In situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization.
Identifieur interne : 000B15 ( Main/Exploration ); précédent : 000B14; suivant : 000B16In situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization.
Auteurs : Scott W. Aesif [États-Unis] ; Vikas Anathy ; Marije Havermans ; Amy S. Guala ; Karina Ckless ; Douglas J. Taatjes ; Yvonne M W. Janssen-HeiningerSource :
- The American journal of pathology [ 1525-2191 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Biocatalyse (MeSH), Cystéine (métabolisme), Dioxyde d'azote (pharmacologie), Glutarédoxines (métabolisme), Glutathion (analyse), Glutathion (métabolisme), Histocytochimie (méthodes), Inclusion en paraffine (MeSH), Maladies pulmonaires (induit chimiquement), Maladies pulmonaires (métabolisme), Microscopie confocale (MeSH), Microscopie de fluorescence (méthodes), Oxydants photochimiques (pharmacologie), Oxydoréduction (MeSH), Oxygène (pharmacologie), Poumon (composition chimique), Poumon (effets des médicaments et des substances chimiques), Poumon (métabolisme), Protéine S (analyse), Protéine S (composition chimique), Protéine S (métabolisme), Souris (MeSH), Souris de lignée C57BL (MeSH).
- MESH :
- analyse : Glutathion, Protéine S.
- composition chimique : Poumon, Protéine S.
- effets des médicaments et des substances chimiques : Poumon.
- induit chimiquement : Maladies pulmonaires.
- métabolisme : Cystéine, Glutarédoxines, Glutathion, Maladies pulmonaires, Poumon, Protéine S.
- méthodes : Histocytochimie, Microscopie de fluorescence.
- pharmacologie : Dioxyde d'azote, Oxydants photochimiques, Oxygène.
- Animaux, Biocatalyse, Inclusion en paraffine, Microscopie confocale, Oxydoréduction, Souris, Souris de lignée C57BL.
English descriptors
- KwdEn :
- Animals (MeSH), Biocatalysis (MeSH), Cysteine (metabolism), Glutaredoxins (metabolism), Glutathione (analysis), Glutathione (metabolism), Histocytochemistry (methods), Lung (chemistry), Lung (drug effects), Lung (metabolism), Lung Diseases (chemically induced), Lung Diseases (metabolism), Mice (MeSH), Mice, Inbred C57BL (MeSH), Microscopy, Confocal (MeSH), Microscopy, Fluorescence (methods), Nitrogen Dioxide (pharmacology), Oxidants, Photochemical (pharmacology), Oxidation-Reduction (MeSH), Oxygen (pharmacology), Paraffin Embedding (MeSH), Protein S (analysis), Protein S (chemistry), Protein S (metabolism).
- MESH :
- chemical , analysis : Glutathione, Protein S.
- chemical , chemistry : Protein S.
- chemical , metabolism : Cysteine, Glutaredoxins, Glutathione, Protein S.
- chemically induced : Lung Diseases.
- chemistry : Lung.
- drug effects : Lung.
- metabolism : Lung, Lung Diseases.
- methods : Histocytochemistry, Microscopy, Fluorescence.
- chemical , pharmacology : Nitrogen Dioxide, Oxidants, Photochemical, Oxygen.
- Animals, Biocatalysis, Mice, Mice, Inbred C57BL, Microscopy, Confocal, Oxidation-Reduction, Paraffin Embedding.
Abstract
Protein S-glutathionylation (PSSG) is a posttranslational modification that involves the conjugation of the small antioxidant molecule glutathione to cysteine residues and is emerging as a critical mechanism of redox-based signaling. PSSG levels increase under conditions of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions, preferentially deglutathionylate cysteines and restore sulfhydryls. Both the occurrence and distribution of PSSG in tissues is unknown because of the labile nature of this oxidative event and the lack of specific reagents. The goal of this study was to establish and validate a protocol that enables detection of PSSG in situ, using the property of Grx to deglutathionylate cysteines. Using Grx1-catalyzed cysteine derivatization, we evaluated PSSG content in mice subjected to various models of lung injury and fibrosis. In control mice, PSSG was detectable primarily in the airway epithelium and alveolar macrophages. Exposure of mice to NO(2) resulted in enhanced PSSG levels in parenchymal regions, while exposure to O(2) resulted in minor detectable changes. Finally, bleomycin exposure resulted in marked increases in PSSG reactivity both in the bronchial epithelium as well as in parenchymal regions. Taken together, these findings demonstrate that Grx1-based cysteine derivatization is a powerful technique to specifically detect patterns of PSSG expression in lungs, and will enable investigations into regional changes in PSSG content in a variety of diseases.
