Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ.
Identifieur interne : 000A03 ( Main/Exploration ); précédent : 000A02; suivant : 000A04Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ.
Auteurs : Scott W. Aesif [États-Unis] ; Yvonne M W. Janssen-Heininger ; Niki L. ReynaertSource :
- Methods in enzymology [ 1557-7988 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- analyse : S-Nitroso-glutathion, S-Nitrosothiols.
- composition chimique : S-Nitroso-glutathion, S-Nitrosothiols.
- cytologie : Poumon.
- Animaux, Glutathion, Techniques de préparation histocytologique.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : S-Nitrosoglutathione, S-Nitrosothiols.
- chemical , chemistry : S-Nitrosoglutathione, S-Nitrosothiols.
- chemical : Glutathione.
- cytology : Lung.
- Animals, Histocytological Preparation Techniques.
Abstract
The oxidation of protein cysteine residues represents significant posttranslational modifications that impact a wide variety of signal transduction cascades and diverse biological processes. Oxidation of cysteines occurs through reactions with reactive oxygen as well as nitrogen species. These oxidative events can lead to irreversible modifications, such as the formation of sulfonic acids, or manifest as reversible modifications such as the conjugation of glutathione with the cysteine moiety, a process termed S-glutathionylation (also referred to as S-glutathiolation, or protein mixed disulfides). Similarly, S-nitrosothiols can also react with the thiol group in a process known as S-nitrosylation (or S-nitrosation). It is the latter two events that have recently come to the forefront of cellular biology through their ability to reversibly impact numerous cellular processes. Herein we describe two protocols for the detection of S-glutathionylated or S-nitrosylated proteins in situ. The protocol for the detection of S-glutathionylated proteins relies on the catalytic specificity of glutaredoxin-1 for the reduction of S-glutathionylated proteins. The protocol for the detection of S-nitrosylated proteins represents a modification of the previously described biotin switch protocol, which relies on ascorbate in the presence of chelators to decompose S-nitrosylated proteins. These techniques can be applied in situ to elucidate which compartments in tissues are affected in diseased states whose underlying pathologies are thought to represent a redox imbalance.
DOI: 10.1016/S0076-6879(10)74017-9
PubMed: 20609917
PubMed Central: PMC3113509
Affiliations:
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Janssen-Heininger</name></author><author><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20609917</idno><idno type="pmid">20609917</idno><idno type="doi">10.1016/S0076-6879(10)74017-9</idno><idno type="pmc">PMC3113509</idno><idno type="wicri:Area/Main/Corpus">000993</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000993</idno><idno type="wicri:Area/Main/Curation">000993</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000993</idno><idno type="wicri:Area/Main/Exploration">000993</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ.</title><author><name sortKey="Aesif, Scott W" sort="Aesif, Scott W" uniqKey="Aesif S" first="Scott W" last="Aesif">Scott W. Aesif</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pathology, University of Vermont College of Medicine, Burlington, Vermont, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, University of Vermont College of Medicine, Burlington, Vermont</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></author><author><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</name></author></analytic><series><title level="j">Methods in enzymology</title><idno type="eISSN">1557-7988</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Glutathione (MeSH)</term><term>Histocytological Preparation Techniques (MeSH)</term><term>Lung (cytology)</term><term>S-Nitrosoglutathione (analysis)</term><term>S-Nitrosoglutathione (chemistry)</term><term>S-Nitrosothiols (analysis)</term><term>S-Nitrosothiols (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Glutathion (MeSH)</term><term>Poumon (cytologie)</term><term>S-Nitroso-glutathion (analyse)</term><term>S-Nitroso-glutathion (composition chimique)</term><term>S-Nitrosothiols (analyse)</term><term>S-Nitrosothiols (composition chimique)</term><term>Techniques de préparation histocytologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>S-Nitrosoglutathione</term><term>S-Nitrosothiols</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>S-Nitrosoglutathione</term><term>S-Nitrosothiols</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutathione</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>S-Nitroso-glutathion</term><term>S-Nitrosothiols</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>S-Nitroso-glutathion</term><term>S-Nitrosothiols</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Poumon</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Histocytological Preparation Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glutathion</term><term>Techniques de préparation histocytologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The oxidation of protein cysteine residues represents significant posttranslational modifications