Oxidative Modification of Redox Proteins: Role in the Regulation of HBL-100 Cell Proliferation
- Authors: Shakhristova E.V.1, Stepovaya E.A.1, Rudikov E.V.1, Novitskii V.V.1
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Affiliations:
- Siberian State Medical University, Ministry of Health of the Russian Federation
- Issue: Vol 167, No 1 (2019)
- Pages: 30-34
- Section: Biophysics and Biochemistry
- URL: https://journals.rcsi.science/0007-4888/article/view/241419
- DOI: https://doi.org/10.1007/s10517-019-04453-9
- ID: 241419
Cite item
Abstract
HBL-100 breast epithelial cells were cultured with a blocker (N-ethylmaleimide) and protector (1,4-dithioerythritol) of SH groups. The study assessed changes in redox potential of glutathione and thioredoxin systems, intensity of oxidative modification of proteins, ROS production, and cell proliferation. The roles of thioredoxin system and protein oxidative modification in HBL-100 cell proliferation under redox status modulation were established. The role of carbonylated thioredoxin in arrest of the cell cycle in S-phase was demonstrated, which could be used for targeted therapy of the diseases accompanied by oxidative stress and disturbed redox status.
About the authors
E. V. Shakhristova
Siberian State Medical University, Ministry of Health of the Russian Federation
Author for correspondence.
Email: shaxristova@yandex.ru
Russian Federation, Tomsk
E. A. Stepovaya
Siberian State Medical University, Ministry of Health of the Russian Federation
Email: shaxristova@yandex.ru
Russian Federation, Tomsk
E. V. Rudikov
Siberian State Medical University, Ministry of Health of the Russian Federation
Email: shaxristova@yandex.ru
Russian Federation, Tomsk
V. V. Novitskii
Siberian State Medical University, Ministry of Health of the Russian Federation
Email: shaxristova@yandex.ru
Russian Federation, Tomsk