A proteomics method to detect acrolein adduction: effects on redox proteins in vitro

摘要

A wide variety of proteins were found to be adducted by acrolein in HBE1 cells in vitro, including proteins that are critical in regulation of cellular redox homeostasis, such as peroxiredoxins, glutathione S-transferase pi, and thioredoxin reductase. Adduction of acrolein to TrxR occurred specifically at the highly nucleophilic selenocysteine residue which is critical for Trx reductase activity and regulation of many redox-sensitive proteins. Changes in enzymatic activity of TrxR by acrolein adduction may contribute to the functional consequences of acrolein exposure to airway epithelial cells. Future studies will characterize the location of acrolein adducts on other redox proteins identified in the first part of this study and determine if acrolein adduction alters enzyme activity.