Thiol redox transitions by thioredoxin and thioredoxin-binding protein-2 in cell signaling.

摘要: The cellular thiol redox state is a crucial mediator of metabolic, signaling and transcriptional processes in cells, an exquisite balance between the oxidizing reducing states essential for normal function survival cells. Reactive oxygen species (ROS) are widely known to as kind second messenger intracellular modulate state. Thiol reduction mainly controlled by thioredoxin (TRX) system glutathione (GSH) systems scavengers ROS regulators protein states. composed several related molecules interacting through cysteine residues at active site, including thioredoxin, thioredoxin-2, mitochondrial family, transmembrane thioredoxin-related (TMX), endoplasmic reticulum (ER)-specific family. Thioredoxin couples with thioredoxin-dependent peroxidases (peroxiredoxin) scavenge hydrogen peroxide. In addition, does not simply act only scavenger but also important regulator oxidative stress response protein-protein interaction. interaction thioredoxin-binding proteins such protein-2 (TBP-2, called Txnip or VDUP1), apoptosis signal kinase (ASK-1), factor 1 (Ref-1), Forkhead box class O 4 (FoxO4), nod-like receptor (NLRPs) suggested unconventional functions novel mechanism regulation. Here, we introduce central transition cell regulated molecules.