Thioredoxin and redox regulation of the nuclear receptor.

Abstract

AbstractOxidative stress evokes various cellular responses including alteration of gene expression to preserve cellular homeostasis (1,2). Thioredoxin (TRX) is a small ubiquitous protein with protein thiol-reducing activity and has been shown to function as a cellular antioxidant buffering system in response to oxidative stress and play essential roles in maintenance of cellular function (3,4). Recently, a growing number of evidence has shown that TRX plays crucial roles in redox regulation of gene expression via either direct or indirect interaction with various transcription factors including NF-κB (5), AP-1 (6), and PEBP2 (7). Alteration in expression and/or subcellular localization of TRX has been indicated to be involved in such redox-dependent control of the transcription factors (8,9), however, precise mechanisms remain unknown.KeywordsGlucocorticoid ReceptorNuclear ReceptorRedox RegulationCellular Redox StateTsukuba Science CityThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.