{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363388846207160704.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.0404762101"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.0404762101"}}],"dc:title":[{"@value":"Widespread sulfenic acid formation in tissues in response to hydrogen peroxide"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>A principal product of the reaction between a protein cysteinyl thiol and hydrogen peroxide is a protein sulfenic acid. Because protein sulfenic acid formation is reversible, it provides a mechanism whereby changes in cellular hydrogen peroxide concentration may directly control protein function. We have developed methods for the detection and purification of proteins oxidized in this way. The methodology is based on the arsenite-specific reduction of protein sulfenic acid under denaturing conditions and their subsequent labeling with biotin–maleimide. Arsenite-dependent signal generation was fully blocked by pretreatment with dimedone, consistent with its reactivity with sulfenic acids to form a covalent adduct that is nonreducible by thiols. The biotin tag facilitates the detection of protein sulfenic acids on Western blots probed with streptavidin–horseradish peroxidase and also their purification by streptavidin–agarose. We have characterized protein sulfenic acid formation in isolated hearts subjected to hydrogen peroxide treatment. We have also purified and identified a number of the proteins that are oxidized in this way by using a proteomic approach. Using Western immunoblotting we demonstrated that a highly significant proportion of some individual proteins (68% of total in one case) form the sulfenic derivative. We conclude that protein sulfenic acids are widespread physiologically relevant posttranslational oxidative modifications that can be detected at basal levels in healthy tissue, and are elevated in response to hydrogen peroxide. These approaches may find widespread utility in the study of oxidative stress, particularly because hydrogen peroxide is used extensively in models of disease or redox signaling.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380294662961205120","@type":"Researcher","foaf:name":[{"@value":"Adrian T. Saurin"}],"jpcoar:affiliationName":[{"@value":"Department of Cardiology, Cardiovascular Division, The Rayne Institute, St. Thomas' Hospital, King's College London, London SE1 7EH, United Kingdom; and Drug Control Centre/Mass Spectrometry Facility, King's College London, 150 Stamford Street, London SE1 9NN, United Kingdom"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294662961205121","@type":"Researcher","foaf:name":[{"@value":"Hendrik Neubert"}],"jpcoar:affiliationName":[{"@value":"Department of Cardiology, Cardiovascular Division, The Rayne Institute, St. Thomas' Hospital, King's College London, London SE1 7EH, United Kingdom; and Drug Control Centre/Mass Spectrometry Facility, King's College London, 150 Stamford Street, London SE1 9NN, United Kingdom"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294662961205122","@type":"Researcher","foaf:name":[{"@value":"Jonathan P. Brennan"}],"jpcoar:affiliationName":[{"@value":"Department of Cardiology, Cardiovascular Division, The Rayne Institute, St. Thomas' Hospital, King's College London, London SE1 7EH, United Kingdom; and Drug Control Centre/Mass Spectrometry Facility, King's College London, 150 Stamford Street, London SE1 9NN, United Kingdom"}]},{"@id":"https://cir.nii.ac.jp/crid/1380294662961205123","@type":"Researcher","foaf:name":[{"@value":"Philip Eaton"}],"jpcoar:affiliationName":[{"@value":"Department of Cardiology, Cardiovascular Division, The Rayne Institute, St. Thomas' Hospital, King's College London, London SE1 7EH, United Kingdom; and Drug Control Centre/Mass Spectrometry Facility, King's College London, 150 Stamford Street, London SE1 9NN, United Kingdom"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2004-12-16","prism:volume":"101","prism:number":"52","prism:startingPage":"17982","prism:endingPage":"17987"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.0404762101"}],"createdAt":"2004-12-16","modifiedAt":"2022-04-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002220510711296","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Localized cysteine sulfenic acid formation by vascular endothelial growth factor: role in endothelial cell migration and angiogenesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283693331688064","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"The origin and future of oxidative stress pathology: From the recognition of carcinogenesis as an iron addiction with ferroptosis‐resistance to non‐thermal plasma therapy"}]},{"@id":"https://cir.nii.ac.jp/crid/1360290617884547456","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Reductively modified albumin attenuates DSS-Induced mouse colitis through rebalancing systemic redox state"}]},{"@id":"https://cir.nii.ac.jp/crid/1360576118716221440","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Comprehensive analyses of the cysteine thiol oxidation of PKM2 reveal the effects of multiple oxidation on cellular oxidative stress response"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846643567758208","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"The Chemical Biology of Naphthoquinones and Its Environmental Implications"}]},{"@id":"https://cir.nii.ac.jp/crid/1360861705585101056","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"The Combined Administration of Vitamin C and Copper Induces a Systemic Oxidative Stress and Kidney Injury"}]},{"@id":"https://cir.nii.ac.jp/crid/1360861707380719104","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Development of Dietary Thiol Antioxidant via Reductive Modification of Whey Protein and Its Application in the Treatment of Ischemic Kidney Injury"}]},{"@id":"https://cir.nii.ac.jp/crid/1360865815694708608","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Gut bacteria exacerbates TNBS-induced colitis and kidney injury through oxidative stress"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1073/pnas.0404762101"},{"@type":"CROSSREF","@value":"10.3109/10715762.2011.602073_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1146/annurev-pharmtox-010611-134517_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1111/pin.12396_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1016/j.redox.2021.101881_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1042/bcj20200897_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1101/2020.05.14.097139_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.3390/biom13010143_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.3390/antiox12010193_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"},{"@type":"CROSSREF","@value":"10.1016/j.redox.2024.103140_references_DOI_L8FjkIjF4cKZOMF2WZVEeZ70C6d"}]}