DOI: 10.2353/ajpath.2009.080736
PubMed: 19556513
PubMed Central: PMC2708792
Affiliations:
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(pharmacology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxygen (pharmacology)</term><term>Paraffin Embedding (MeSH)</term><term>Protein S (analysis)</term><term>Protein S (chemistry)</term><term>Protein S (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Biocatalyse (MeSH)</term><term>Cystéine (métabolisme)</term><term>Dioxyde d'azote (pharmacologie)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (analyse)</term><term>Glutathion (métabolisme)</term><term>Histocytochimie (méthodes)</term><term>Inclusion en paraffine (MeSH)</term><term>Maladies pulmonaires (induit chimiquement)</term><term>Maladies pulmonaires (métabolisme)</term><term>Microscopie confocale (MeSH)</term><term>Microscopie de fluorescence (méthodes)</term><term>Oxydants photochimiques (pharmacologie)</term><term>Oxydoréduction (MeSH)</term><term>Oxygène (pharmacologie)</term><term>Poumon (composition chimique)</term><term>Poumon (effets des médicaments et des substances chimiques)</term><term>Poumon (métabolisme)</term><term>Protéine S (analyse)</term><term>Protéine S (composition chimique)</term><term>Protéine S (métabolisme)</term><term>Souris (MeSH)</term><term>Souris de lignée C57BL (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Glutathione</term><term>Protein S</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Protein S</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione</term><term>Protein S</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glutathion</term><term>Protéine S</term></keywords><keywords scheme="MESH" qualifier="chemically induced" xml:lang="en"><term>Lung Diseases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Poumon</term><term>Protéine S</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Poumon</term></keywords><keywords scheme="MESH" qualifier="induit chimiquement" xml:lang="fr"><term>Maladies pulmonaires</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lung</term><term>Lung Diseases</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Histocytochemistry</term><term>Microscopy, Fluorescence</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term><term>Glutarédoxines</term><term>Glutathion</term><term>Maladies pulmonaires</term><term>Poumon</term><term>Protéine S</term></keywords><keywords scheme="MESH" 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xml:lang="en">Protein S-glutathionylation (PSSG) is a posttranslational modification that involves the conjugation of the small antioxidant molecule glutathione to cysteine residues and is emerging as a critical mechanism of redox-based signaling. PSSG levels increase under conditions of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions, preferentially deglutathionylate cysteines and restore sulfhydryls. Both the occurrence and distribution of PSSG in tissues is unknown because of the labile nature of this oxidative event and the lack of specific reagents. The goal of this study was to establish and validate a protocol that enables detection of PSSG in situ, using the property of Grx to deglutathionylate cysteines. Using Grx1-catalyzed cysteine derivatization, we evaluated PSSG content in mice subjected to various models of lung injury and fibrosis. In control mice, PSSG was detectable primarily in the airway epithelium and alveolar macrophages. Exposure of mice to NO(2) resulted in enhanced PSSG levels in parenchymal regions, while exposure to O(2) resulted in minor detectable changes. Finally, bleomycin exposure resulted in marked increases in PSSG reactivity both in the bronchial epithelium as well as in parenchymal regions. Taken together, these findings demonstrate that Grx1-based cysteine derivatization is a powerful technique to specifically detect patterns of PSSG expression in lungs, and will enable investigations into regional changes in PSSG content in a variety of diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19556513</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1525-2191</ISSN><JournalIssue CitedMedium="Internet"><Volume>175</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>Jul</Month></PubDate></JournalIssue><Title>The American journal of pathology</Title><ISOAbbreviation>Am J Pathol</ISOAbbreviation></Journal><ArticleTitle>In situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization.