Key result
Acute pancreatitis is characterized by disulfide stress and thiol oxidation in proteins, particularly protein cysteinylation, without significant changes in the glutathione redox status.
This review highlights the role of reversible oxidation of protein cysteines and disulfide stress in the progression of severe acute pancreatitis.
Protein thiol oxidation may mark severe acute pancreatitis progression; leaves open cysteine-targeted interventions pending prospective trials.
Under physiological conditions, the balance between ROS production and removal properly maintains the intracellular redox-sensitive signaling as well as the appropriate status of protein thiols and disulfides. However, inflammation among other factors can modify this balance causing a rapid increase in intracellular ROS levels and hence thiol oxidation, eventually leading to oxidative stress. In the case of acute pancreatitis, both redox signaling and oxidative stress seem to contribute to the progression of the severe form of the disease. In this review we will focus on the reversible oxidation of protein cysteines during the course of acute pancreatitis. We describe disulfide stress in an acute inflammatory process, which is characterized by thiol oxidation in proteins, particularly protein cysteinylation, without significant changes in the glutathione redox status.
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Moreno et al. (2015) conducted a review in Acute pancreatitis. Disulfide stress and reversible oxidation of protein cysteines was evaluated. Acute pancreatitis is characterized by disulfide stress and thiol oxidation in proteins, particularly protein cysteinylation, without significant changes in the glutathione redox status.
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