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

   


1. Siberian State Medical University, Tomsk, Russia
2. Siberian Federal University, Krasnoyarsk, Russia; Voino-Yasenetsky Krasnoyarsk State Medical University, Krasnoyarsk, Russia
Type: Experimental study
DOI: 10.18097/PBMC20166201064      UDK: 577.121.7:542.943-092'78:618.19      PubMed Id: 26973189
Year: 2016 vol: 62  issue:1  pages: 64-68
Abstract: The effects of the SH-group blocker N-ethylmaleimide (NEM) and thiol group protector 1,4-dithioerythritol (DTE) on the redox status of cells HBL-100 cells, oxidative modification of their proteins and the state of glutathione and thioredoxin systems have been investigated. Breast epithelial cells cultivated in the presence of NEM were characterized by decreased redox status, increased glutathione reductase activity, and increased concentrations of products of irreversible oxidative modification of protein and amino acids. Cultivation of HBL-100 cells in the presence of DTE resulted in a shift of 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).
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Reference: Stepovaya E.A., Shakhristova E.V., Ryazantseva N.V., Nosareva O.L., Yakushina V.D., Nosova A.I., Gulaya V.S., Stepanova E.A., Chil'chigashev R.I., Novitsky V.V., The role of oxidative protein modification and the gluthatione system in modulation of the redox status of breast epithelial cells, Biomeditsinskaya khimiya, 2016, vol: 62(1), 64-68.
This paper is also available as the English translation:10.1134/S1990750816030161
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