>Robert W</ForeName>
<Initials>RW</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nolin</LastName>
<ForeName>James D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Anathy</LastName>
<ForeName>Vikas</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van der Vliet</LastName>
<ForeName>Albert</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Townsend</LastName>
<ForeName>Danyelle M</ForeName>
<Initials>DM</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, SC, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tew</LastName>
<ForeName>Kenneth D</ForeName>
<Initials>KD</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Janssen-Heininger</LastName>
<ForeName>Yvonne M W</ForeName>
<Initials>YM</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, The University of Vermont, Burlington, VT, United States. Electronic address: yvonne.janssen@uvm.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 CA085660</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 HL060014</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 HL085464</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P20 GM103542</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS 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>R01 ES021476</GrantID>
<Acronym>ES</Acronym>
<Agency>NIEHS 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>2016</Year>
<Month>03</Month>
<Day>26</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Redox Biol</MedlineTA>
<NlmUniqueID>101605639</NlmUniqueID>
<ISSNLinking>2213-2317</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008070">Lipopolysaccharides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016328">NF-kappa B</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber>
<NameOfSubstance UI="D051549">Glutathione S-Transferase pi</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.10</RegistryNumber>
<NameOfSubstance UI="D051550">I-kappa B Kinase</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001249" MajorTopicYN="N">Asthma</DescriptorName>
<QualifierName UI="Q000139" MajorTopicYN="N">chemically induced</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051549" MajorTopicYN="N">Glutathione S-Transferase pi</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051550" MajorTopicYN="N">I-kappa B Kinase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007249" MajorTopicYN="N">Inflammation</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008070" MajorTopicYN="N">Lipopolysaccharides</DescriptorName>
<QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016328" MajorTopicYN="N">NF-kappa B</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Asthma</Keyword>
<Keyword MajorTopicYN="Y">GSTP</Keyword>
<Keyword MajorTopicYN="Y">Inflammation</Keyword>
<Keyword MajorTopicYN="Y">Lung</Keyword>
<Keyword MajorTopicYN="Y">NF-κB</Keyword>
<Keyword MajorTopicYN="Y">S-glutathionylation</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>03</Month>
<Day>15</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>03</Month>
<Day>22</Day>
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<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Caroline du Sud</li>
<li>Vermont</li>
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<settlement><li>Columbia (Caroline du Sud)</li>
</settlement>
<orgName><li>Université de Caroline du Sud</li>
</orgName>
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<tree><country name="États-Unis"><region name="Vermont"><name sortKey="Jones, Jane T" sort="Jones, Jane T" uniqKey="Jones J" first="Jane T" last="Jones">Jane T. Jones</name>
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<name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name>
<name sortKey="Chia, Shi Biao" sort="Chia, Shi Biao" uniqKey="Chia S" first="Shi Biao" last="Chia">Shi Biao Chia</name>
<name sortKey="Flemer, Stevenson" sort="Flemer, Stevenson" uniqKey="Flemer S" first="Stevenson" last="Flemer">Stevenson Flemer</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="Lahue, Karolyn G" sort="Lahue, Karolyn G" uniqKey="Lahue K" first="Karolyn G" last="Lahue">Karolyn G. Lahue</name>
<name sortKey="Mcmillan, David H" sort="Mcmillan, David H" uniqKey="Mcmillan D" first="David H" last="Mcmillan">David H. Mcmillan</name>
<name sortKey="Nolin, James D" sort="Nolin, James D" uniqKey="Nolin J" first="James D" last="Nolin">James D. Nolin</name>
<name sortKey="Qian, Xi" sort="Qian, Xi" uniqKey="Qian X" first="Xi" last="Qian">Xi Qian</name>
<name sortKey="Schneider, Robert W" sort="Schneider, Robert W" uniqKey="Schneider R" first="Robert W" last="Schneider">Robert W. Schneider</name>
<name sortKey="Tew, Kenneth D" sort="Tew, Kenneth D" uniqKey="Tew K" first="Kenneth D" last="Tew">Kenneth D. Tew</name>
<name sortKey="Townsend, Danyelle M" sort="Townsend, Danyelle M" uniqKey="Townsend D" first="Danyelle M" last="Townsend">Danyelle M. Townsend</name>
<name sortKey="Van Der Velden, Jos L J" sort="Van Der Velden, Jos L J" uniqKey="Van Der Velden J" first="Jos L J" last="Van Der Velden">Jos L J. 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>
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