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dc.creatorWedmann, Rudolf
dc.creatorOnderka, Constantin
dc.creatorWei, Shengwei
dc.creatorSzijarto, Istvan Andras
dc.creatorMiljkovic, Jan Lj
dc.creatorMitrović, Aleksandra D.
dc.creatorLange, Mike
dc.creatorSavitsky, Sergey
dc.creatorYadav, Pramod Kumar
dc.creatorTorregrossa, Roberta
dc.creatorHarrer, Ellen G.
dc.creatorHarrer, Thomas
dc.creatorIshii, Isao
dc.creatorGollasch, Maik
dc.creatorWood, Mark E.
dc.creatorGalardon, Erwan
dc.creatorXian, Ming
dc.creatorWhiteman, Matthew
dc.creatorBanerjee, Ruma
dc.creatorFilipovi, Milos R.
dc.date.accessioned2018-11-22T00:34:47Z
dc.date.available2018-11-22T00:34:47Z
dc.date.issued2016
dc.identifier.issn2041-6520
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1925
dc.description.abstractHydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system caused an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.en
dc.publisherRoyal Soc Chemistry, Cambridge
dc.relationMedical Research Council [MR/M022706/1]
dc.relationFrench State in the frame of the Investments for the future Programme IdEx Bordeaux [ANR-10-IDEX-03-02]
dc.relationDeutsche Forschungsgemeinschaft
dc.relationDr Werner Jackstadt-Stiftung
dc.relationAmerican Heart Association [14POST18760003]
dc.relationFriedrich-Alexander University within the Emerging Field Initiative (MRIC)
dc.relationBrian Ridge Scholarship
dc.relationNational Institutes of Health [HL58984, GM112455, NIH R01HL116571]
dc.rightsopenAccess
dc.sourceChemical Science
dc.titleImproved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidationen
dc.typearticle
dc.rights.licenseBY
dcterms.abstractXиан, Минг; Филипови, Милос Р.; Харрер, Тхомас; Голласцх, Маик; Исхии, Исао; Торрегросса, Роберта; Савитскy, Сергеy; Ланге, Мике; Миљковиц, Јан Љ; Харрер, Еллен Г.; Сзијарто, Истван Aндрас; Wеи, Схенгwеи; Ондерка, Цонстантин; Wедманн, Рудолф; Митровић, Aлександра; Yадав, Прамод Кумар; Wоод, Марк Е.; Галардон, Ерwан; Wхитеман, Маттхеw; Банерјее, Рума;
dc.citation.volume7
dc.citation.issue5
dc.citation.spage3414
dc.citation.epage3426
dc.identifier.wos000374859300056
dc.identifier.doi10.1039/c5sc04818d
dc.citation.other7(5): 3414-3426
dc.citation.rankM21
dc.identifier.pmid27170841
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-84966356269
dc.identifier.rcubKon_3044


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