6533b82efe1ef96bd1292991
RESEARCH PRODUCT
Oxidative post‐translational modifications in histones
Carlos Romá-mateoCarlos Romá-mateoFederico V. PallardóFederico V. PallardóJosé Luis García-jiménezJosé Luis García-giménezsubject
0301 basic medicineProtein CarbonylationClinical BiochemistryOxidative phosphorylationmedicine.disease_causeBiochemistryEpigenesis GeneticHistonesProtein CarbonylationMice03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansEpigeneticsEpigenesisSulfur CompoundsbiologyChemistryNitrosylationGeneral MedicineGlutathioneReactive Nitrogen SpeciesCell biologyOxidative Stress030104 developmental biologyHistone030220 oncology & carcinogenesisbiology.proteinMolecular MedicineSignal transductionReactive Oxygen SpeciesOxidation-ReductionProtein Processing Post-TranslationalOxidative stressNitroso CompoundsSignal Transductiondescription
Epigenetic regulation is attracting much attention because it explains many of the effects that the external environment induces in organisms. Changes in the cellular redox status and even more specifically in its nuclear redox compartment is one of these examples. Redox changes can induce modulation of the epigenetic regulation in cells. Here we present a few cases where reactive oxygen or nitrogen species induces epigenetic marks in histones. Posttranslational modification of these proteins like histone nitrosylation, carbonylation, or glutathionylation together with other mechanisms not reviewed here are the cornerstones of redox-related epigenetic regulation. We currently face a new field of research with potential important consequences for the treatment of many pathologies.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-06-11 | BioFactors |