@prefix prodottidellaricerca: . @prefix istituto: . @prefix prodotto: . istituto:CDS021 prodottidellaricerca:prodotto prodotto:ID289430 . @prefix modulo: . modulo:ID2856 prodottidellaricerca:prodotto prodotto:ID289430 . @prefix pubblicazioni: . @prefix unitaDiPersonaleEsterno: . unitaDiPersonaleEsterno:ID6021 pubblicazioni:autoreCNRDi prodotto:ID289430 . @prefix rdf: . prodotto:ID289430 rdf:type prodotto:TIPO1101 . @prefix retescientifica: . prodotto:ID289430 rdf:type retescientifica:ProdottoDellaRicerca . @prefix rdfs: . prodotto:ID289430 rdfs:label "Inactivation of human salivary glutathione transferase p1-1 by hypothiocyanite: a post-translational control system in search of a role. (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID289430 pubblicazioni:anno "2014-01-01T00:00:00+01:00"^^xsd:gYear ; pubblicazioni:doi "10.1371/journal.pone.0112797"^^xsd:string . @prefix skos: . prodotto:ID289430 skos:altLabel "
Fabrini, Raffaele; Bocedi, Alessio; Camerini, Serena; Fusetti, Marco; Ottaviani, Fabrizio; Passali, Francesco M; Topazio, Davide; Iavarone, Federica; Francia, Irene; Castagnola, Massimo; Ricci, Giorgio (2014)
Inactivation of human salivary glutathione transferase p1-1 by hypothiocyanite: a post-translational control system in search of a role.
in PloS one
"^^rdf:HTML ; pubblicazioni:autori "Fabrini, Raffaele; Bocedi, Alessio; Camerini, Serena; Fusetti, Marco; Ottaviani, Fabrizio; Passali, Francesco M; Topazio, Davide; Iavarone, Federica; Francia, Irene; Castagnola, Massimo; Ricci, Giorgio"^^xsd:string ; pubblicazioni:paginaInizio "e112797"^^xsd:string ; pubblicazioni:numeroVolume "9"^^xsd:string . @prefix ns11: . prodotto:ID289430 pubblicazioni:rivista ns11:ID114232 ; pubblicazioni:numeroFascicolo "11"^^xsd:string ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:affiliazioni "CNR-ICRM"^^xsd:string ; pubblicazioni:titolo "Inactivation of human salivary glutathione transferase p1-1 by hypothiocyanite: a post-translational control system in search of a role."^^xsd:string ; prodottidellaricerca:abstract "Glutathione transferases (GSTs) are a superfamily of detoxifying enzymes over-expressed in tumor tissues and tentatively proposed as biomarkers for localizing and monitoring injury of specific tissues. Only scarce and contradictory reports exist about the presence and the level of these enzymes in human saliva. This study shows that GSTP1-1 is the most abundant salivary GST isoenzyme, mainly coming from salivary glands. Surprisingly, its activity is completely obscured by the presence of a strong oxidizing agent in saliva that causes a fast and complete, but reversible, inactivation. Although salivary alpha-defensins are also able to inhibit the enzyme causing a peculiar half-site inactivation, a number of approaches (mass spectrometry, site directed mutagenesis, chromatographic and spectrophotometric data) indicated that hypothiocyanite is the main salivary inhibitor of GSTP1-1. Cys47 and Cys101, the most reactive sulfhydryls of GSTP1-1, are mainly involved in a redox interaction which leads to the formation of an intra-chain disulfide bridge. A reactivation procedure has been optimized and used to quantify GSTP1-1 in saliva of 30 healthy subjects with results of 42\u00B14 mU/mg-protein. The present study represents a first indication that salivary GSTP1-1 may have a different and hitherto unknown function. In addition it fulfills the basis for future investigations finalized to check the salivary GSTP1-1 as a diagnostic biomarker for diseases." ; prodottidellaricerca:prodottoDi istituto:CDS021 , modulo:ID2856 ; pubblicazioni:autoreCNR unitaDiPersonaleEsterno:ID6021 . ns11:ID114232 pubblicazioni:rivistaDi prodotto:ID289430 .