that impact a wide variety of signal transduction cascades and diverse biological processes. Oxidation of cysteines occurs through reactions with reactive oxygen as well as nitrogen species. These oxidative events can lead to irreversible modifications, such as the formation of sulfonic acids, or manifest as reversible modifications such as the conjugation of glutathione with the cysteine moiety, a process termed S-glutathionylation (also referred to as S-glutathiolation, or protein mixed disulfides). Similarly, S-nitrosothiols can also react with the thiol group in a process known as S-nitrosylation (or S-nitrosation). It is the latter two events that have recently come to the forefront of cellular biology through their ability to reversibly impact numerous cellular processes. Herein we describe two protocols for the detection of S-glutathionylated or S-nitrosylated proteins in situ. The protocol for the detection of S-glutathionylated proteins relies on the catalytic specificity of glutaredoxin-1 for the reduction of S-glutathionylated proteins. The protocol for the detection of S-nitrosylated proteins represents a modification of the previously described biotin switch protocol, which relies on ascorbate in the presence of chelators to decompose S-nitrosylated proteins. These techniques can be applied in situ to elucidate which compartments in tissues are affected in diseased states whose underlying pathologies are thought to represent a redox imbalance.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20609917</PMID><DateCompleted><Year>2010</Year><Month>10</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7988</ISSN><JournalIssue CitedMedium="Internet"><Volume>474</Volume><PubDate><Year>2010</Year></PubDate></JournalIssue><Title>Methods in enzymology</Title><ISOAbbreviation>Methods Enzymol</ISOAbbreviation></Journal><ArticleTitle>Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ.</ArticleTitle><Pagination><MedlinePgn>289-96</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/S0076-6879(10)74017-9</ELocationID><Abstract><AbstractText>The oxidation of protein cysteine residues represents significant posttranslational modifications that impact a wide variety of signal transduction cascades and diverse biological processes. Oxidation of cysteines occurs through reactions with reactive oxygen as well as nitrogen species. These oxidative events can lead to irreversible modifications, such as the formation of sulfonic acids, or manifest as reversible modifications such as the conjugation of glutathione with the cysteine moiety, a process termed S-glutathionylation (also referred to as S-glutathiolation, or protein mixed disulfides). Similarly, S-nitrosothiols can also react with the thiol group in a process known as S-nitrosylation (or S-nitrosation). It is the latter two events that have recently come to the forefront of cellular biology through their ability to reversibly impact numerous cellular processes. Herein we describe two protocols for the detection of S-glutathionylated or S-nitrosylated proteins in situ. The protocol for the detection of S-glutathionylated proteins relies on the catalytic specificity of glutaredoxin-1 for the reduction of S-glutathionylated proteins. The protocol for the detection of S-nitrosylated proteins represents a modification of the previously described biotin switch protocol, which relies on ascorbate in the presence of chelators to decompose S-nitrosylated proteins. These techniques can be applied in situ to elucidate which compartments in tissues are affected in diseased states whose underlying pathologies are thought to represent a redox imbalance.</AbstractText><CopyrightInformation>Copyright (c) 2010 Elsevier Inc. All rights reserved.</CopyrightInformation></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, Vermont, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Janssen-Heininger</LastName><ForeName>Yvonne M W</ForeName><Initials>YM</Initials></Author><Author ValidYN="Y"><LastName>Reynaert</LastName><ForeName>Niki L</ForeName><Initials>NL</Initials></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>R01 HL060014-13</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></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>06</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Methods Enzymol</MedlineTA><NlmUniqueID>0212271</NlmUniqueID><ISSNLinking>0076-6879</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026403">S-Nitrosothiols</NameOfSubstance></Chemical><Chemical><RegistryNumber>57564-91-7</RegistryNumber><NameOfSubstance UI="D026422">S-Nitrosoglutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="Y">Glutathione</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016591" MajorTopicYN="Y">Histocytological Preparation Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026422" MajorTopicYN="N">S-Nitrosoglutathione</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026403" MajorTopicYN="N">S-Nitrosothiols</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000737" 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Janssen-Heininger</name><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</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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