</ArticleTitle><Pagination><MedlinePgn>36-45</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.2353/ajpath.2009.080736</ELocationID><Abstract><AbstractText>Protein S-glutathionylation (PSSG) is a posttranslational modification that involves the conjugation of the small antioxidant molecule glutathione to cysteine residues and is emerging as a critical mechanism of redox-based signaling. PSSG levels increase under conditions of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions, preferentially deglutathionylate cysteines and restore sulfhydryls. Both the occurrence and distribution of PSSG in tissues is unknown because of the labile nature of this oxidative event and the lack of specific reagents. The goal of this study was to establish and validate a protocol that enables detection of PSSG in situ, using the property of Grx to deglutathionylate cysteines. Using Grx1-catalyzed cysteine derivatization, we evaluated PSSG content in mice subjected to various models of lung injury and fibrosis. In control mice, PSSG was detectable primarily in the airway epithelium and alveolar macrophages. Exposure of mice to NO(2) resulted in enhanced PSSG levels in parenchymal regions, while exposure to O(2) resulted in minor detectable changes. Finally, bleomycin exposure resulted in marked increases in PSSG reactivity both in the bronchial epithelium as well as in parenchymal regions. Taken together, these findings demonstrate that Grx1-based cysteine derivatization is a powerful technique to specifically detect patterns of PSSG expression in lungs, and will enable investigations into regional changes in PSSG content in a variety of diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aesif</LastName><ForeName>Scott W</ForeName><Initials>SW</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></Author><Author ValidYN="Y"><LastName>Havermans</LastName><ForeName>Marije</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Guala</LastName><ForeName>Amy S</ForeName><Initials>AS</Initials></Author><Author ValidYN="Y"><LastName>Ckless</LastName><ForeName>Karina</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Taatjes</LastName><ForeName>Douglas J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Janssen-Heininger</LastName><ForeName>Yvonne M W</ForeName><Initials>YM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R03 HL 095404</GrantID><Acronym>HL</Acronym><Agency>NHLBI 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 HL60014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL079331</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R03 HL095404</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01HL079331</GrantID><Acronym>HL</Acronym><Agency>NHLBI 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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Am J Pathol</MedlineTA><NlmUniqueID>0370502</NlmUniqueID><ISSNLinking>0002-9440</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010083">Oxidants, Photochemical</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017293">Protein S</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>S7G510RUBH</RegistryNumber><NameOfSubstance UI="D009585">Nitrogen Dioxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>AIM</CitationSubset><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006651" MajorTopicYN="N">Histocytochemistry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008171" MajorTopicYN="N">Lung Diseases</DescriptorName><QualifierName UI="Q000139" MajorTopicYN="N">chemically induced</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="D018613" MajorTopicYN="N">Microscopy, Confocal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009585" MajorTopicYN="N">Nitrogen Dioxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010083" MajorTopicYN="N">Oxidants, Photochemical</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016612" MajorTopicYN="N">Paraffin Embedding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017293" MajorTopicYN="N">Protein S</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>6</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Aug;35(8):1000-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15297967</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Vermont</li></region></list><tree><noCountry><name sortKey="Anathy, Vikas" sort="Anathy, Vikas" uniqKey="Anathy V" first="Vikas" last="Anathy">Vikas Anathy</name><name sortKey="Ckless, Karina" sort="Ckless, Karina" uniqKey="Ckless K" first="Karina" last="Ckless">Karina Ckless</name><name sortKey="Guala, Amy S" sort="Guala, Amy S" uniqKey="Guala A" first="Amy S" last="Guala">Amy S. Guala</name><name sortKey="Havermans, Marije" sort="Havermans, Marije" uniqKey="Havermans M" first="Marije" last="Havermans">Marije Havermans</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="Taatjes, Douglas J" sort="Taatjes, Douglas J" uniqKey="Taatjes D" first="Douglas J" last="Taatjes">Douglas J. Taatjes</name></noCountry><country name="États-Unis"><region name="Vermont"><name sortKey="Aesif, Scott W" sort="Aesif, Scott W" uniqKey="Aesif S" first="Scott W" last="Aesif">Scott W. Aesif</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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