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).
Issledovali uroven' okislitel'noĭ modifikatsii belkov, sostoianie sistemy glutationa i tioredoksina v usloviiakh moduliatsii redoks-statusa épitelial'nykh kletok molochnoĭ zhelezy linii HBL-100 s pomoshch'iu N-étilmaleimida i 1,4-ditioéritritola. Pri kul'tivirovanii kletok v prisutstvii N-étilmaleimida proiskhodit snizhenie ikh redoks-statusa, uvelichenie aktivnosti glutationreduktazy i povyshenie kontsentratsii produktov neobratimoĭ okislitel'noĭ modifikatsii belkov i aminokislot. Dobavlenie v kul'tural'nuiu sredu protektora SH-grupp sposobstvovalo smeshcheniiu redoks-statusa v storonu vosstanovitel'nykh protsessov i vozrastaniiu obratimoĭ modifikatsii proteinov s pomoshch'iu glutationilirovaniia. Predlozhennaia model' vnutrikletochnoĭ redoks-moduliatsii mozhet byt' ispol'zovana pri razrabotke novykh terapevticheskikh podkhodov dlia lecheniia zabolevaniĭ, soprovozhdaiushchikhsia narusheniem redoks-gomeostaza (onkologicheskikh, vospalitel'nykh, serdechno-sosudistykh, neĭro-degenerativnykh i dr.).
Keywords: breast epithelial cells; cell redox status; oxidative stress; protein oxidative modification.