Ligand/receptor stimulation of cells promotes protein carbonylation that is followed by the decarbonylation process,which might involve thiol-dependent reduction(C.M.Wongetal.,Circ.Res.102:301–318;2008). This study furthe rinvestigated the properties of this proteinde carbonylation mechanism.We found that the thiol-mediated reduction o fprotein carbonylsis dependent on heat-labile biologic components. Cysteine and glutathione were efficient substrates for decarbonylation.Thiolsdecreasedtheproteincarbonylcontent, asdetectedby2,4-dinitrophenylhydrazine,butnotthe levelsofmalondialdehyde or4-hydroxynonenal proteinadducts.Massspectrometryidentified proteinsthatundergothiol-dependentdecarbonylation, whichincludeperoxiredoxins.Peroxiredoxin-2and-6werecarbonylatedandsubsequentlydecarbonylated in responsetotheligand/receptorstimulationofcells.siRNAknockdownofglutaredoxininhibitedthe decarbonylationofperoxiredoxin.Theseresultsstrengthen theconceptthatthiol-dependent decarbonylation definesthekineticsofproteincarbonylationsignaling.
Mechanism of protein decarbonylation / Wong, Cm; Marcocci, Lucia; Das, D; Wang, X; Luo, H; Zungu Edmondson, M; Suzuki, Yj. - In: FREE RADICAL BIOLOGY & MEDICINE. - ISSN 0891-5849. - STAMPA. - 65:(2013), pp. 1126-1133. [10.1016/j.freeradbiomed.2013.09.005]
Mechanism of protein decarbonylation
MARCOCCI, Lucia;
2013
Abstract
Ligand/receptor stimulation of cells promotes protein carbonylation that is followed by the decarbonylation process,which might involve thiol-dependent reduction(C.M.Wongetal.,Circ.Res.102:301–318;2008). This study furthe rinvestigated the properties of this proteinde carbonylation mechanism.We found that the thiol-mediated reduction o fprotein carbonylsis dependent on heat-labile biologic components. Cysteine and glutathione were efficient substrates for decarbonylation.Thiolsdecreasedtheproteincarbonylcontent, asdetectedby2,4-dinitrophenylhydrazine,butnotthe levelsofmalondialdehyde or4-hydroxynonenal proteinadducts.Massspectrometryidentified proteinsthatundergothiol-dependentdecarbonylation, whichincludeperoxiredoxins.Peroxiredoxin-2and-6werecarbonylatedandsubsequentlydecarbonylated in responsetotheligand/receptorstimulationofcells.siRNAknockdownofglutaredoxininhibitedthe decarbonylationofperoxiredoxin.Theseresultsstrengthen theconceptthatthiol-dependent decarbonylation definesthekineticsofproteincarbonylationsignaling.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
