The role of oxidative protein modification and the glutathione system in modulation of the redox status of breast epithelial cells

Abstract

The effects of N-ethylmaleimide (NEM) and 1,4-dithioerythritol (DTE) on the level of oxidative modification of proteins, the state of glutathione and thioredoxin systems and the cellular redox status have been investigated in HBL-100 cells (breast epithelial cells). Breast epithelial cells cultivated in the presence of NEM were characterized by the decreased redox status, increased glutathione reductase activity, and increased concentrations of products of irreversible oxidative modification of proteins and amino acids. Cell cultivation in the presence of DTE shifted the redox status towards reduction processes and increased reversible protein modification by glutathionylation. The proposed model of intracellular redox modulation may be used in the development of new therapeutic approaches to treat diseases accompanied by impaired redox homeostasis (e.g. oncologic, inflammatory, cardiovascular and neurodegenerative disease).